ID ACKA_MYCPN Reviewed; 390 AA. AC P75245; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 98. DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=MPN_533; ORFNames=MP309; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260816, EBI-2260816; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95957.1; -; Genomic_DNA. DR PIR; S73635; S73635. DR RefSeq; NP_110222.1; NC_000912.1. DR RefSeq; WP_010874890.1; NC_000912.1. DR ProteinModelPortal; P75245; -. DR IntAct; P75245; 1. DR EnsemblBacteria; AAB95957; AAB95957; MPN_533. DR GeneID; 877249; -. DR KEGG; mpn:MPN533; -. DR PATRIC; 20022541; VBIMycPne110_0594. DR KO; K00925; -. DR OMA; ISIFEIQ; -. DR OrthoDB; EOG69975F; -. DR BioCyc; MetaCyc:MONOMER-603; -. DR BioCyc; MPNE272634:GJ6Z-578-MONOMER; -. DR BRENDA; 2.7.2.1; 3534. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 390 Acetate kinase. FT /FTId=PRO_0000107588. FT NP_BIND 204 208 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 278 280 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 323 327 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 376 376 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 237 237 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. SQ SEQUENCE 390 AA; 43700 MW; 6E24F005205AE5E4 CRC64; MNDNKILVVN AGSSSIKFQL FDYHKKVLAK ALCERIFVDG FFKLEFNEQK VEEKVAFPDH HAAVTHFLNT LKKHKIIQEL SDIILVGHRV VQGANYFKDS VIVDAEALAK IKEFIKLAPL HNKPEADVIE IFFKEVPSAK NVAVFDTTFH TTIPQENYLY AVPRSWEQKH LVRRYGFHGT SYKFINNYLE KHLNKQNLNL IVCHLGNGAS VCAIKNGKSF NTSMGFTPLE GLIMGTRSGD LDPAIIGYVA EQENMSASDV VNALNKKSGM LALTGASDMR DVFAKPQENA VAIKMYVNRV ADYIAKYLNQ LEGNIDGLVF TGGIGENASD CVELFINAVK SLGFATDLKL FVKYGDSCVV STPQSKYKIY RVRTNEELMI VEDSIRLTQK // ID ACPH_MYCPN Reviewed; 84 AA. AC P75378; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Acyl carrier protein homolog; DE Short=ACP; GN OrderedLocusNames=MPN_406; ORFNames=MP432; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000250}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of the apo-ACP-like protein. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|PROSITE- CC ProRule:PRU00258}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96080.1; -; Genomic_DNA. DR PIR; S73758; S73758. DR RefSeq; NP_110094.1; NC_000912.1. DR RefSeq; WP_010874762.1; NC_000912.1. DR ProteinModelPortal; P75378; -. DR EnsemblBacteria; AAB96080; AAB96080; MPN_406. DR GeneID; 877357; -. DR KEGG; mpn:MPN406; -. DR PATRIC; 20022202; VBIMycPne110_0439. DR KO; K02078; -. DR OMA; FMEILSV; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; MPNE272634:GJ6Z-434-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1200.10; -; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; KW Phosphoprotein; Reference proteome. FT CHAIN 1 84 Acyl carrier protein homolog. FT /FTId=PRO_0000180266. FT MOD_RES 39 39 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|PROSITE-ProRule:PRU00258}. SQ SEQUENCE 84 AA; 9838 MW; B5F7C612AA50C1CB CRC64; MQERDILLKI KEIAKAKNFK TELDESVLQK PFRELKIDSL DMFSVIVSLE KEFDIMFEDE KLMQLNNLAE LIAEVKHLIS QKGV // ID ADH_MYCPN Reviewed; 351 AA. AC P75214; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Probable NADP-dependent isopropanol dehydrogenase; DE EC=1.1.1.80; GN Name=adh; OrderedLocusNames=MPN_564; ORFNames=MP278; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Alcohol dehydrogenase with a preference for medium chain CC secondary alcohols, such as 2-butanol and isopropanol. Has very CC low activity with primary alcohols, such as ethanol. Under CC physiological conditions, the enzyme reduces aldehydes and 2- CC ketones to produce secondary alcohols. Is also active with CC acetaldehyde and propionaldehyde (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Propan-2-ol + NADP(+) = acetone + NADPH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase 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; U00089; AAB95926.1; -; Genomic_DNA. DR PIR; S73604; S73604. DR RefSeq; NP_110253.1; NC_000912.1. DR RefSeq; WP_010874921.1; NC_000912.1. DR ProteinModelPortal; P75214; -. DR SMR; P75214; 1-351. DR IntAct; P75214; 1. DR EnsemblBacteria; AAB95926; AAB95926; MPN_564. DR GeneID; 876853; -. DR KEGG; mpn:MPN564; -. DR PATRIC; 20022607; VBIMycPne110_0626. DR OMA; GYQTSCV; -. DR OrthoDB; EOG6BGP28; -. DR BioCyc; MPNE272634:GJ6Z-610-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0050009; F:isopropanol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. 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; Metal-binding; NADP; Oxidoreductase; KW Reference proteome; Zinc. FT CHAIN 1 351 Probable NADP-dependent isopropanol FT dehydrogenase. FT /FTId=PRO_0000160746. FT NP_BIND 175 178 NADP. {ECO:0000250}. FT NP_BIND 198 200 NADP. {ECO:0000250}. FT NP_BIND 265 267 NADP. {ECO:0000250}. FT METAL 37 37 Zinc; catalytic. {ECO:0000250}. FT METAL 59 59 Zinc; catalytic. {ECO:0000250}. FT METAL 60 60 Zinc; catalytic. {ECO:0000250}. FT METAL 150 150 Zinc; catalytic. {ECO:0000250}. FT BINDING 340 340 NADP. {ECO:0000250}. SQ SEQUENCE 351 AA; 37812 MW; 3153B93BFFE64D2C CRC64; MKAYAMLKIG ATGWIEKPRP VCGPNDAIIR PLAVAPCTSD VHTVWEGGIG ERHNMVLGHE GCGVVDEVGS EVKSFKVGDR VLVAAITPEW NSVNAQAGYP MHSGGMLGGW KFSNVKDGMF AEYFHVNDAE GNLALMPEGM DLADACMLSD MIPTGFHANE LADIQYGVAL SFFCAGPVGL MAIAGAALKG AGRIIVVDSR PDIVEIAKAY GATDYIDFKK VSVVDEILKW TNNEGVEKVL ISGGGSTILE TAIKVLRPGG KIGNVNYFGA GEFLTIPRVE WGVGMAHKAI HGGLMLGGRL RLEKLARLIM TKKLDPSKMI THRFKGFEHI EEALFLMKDK PKDLIKSVVI F // ID ACPS_MYCPN Reviewed; 119 AA. AC P75480; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. 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=MPN_298; ORFNames=MP538; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96186.1; -; Genomic_DNA. DR PIR; S73864; S73864. DR RefSeq; NP_109986.1; NC_000912.1. DR RefSeq; WP_010874655.1; NC_000912.1. DR ProteinModelPortal; P75480; -. DR IntAct; P75480; 1. DR EnsemblBacteria; AAB96186; AAB96186; MPN_298. DR GeneID; 877350; -. DR KEGG; mpn:MPN298; -. DR PATRIC; 20021931; VBIMycPne110_0322. DR KO; K00997; -. DR OMA; KFLATRW; -. DR OrthoDB; EOG6384R9; -. DR BioCyc; MPNE272634:GJ6Z-305-MONOMER; -. DR Proteomes; UP000000808; 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; 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 1 119 Holo-[acyl-carrier-protein] synthase. FT /FTId=PRO_0000175673. FT METAL 8 8 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. FT METAL 60 60 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. SQ SEQUENCE 119 AA; 13774 MW; 9394A16B4FCBC131 CRC64; MILGIGIDLV EIKRFEQLAR QTDNCFAKRL LTSTEYAHYA KLRKDSEKSS FLAVHWSLKE AIYKAVNHIK PLFSQLEITK KNQRYNCQID PKIELLLSVS YSSNNITAIC LAQQTPWKN // ID ALF_MYCPN Reviewed; 288 AA. AC P75089; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Fructose-bisphosphate aldolase; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; GN Name=fba; Synonyms=tsr; OrderedLocusNames=MPN_025; ORFNames=MP129; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3- CC phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in CC gluconeogenesis and the reverse reaction in glycolysis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the CC other provides a structural contribution. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase 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; U00089; AAB95777.1; -; Genomic_DNA. DR PIR; S73455; S73455. DR RefSeq; NP_109713.1; NC_000912.1. DR RefSeq; WP_010874382.1; NC_000912.1. DR ProteinModelPortal; P75089; -. DR IntAct; P75089; 7. DR EnsemblBacteria; AAB95777; AAB95777; MPN_025. DR GeneID; 876888; -. DR KEGG; mpn:MPN025; -. DR PATRIC; 20021325; VBIMycPne110_0024. DR KO; K01624; -. DR OMA; VNTREMF; -. DR OrthoDB; EOG6HXJ7B; -. DR BioCyc; MetaCyc:MONOMER-546; -. DR BioCyc; MPNE272634:GJ6Z-27-MONOMER; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000808; 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:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011289; Fruc_bis_ald_class-2. 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; TIGR01859; fruc_bis_ald_; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Lyase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 288 Fructose-bisphosphate aldolase. FT /FTId=PRO_0000178720. FT REGION 207 209 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT REGION 228 231 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT ACT_SITE 84 84 Proton donor. {ECO:0000250}. FT METAL 85 85 Zinc 1; catalytic. {ECO:0000250}. FT METAL 105 105 Zinc 2. {ECO:0000250}. FT METAL 135 135 Zinc 2. {ECO:0000250}. FT METAL 177 177 Zinc 1; catalytic. {ECO:0000250}. FT METAL 206 206 Zinc 1; catalytic. {ECO:0000250}. FT BINDING 49 49 Glyceraldehyde 3-phosphate. FT {ECO:0000250}. FT BINDING 178 178 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 288 AA; 31069 MW; 174A7F2E4E215FD8 CRC64; MLVNIKQMLQ HAKQHHYAVP HININNYEWA KAVLTAAQQA KSPIIVSTSE GALKYISGHQ VVVPMVKGLV DALKITVPVA LHLDHGSYEG CKAALQAGFS SIMFDGSHLP FQENFTKSKE LIELAKQTNA SVELEVGTLG GEEDGIVGQG ELANIEECKQ IATLKPDALA AGIGNIHGLY PDNWKGLNYE LIEAIAKATN LPLVLHGGSG IPEADVKKAI GLGISKLNIN TECQLAFAKA IREYVEAKKD LDTHNKGYDP RKLLKSPTQA IVDCCLEKMQ LCGSTNKA // ID AMPA_MYCPN Reviewed; 445 AA. AC P75206; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Probable cytosol aminopeptidase; DE EC=3.4.11.1; DE AltName: Full=Leucine aminopeptidase; DE Short=LAP; DE EC=3.4.11.10; DE AltName: Full=Leucyl aminopeptidase; GN Name=pepA; OrderedLocusNames=MPN_572; ORFNames=MP270; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By CC similarity). {ECO:0000250}. 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. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, CC preferentially leucine, but not glutamic or aspartic acids. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M17 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; U00089; AAB95918.1; -; Genomic_DNA. DR PIR; S73596; S73596. DR RefSeq; NP_110261.1; NC_000912.1. DR RefSeq; WP_010874929.1; NC_000912.1. DR ProteinModelPortal; P75206; -. DR EnsemblBacteria; AAB95918; AAB95918; MPN_572. DR GeneID; 876829; -. DR KEGG; mpn:MPN572; -. DR PATRIC; 20022623; VBIMycPne110_0634. DR KO; K01255; -. DR OMA; ISGTALW; -. DR OrthoDB; EOG6FV8B3; -. DR BioCyc; MPNE272634:GJ6Z-618-MONOMER; -. DR Proteomes; UP000000808; 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 Pfam; PF00883; Peptidase_M17; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese; KW Metal-binding; Protease; Reference proteome. FT CHAIN 1 445 Probable cytosol aminopeptidase. FT /FTId=PRO_0000165768. FT ACT_SITE 229 229 {ECO:0000255}. FT ACT_SITE 303 303 {ECO:0000255}. FT METAL 217 217 Manganese 2. {ECO:0000250}. FT METAL 222 222 Manganese 1. {ECO:0000250}. FT METAL 222 222 Manganese 2. {ECO:0000250}. FT METAL 240 240 Manganese 2. {ECO:0000250}. FT METAL 299 299 Manganese 1. {ECO:0000250}. FT METAL 301 301 Manganese 1. {ECO:0000250}. FT METAL 301 301 Manganese 2. {ECO:0000250}. SQ SEQUENCE 445 AA; 48789 MW; 9CE6A05822C4D8E2 CRC64; MKLNKLFDSK TVVFKKSDKY GKSDCCKTKC VEGQIEFGVK IPTDFPAFNR ALVTFLKTQK NQLNVDLDSF VELYKAENLC YKTALKVVVA SITFCETTPF TMKTEPQKNV EVAVKCDSEH TSLIKEYEVV GNYVNMARQL QDTPSDQLYP EEFVKRFEKA ATGLGVKITV LKQADLIKKK MGLLLGVNKG SEREARLLVI SYNNNKKSSE TLALVGKGIT YDSGGMNIKT GDYMRGMKYD MSGAAIVCST VLALAKNKVK TNVVAVAALT ENLPGPHAQR PDDIQTAYNG KTVEIDNTDA EGRLVLADAI SYAAKDLKAT QIIDVATLTG LMSYILSTTY TGIFSTCDMA WDAFKKAACC AGEPVWRLPM HPDYLKPLES KLADLQNSTS VKGAGSSRAA CFLAEFREGV PLIHCDIAST ASIQDLGQGV LVRTLYERAA QQAKE // ID ADP1_MYCPN Reviewed; 1627 AA. AC P11311; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 24-JUN-2015, entry version 102. DE RecName: Full=Adhesin P1; DE AltName: Full=Attachment protein; DE AltName: Full=Cytadhesin P1; DE Flags: Precursor; GN Name=mgpA; OrderedLocusNames=MPN_141; ORFNames=MP013; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 29342 / M129; RX PubMed=3119495; RA Su C.-J., Tryon V.V., Baseman J.B.; RT "Cloning and sequence analysis of cytadhesin P1 gene from Mycoplasma RT pneumoniae."; RL Infect. Immun. 55:3023-3029(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2841195; DOI=10.1016/0378-1119(88)90337-X; RA Inamine J.M., Denny T.P., Loechel S., Schaper U., Huang C.H., RA Bott K.F., Hu P.C.; RT "Nucleotide sequence of the P1 attachment-protein gene of Mycoplasma RT pneumoniae."; RL Gene 64:217-229(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1301-1520. RC STRAIN=ATCC 29342 / M129; RX PubMed=2450165; DOI=10.1084/jem.167.2.718; RA Dallo S.F., Su C.-J., Horton J.R., Baseman J.B.; RT "Identification of P1 gene domain containing epitope(s) mediating RT Mycoplasma pneumoniae cytoadherence."; RL J. Exp. Med. 167:718-723(1988). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: The protein is the major adhesin mediating the CC attachment of this mycoplasma to respiratory epithelium. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC type I membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the adhesin P1 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; M18639; AAA25424.1; -; Genomic_DNA. DR EMBL; M21519; AAA88325.1; -; Genomic_DNA. DR EMBL; U00089; AAB95661.1; -; Genomic_DNA. DR EMBL; X07191; CAB37298.1; -; Genomic_DNA. DR PIR; A41480; A41480. DR PIR; S03725; IJYMAP. DR RefSeq; NP_109829.1; NC_000912.1. DR RefSeq; WP_010874498.1; NC_000912.1. DR IntAct; P11311; 2. DR EnsemblBacteria; AAB95661; AAB95661; MPN_141. DR GeneID; 877268; -. DR KEGG; mpn:MPN141; -. DR PATRIC; 20021597; VBIMycPne110_0155. DR OMA; GKENEFA; -. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-148-MONOMER; -. DR Proteomes; UP000000808; 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:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR InterPro; IPR022400; Adhesin_P1. DR InterPro; IPR004940; Adhesin_P1_dom. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF03257; Adhesin_P1; 1. DR Pfam; PF12378; CytadhesinP1; 2. DR TIGRFAMs; TIGR03839; termin_org_P1; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Cytadherence; KW Direct protein sequencing; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 59 FT CHAIN 60 1627 Adhesin P1. FT /FTId=PRO_0000020629. FT TRANSMEM 1527 1547 Helical. {ECO:0000255}. FT REGION 1403 1415 Cytadherence epitope. SQ SEQUENCE 1627 AA; 176270 MW; 14F7A2CBA36E6116 CRC64; MHQTKKTALS KSTWILILTA TASLATGLTV VGHFTSTTTT LKRQQFSYTR PDEVALRHTN AINPRLTPWT YRNTSFSSLP LTGENPGAWA LVRDNSAKGI TAGSGSQQTT YDPTRTEAAL TASTTFALRR YDLAGRALYD LDFSKLNPQT PTRDQTGQIT FNPFGGFGLS GAAPQQWNEV KNKVPVEVAQ DPSNPYRFAV LLVPRSVVYY EQLQRGLGLP QQRTESGQNT STTGAMFGLK VKNAEADTAK SNEKLQGAEA TGSSTTSGSG QSTQRGGSSG DTKVKALKIE VKKKSDSEDN GQLQLEKNDL ANAPIKRSEE SGQSVQLKAD DFGTALSSSG SGGNSNPGSP TPWRPWLATE QIHKDLPKWS ASILILYDAP YARNRTAIDR VDHLDPKAMT ANYPPSWRTP KWNHHGLWDW KARDVLLQTT GFFNPRRHPE WFDGGQTVAD NEKTGFDVDN SENTKQGFQK EADSDKSAPI ALPFEAYFAN IGNLTWFGQA LLVFGGNGHV TKSAHTAPLS IGVFRVRYNA TGTSATVTGW PYALLFSGMV NKQTDGLKDL PFNNNRWFEY VPRMAVAGAK FVGRELVLAG TITMGDTATV PRLLYDELES NLNLVAQGQG LLREDLQLFT PYGWANRPDL PIGAWSSSSS SSHNAPYYFH NNPDWQDRPI QNVVDAFIKP WEDKNGKDDA KYIYPYRYSG MWAWQVYNWS NKLTDQPLSA DFVNENAYQP NSLFAAILNP ELLAALPDKV KYGKENEFAA NEYERFNQKL TVAPTQGTNW SHFSPTLSRF STGFNLVGSV LDQVLDYVPW IGNGYRYGNN HRGVDDITAP QTSAGSSSGI STNTSGSRSF LPTFSNIGVG LKANVQATLG GSQTMITGGS PRRTLDQANL QLWTGAGWRN DKASSGQSDE NHTKFTSATG MDQQGQSGTS AGNPDSLKQD NISKSGDSLT TQDGNAIDQQ EATNYTNLPP NLTPTADWPN ALSFTNKNNA QRAQLFLRGL LGSIPVLVNR SGSDSNKFQA TDQKWSYTDL HSDQTKLNLP AYGEVNGLLN PALVETYFGN TRAGGSGSNT TSSPGIGFKI PEQNNDSKAT LITPGLAWTP QDVGNLVVSG TTVSFQLGGW LVTFTDFVKP RAGYLGLQLT GLDASDATQR ALIWAPRPWA AFRGSWVNRL GRVESVWDLK GVWADQAQSD SQGSTTTATR NALPEHPNAL AFQVSVVEAS AYKPNTSSGQ TQSTNSSPYL HLVKPKKVTQ SDKLDDDLKN LLDPNQVRTK LRQSFGTDHS TQPQPQSLKT TTPVFGTSSG NLSSVLSGGG AGGGSSGSGQ SGVDLSPVEK VSGWLVGQLP STSDGNTSST NNLAPNTNTG NDVVGVGRLS ESNAAKMNDD VDGIVRTPLA ELLDGEGQTA DTGPQSVKFK SPDQIDFNRL FTHPVTDLFD PVTMLVYDQY IPLFIDIPAS VNPKMVRLKV LSFDTNEQSL GLRLEFFKPD QDTQPNNNVQ VNPNNGDFLP LLTASSQGPQ TLFSPFNQWP DYVLPLAITV PIVVIVLSVT LGLAIGIPMH KNKQALKAGF ALSNQKVDVL TKAVGSVFKE IINRTGISQA PKRLKQTSAA KPGAPRPPVP PKPGAPKPPV QPPKKPA // ID AMPP_MYCPN Reviewed; 354 AA. AC P75313; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Putative Xaa-Pro aminopeptidase; DE Short=X-Pro aminopeptidase; DE EC=3.4.11.9; DE AltName: Full=Aminoacylproline aminopeptidase; DE AltName: Full=Aminopeptidase P; DE Short=APP; GN Name=pepP; OrderedLocusNames=MPN_470; ORFNames=MP371; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Release of any N-terminal amino acid, CC including proline, that is linked to proline, even from a CC dipeptide or tripeptide. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M24B 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; U00089; AAB96019.1; -; Genomic_DNA. DR PIR; S73697; S73697. DR RefSeq; NP_110158.1; NC_000912.1. DR RefSeq; WP_010874826.1; NC_000912.1. DR ProteinModelPortal; P75313; -. DR EnsemblBacteria; AAB96019; AAB96019; MPN_470. DR GeneID; 877187; -. DR KEGG; mpn:MPN470; -. DR PATRIC; 20022362; VBIMycPne110_0508. DR OMA; QAPGEMD; -. DR OrthoDB; EOG618QTW; -. DR BioCyc; MPNE272634:GJ6Z-511-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.350.10; -; 1. 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; IPR001131; Peptidase_M24B_aminopep-P_CS. DR Pfam; PF01321; Creatinase_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR SUPFAM; SSF53092; SSF53092; 1. DR SUPFAM; SSF55920; SSF55920; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Hydrolase; Manganese; KW Metal-binding; Metalloprotease; Protease; Reference proteome. FT CHAIN 1 354 Putative Xaa-Pro aminopeptidase. FT /FTId=PRO_0000185078. FT METAL 213 213 Manganese 2. {ECO:0000250}. FT METAL 224 224 Manganese 1. {ECO:0000250}. FT METAL 224 224 Manganese 2. {ECO:0000250}. FT METAL 290 290 Manganese 1. {ECO:0000250}. FT METAL 319 319 Manganese 1. {ECO:0000250}. FT METAL 333 333 Manganese 1. {ECO:0000250}. FT METAL 333 333 Manganese 2. {ECO:0000250}. SQ SEQUENCE 354 AA; 39624 MW; A5286BD9F414A132 CRC64; MHNELQQKLA VLHKLLQDNK ADAILIGSDQ NRFWLTGFPS SAGWLVVHKQ RVNLFIDGRY FEAAKTAIDP LVKVELFTTY KQVKALCEQV GVKHLLIEGD YLTFNYQNFI KELCAQYTVI NAQEIRRQKL PSEILAIEKV VEITRKVAVK LKRFIQPGMT ELFIAQWITD QLVKAGGAKN SFDPIVATGK NGANPHHKPS KLKVKSGDFV TCDFGTIYNG YCSDITRTFL VGKKPNNEVL LKAYKKVDEA NMAGINAANT QLTGAEVDKV CRDIIEASEF KDYFVHSTGH GVGLDIHEMP NVSTSYNKLL CENAVITIEP GIYIPSVGGI RIEDMVLVKD HKSVWLSAKI PRAF // ID ARCL_MYCPN Reviewed; 309 AA. AC P78030; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Carbamate kinase-like protein; GN OrderedLocusNames=MPN_307; ORFNames=F10_orf309, MP529; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260448, EBI-2260448; CC P09924:deoC; NbExp=1; IntAct=EBI-2260448, EBI-2260368; CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96177.1; -; Genomic_DNA. DR EMBL; U59896; AAB52524.1; -; Genomic_DNA. DR PIR; S73855; S73855. DR RefSeq; NP_109995.1; NC_000912.1. DR RefSeq; WP_010874663.1; NC_000912.1. DR ProteinModelPortal; P78030; -. DR IntAct; P78030; 2. DR EnsemblBacteria; AAB96177; AAB96177; MPN_307. DR GeneID; 876908; -. DR KEGG; mpn:MPN307; -. DR PATRIC; 20021966; VBIMycPne110_0331. DR KO; K00926; -. DR OMA; ADIFMIL; -. DR OrthoDB; EOG65QWKX; -. DR BioCyc; MPNE272634:GJ6Z-323-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008804; F:carbamate kinase activity; IEA:InterPro. DR GO; GO:0006525; P:arginine metabolic process; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR003964; Carb_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000723; Carbamate_kin; 1. DR PRINTS; PR01469; CARBMTKINASE. DR SUPFAM; SSF53633; SSF53633; 1. PE 1: Evidence at protein level; KW Complete proteome; Kinase; Reference proteome; Transferase. FT CHAIN 1 309 Carbamate kinase-like protein. FT /FTId=PRO_0000185145. SQ SEQUENCE 309 AA; 32785 MW; 28BDDD8D89EB1E28 CRC64; MQKIVIALGG NALGNNPTEQ KDLVQLPARQ AVALLKQGYQ ILLGHGNGPQ VGMIYNAFSA AKQVNPNTPT VPFAESGAMS QGYIGLHLLT ALYNELLHQK LPHQAVYFLT QTLVEASDPA FQNPNKPVGP FYNTEETARS ANPNSTVVED AGRGWRKVVA SPKPVDVLGI DAIKSSFNQG NLVIVGGGGG VPTIKTKSGY ATVDGVIDKD LALSEIAIKV EADLFVILTA VDFVYINYGQ PNEQKLTCIN TKEAKTLMAA NQFAKGSMLP KVEACLNFVQ SGTNKTAIIA QLDQLAAAIA GKIGTKIVK // ID ARCA_MYCPN Reviewed; 404 AA. AC P75475; P75474; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-MAY-2016, entry version 94. DE RecName: Full=Putative arginine deiminase; DE Short=ADI; DE EC=3.5.3.6; DE AltName: Full=Arginine dihydrolase; DE Short=AD; GN Name=arcA; OrderedLocusNames=MPN_304/MPN_305; ORFNames=MP531/MP532; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: L-arginine + H(2)O = L-citrulline + NH(3). CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI CC pathway; carbamoyl phosphate from L-arginine: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the arginine deiminase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96179.1; Type=Frameshift; Positions=Several; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; CC Sequence=AAB96180.1; Type=Frameshift; Positions=Several; Note=Produces two separate ORFs.; 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; U00089; AAB96180.1; ALT_FRAME; Genomic_DNA. DR EMBL; U00089; AAB96179.1; ALT_FRAME; Genomic_DNA. DR PIR; S73857; S73857. DR PIR; S73858; S73858. DR ProteinModelPortal; P75475; -. DR SMR; P75475; 4-404. DR IntAct; P75475; 1. DR EnsemblBacteria; AAB96179; AAB96179; MPN_305. DR EnsemblBacteria; AAB96180; AAB96180; MPN_304. DR PATRIC; 20021959; VBIMycPne110_0328. DR OrthoDB; EOG65J52D; -. DR BioCyc; MPNE272634:GJ6Z-321-MONOMER; -. DR UniPathway; UPA00254; UER00364. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00242; Arg_deiminase; 1. DR InterPro; IPR003876; Arg_deiminase. DR InterPro; IPR033199; DDAH/AD. DR PANTHER; PTHR12737; PTHR12737; 3. DR PIRSF; PIRSF006356; Arg_deiminase; 1. DR PRINTS; PR01466; ARGDEIMINASE. PE 3: Inferred from homology; KW Arginine metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Reference proteome. FT CHAIN 1 404 Putative arginine deiminase. FT /FTId=PRO_0000182222. FT ACT_SITE 394 394 Amidino-cysteine intermediate. FT {ECO:0000250}. SQ SEQUENCE 404 AA; 45479 MW; 22A99F5437A7E3BE CRC64; MKYNINVHSE IGQLQTVLVH TPGNEIRRIS PRRLDDLLFS AVIEPDTAIQ EHQTFCQLLQ EQNIEVVQLT DLTATTFDKA NATAQNQFIE TWLDQAEPKL TPEHRKVAKQ YLLEQKAKST LSMVRSMMGG IDKRKVAAAN TINGDFLVDP MPNLYFTRDP FASIGHGISI NRMKYLTRRR ETLFASFIFA NHPIIAARKF YFKPIDMGTI EGGDIFVYDQ QTVVMGLSER TTEAAINVLA KKIQQDSSTS FKRIFVINVP QLPNLMHLDT WLTMLDRNKF LYSPNMLAVL KAWRIDFTDP ALKWNEIAGD LSTILHTIIG QKPMLIPIAG ADANQTEIDI ETHFDGTNYL TIAPSVVVGY ARNKLTHQTL EAAGVKVIAF KGNQLSLGMG SARCMSMPLV RKPL // ID ARCX_MYCPN Reviewed; 438 AA. AC P75218; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Arginine deiminase-like protein; GN OrderedLocusNames=MPN_560; ORFNames=MP282; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260847, EBI-2260847; CC -!- SIMILARITY: Belongs to the arginine deiminase 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; U00089; AAB95930.1; -; Genomic_DNA. DR PIR; S73608; S73608. DR RefSeq; NP_110249.1; NC_000912.1. DR RefSeq; WP_010874917.1; NC_000912.1. DR ProteinModelPortal; P75218; -. DR DNASU; 877192; -. DR EnsemblBacteria; AAB95930; AAB95930; MPN_560. DR GeneID; 877192; -. DR KEGG; mpn:MPN560; -. DR PATRIC; 20022599; VBIMycPne110_0622. DR KO; K01478; -. DR OMA; EMINAMI; -. DR OrthoDB; EOG65J52D; -. DR BioCyc; MetaCyc:MONOMER-507; -. DR BioCyc; MPNE272634:GJ6Z-606-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016990; F:arginine deiminase activity; IEA:InterPro. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR InterPro; IPR003876; Arg_deiminase. DR InterPro; IPR033199; DDAH/AD. DR PANTHER; PTHR12737; PTHR12737; 3. DR PIRSF; PIRSF006356; Arg_deiminase; 1. DR PRINTS; PR01466; ARGDEIMINASE. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 438 Arginine deiminase-like protein. FT /FTId=PRO_0000182257. SQ SEQUENCE 438 AA; 49442 MW; E3DB589827675010 CRC64; MSKKQLVKTD GHNQLDQPNT KALQLKKKQF NSGVRVTSEI SFLREVIAHH PGIETERVID NQTFGSAMYL ERAQKEHQLF IKILRQHGTK VHYLQDLLLE ALSAADPNVR QDFIKNFLLE SGIKSVSTFE ACLNFFRSLD SLVDVIKVMF GGIKVSDVPP ITPQRFADIH VSNSPFLIKP LSFSLYPHKF FNTLGTGVAL FVTNDSELKR HSLVYEYIMR FHPRFDGVKL YTNRDFKNCL INSSDIIQIS NEILLIGISH DTDVLGIESL ARNLLSDHTN PIKQIIAINI HKFGAKTNLN KLIAMVDVDK FIIARKVLQA TEIFELTATA QRDVDGLAQI KFKPLKFNFG EIIEAIIDKQ PRFVIIGGGD EVAERKELLD CGMGVLNLSP GEIVVFDRNH YTNNLLNELG LIIHKIPASE LSRGPSGPLE MVCSLWRE // ID APT_MYCPN Reviewed; 177 AA. AC P75388; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 96. 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=MPN_395; GN ORFNames=MP443; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34752.1; -; Genomic_DNA. DR PIR; S73769; S73769. DR RefSeq; NP_110083.1; NC_000912.1. DR RefSeq; WP_010874751.1; NC_000912.1. DR ProteinModelPortal; P75388; -. DR IntAct; P75388; 4. DR EnsemblBacteria; AAG34752; AAG34752; MPN_395. DR GeneID; 877054; -. DR KEGG; mpn:MPN395; -. DR PATRIC; 20022166; VBIMycPne110_0426. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; MPNE272634:GJ6Z-418-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000808; 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 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149417. SQ SEQUENCE 177 AA; 19925 MW; 78424B8FBD804A73 CRC64; MKQKLQALDR AIKRFNDFPT PGILFYDITP IFLNSELFEF VLEQMAQFIQ EVKADGIVCP EARGFIFGGA LASKTKLPLV LVRKPHKLSG ELARETYDLE YRQNSILEMR VDALENCKRC VIVDDLLATA GTVAAIDKLI ARLGSQTVGY CFLIELQKLH GKAKLQPNVA TKILLHY // ID ATPA_MYCPN Reviewed; 518 AA. AC Q50329; Q50344; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 120. 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=MPN_600; ORFNames=MP242; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-113. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). 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 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; U43738; AAC43657.1; -; Genomic_DNA. DR EMBL; U00089; AAB95890.1; -; Genomic_DNA. DR EMBL; Z32649; CAA83571.1; -; Genomic_DNA. DR PIR; S62847; S62847. DR RefSeq; NP_110289.1; NC_000912.1. DR RefSeq; WP_010874957.1; NC_000912.1. DR ProteinModelPortal; Q50329; -. DR SMR; Q50329; 26-499. DR IntAct; Q50329; 2. DR EnsemblBacteria; AAB95890; AAB95890; MPN_600. DR GeneID; 877099; -. DR KEGG; mpn:MPN600; -. DR PATRIC; 20022681; VBIMycPne110_0663. DR KO; K02111; -. DR OMA; PVFCIYV; -. DR OrthoDB; EOG67X1S1; -. DR BioCyc; MPNE272634:GJ6Z-646-MONOMER; -. DR Proteomes; UP000000808; 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 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 membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 518 ATP synthase subunit alpha. FT /FTId=PRO_0000144337. FT NP_BIND 169 176 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 362 362 Required for activity. FT {ECO:0000255|HAMAP-Rule:MF_01346}. FT CONFLICT 111 113 LGE -> WEN (in Ref. 3; CAA83571). FT {ECO:0000305}. SQ SEQUENCE 518 AA; 57375 MW; DA0ACBFA31C1C368 CRC64; MADKLNEYVA LIKNEIKKYS KQIFNSEIGK VISVADGIAK VSGLENALLN ELIEFENNVQ GIALNLEQNT VGVALFGDYS KIREGSTAKR THNVMQTPVG DVMLGRIVNA LGEPVDGRGP IKAEEFDQVE KIAPGVMTRK TVNQPLETGI LTIDALFPIG KGQRELIVGD RQTGKTSIAI DTIINQRGKD VYCVYVAMGQ KNSSVAQIVH QLEVTDSMKY TTVVCATASD PASMIYLTPF TGITIAEYWL KQGKDVLIVF DDLSKHAIAY RTLSLLLRRP PGREAFPGDV FYLHSRLLER ACRLNEEHGG GSITALPIIE TQAGDISAYI PTNVISITDG QLFMVSNLFN SGQRPAIHVG LSVSRVGSAA QIKAIKQQTG SLKLELAQYS ELDSFSQFGS DLDENTKQIL ERGKRVMEMI KQPNGKPYSQ THEALFLFAI AKSFIKFIPL DYIAKFKQRI MEEFDKEHPI YKEIATQKSF SEALEAQTNT AFKALVKRFV SALPDYDITK YGTMEELE // ID ATPB_MYCPN Reviewed; 475 AA. AC Q50331; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 113. 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=MPN_598; ORFNames=MP244; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 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; U43738; AAC43659.1; -; Genomic_DNA. DR EMBL; U00089; AAB95892.1; -; Genomic_DNA. DR PIR; S62849; S62849. DR RefSeq; NP_110287.1; NC_000912.1. DR RefSeq; WP_010874955.1; NC_000912.1. DR ProteinModelPortal; Q50331; -. DR SMR; Q50331; 9-467. DR IntAct; Q50331; 1. DR PRIDE; Q50331; -. DR EnsemblBacteria; AAB95892; AAB95892; MPN_598. DR GeneID; 877122; -. DR KEGG; mpn:MPN598; -. DR PATRIC; 20022677; VBIMycPne110_0661. DR KO; K02112; -. DR OMA; FKESGVI; -. DR OrthoDB; EOG6HQSP3; -. DR BioCyc; MPNE272634:GJ6Z-644-MONOMER; -. DR Proteomes; UP000000808; 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 membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 475 ATP synthase subunit beta. FT /FTId=PRO_0000144453. FT NP_BIND 156 163 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 475 AA; 52237 MW; 1533D5A16D5135AC CRC64; MKKENITYGK VHQVIGPVVD VIFTESSQLP RIYDCLSVKL AGEELFLEAA QLIGDDIVRC IALGPTEGLA RNEKVTNYNH PIEVPVGKNV LGRMFNVLGK PIDGKEELPK KPQLPIHRKP PSFDDQSNTL EIFETGIKVI DLLTPYARGG KIGLFGGAGV GKTVLVQELI HNIAKEHSGL SVFAGVGERT REGNDLYYEM IQGGVIDKTA LVFGQMNEPP GARMRVALTA LTMAEYFRDH DNQDVLLFID NIFRFTQAGS EVSALLGRMP SAVGYQPTLA TEMGQLQERI ASTKTGSITS VQAIYVPADD LTDPAPATTF THLDAKTVLD RNIAALGIFP AINPLESTSR LLDPNIVGIN HYKVALGVQN ILQRFAELQD IIAILGIDEL ADEDKIIVER ARRIRNFLSQ PFFVAEKFSG IAGKYVPLSD TIQSFKEILD GKHDDLPEQA FFFVGTIQEA VEKAKRLKKA TVEEK // ID ATPD_MYCPN Reviewed; 178 AA. AC Q50328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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=MPN_601; ORFNames=MP241; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 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; U43738; AAC43656.1; -; Genomic_DNA. DR EMBL; U00089; AAB95889.1; -; Genomic_DNA. DR PIR; S62846; S62846. DR RefSeq; NP_110290.1; NC_000912.1. DR RefSeq; WP_010874958.1; NC_000912.1. DR ProteinModelPortal; Q50328; -. DR EnsemblBacteria; AAB95889; AAB95889; MPN_601. DR GeneID; 876990; -. DR KEGG; mpn:MPN601; -. DR PATRIC; 20022683; VBIMycPne110_0664. DR KO; K02113; -. DR OMA; SAFEIDN; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; MPNE272634:GJ6Z-647-MONOMER; -. DR Proteomes; UP000000808; 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 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 membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 178 ATP synthase subunit delta. FT /FTId=PRO_0000193469. SQ SEQUENCE 178 AA; 20740 MW; 97774BA8D23FCBCA CRC64; MINAQAFGMA LFQLSEEEKK VKKVYDQSHD FLKLARNFKD GSLAALLNAY TLTKKEKLKL IDKLFKNHFC DLFVDFLKTI VLKGYFNLVE QALKYFFDCV ENEKHVQFIR IITAFELSAP QLKRIVAAME KKLNSKIVYK TEIDKSLISG IRIESSAQLF EKNIRDQLSR LMEQFKGN // ID ATPF_MYCPN Reviewed; 207 AA. AC Q50327; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 97. 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}; DE Flags: Precursor; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; GN OrderedLocusNames=MPN_602; ORFNames=MP240; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP CHARACTERIZATION AS A LIPOPROTEIN, DIACYLGLYCEROL AT CYS-28, AND RP PALMITOYLATION AT CYS-28. RC STRAIN=ATCC 29342 / M129; RX PubMed=9733782; DOI=10.1074/jbc.273.38.24792; RA Pyrowolakis G., Hofmann D., Herrmann R.; RT "The subunit b of the F0F1-type ATPase of the bacterium Mycoplasma RT pneumoniae is a lipoprotein."; RL J. Biol. Chem. 273:24792-24796(1998). 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 -!- INTERACTION: CC Q50331:atpD; NbExp=1; IntAct=EBI-2259688, EBI-2259684; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. 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; U43738; AAC43655.1; -; Genomic_DNA. DR EMBL; U00089; AAB95888.1; -; Genomic_DNA. DR PIR; S62845; S62845. DR RefSeq; NP_110291.1; NC_000912.1. DR RefSeq; WP_010874959.1; NC_000912.1. DR ProteinModelPortal; Q50327; -. DR IntAct; Q50327; 3. DR EnsemblBacteria; AAB95888; AAB95888; MPN_602. DR GeneID; 877080; -. DR KEGG; mpn:MPN602; -. DR PATRIC; 20022685; VBIMycPne110_0665. DR KO; K02109; -. DR OMA; HFAWGPV; -. DR OrthoDB; EOG63VC12; -. DR BioCyc; MPNE272634:GJ6Z-648-MONOMER; -. DR Proteomes; UP000000808; 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 HAMAP; MF_01398; ATP_synth_b_bact; 1. 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 TIGRFAMs; TIGR01144; ATP_synt_b; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW ATP synthesis; Cell membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 27 FT CHAIN 28 207 ATP synthase subunit b. FT /FTId=PRO_0000002632. FT TRANSMEM 49 69 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000269|PubMed:9733782}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000269|PubMed:9733782}. SQ SEQUENCE 207 AA; 24019 MW; C1B0DF1D66D4E853 CRC64; MKLRATFVFK TTLVALSFAL FALFLVSCTE NVKEIKSESV INELFPNLWV FLAHLLAFVI LLFLLLFLFW KPTQKFLNQR KALLEEQVNQ ANSLEQQAQA LLQQANQRHE NSLVVAKEIV DQANYEALQL KSEIEKKANR QANLMIFQAR QEIEKEKRLI QEQSLKESVE LAMLAAKELI IKKVDVKADK AFIEEFIREL EAEDDHD // ID ATPE_MYCPN Reviewed; 133 AA. AC Q50332; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=ATP synthase epsilon chain; DE AltName: Full=ATP synthase F1 sector epsilon subunit; DE AltName: Full=F-ATPase epsilon subunit; GN Name=atpC; OrderedLocusNames=MPN_597; ORFNames=MP245; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. 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 membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain 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; U43738; AAC43660.1; -; Genomic_DNA. DR EMBL; U00089; AAB95893.1; -; Genomic_DNA. DR PIR; S62850; S62850. DR RefSeq; NP_110286.1; NC_000912.1. DR RefSeq; WP_010874954.1; NC_000912.1. DR ProteinModelPortal; Q50332; -. DR EnsemblBacteria; AAB95893; AAB95893; MPN_597. DR GeneID; 877138; -. DR KEGG; mpn:MPN597; -. DR PATRIC; 20022675; VBIMycPne110_0660. DR KO; K02114; -. DR OMA; KIEMIIV; -. DR OrthoDB; EOG6DRPKK; -. DR BioCyc; MPNE272634:GJ6Z-643-MONOMER; -. DR Proteomes; UP000000808; 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 Pfam; PF02823; ATP-synt_DE_N; 1. DR SUPFAM; SSF51344; SSF51344; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 133 ATP synthase epsilon chain. FT /FTId=PRO_0000188164. SQ SEQUENCE 133 AA; 15171 MW; C17DCA7DE6ADB95A CRC64; MQPLRFLVLS PSGIKLDQAI ISAQVKTTNG YLGLNYNRAP LIAAVQSHFC KILFANNTRR NAIIGAGLVL IKKTEAKIFT ENFVFEDEID LEATLKRKAE LERQMNHSKD LKLNIKIEQN LMFELLKLSN KQR // ID ATCL_MYCPN Reviewed; 872 AA. AC P78036; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Probable cation-transporting P-type ATPase; DE EC=3.6.3.-; GN Name=pacL; OrderedLocusNames=MPN_209; ORFNames=MP622; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Could mediate calcium influx. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type II 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; U00089; AAB96270.1; -; Genomic_DNA. DR PIR; S73948; S73948. DR RefSeq; NP_109897.1; NC_000912.1. DR RefSeq; WP_010874566.1; NC_000912.1. DR ProteinModelPortal; P78036; -. DR IntAct; P78036; 1. DR EnsemblBacteria; AAB96270; AAB96270; MPN_209. DR GeneID; 876769; -. DR KEGG; mpn:MPN209; -. DR PATRIC; 20021743; VBIMycPne110_0228. DR OMA; FLIFNGV; -. DR OrthoDB; EOG6HF5WH; -. DR BioCyc; MPNE272634:GJ6Z-216-MONOMER; -. DR Proteomes; UP000000808; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.1110.10; -; 2. DR Gene3D; 2.70.150.10; -; 2. DR Gene3D; 3.40.1110.10; -; 1. DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR PRINTS; PR00120; HATPASE. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR TIGRFAMs; TIGR01494; ATPase_P-type; 2. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 872 Probable cation-transporting P-type FT ATPase. FT /FTId=PRO_0000046163. FT TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TOPO_DOM 63 79 Extracellular. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TOPO_DOM 101 237 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 238 257 Helical. {ECO:0000255}. FT TOPO_DOM 258 275 Extracellular. {ECO:0000255}. FT TRANSMEM 276 293 Helical. {ECO:0000255}. FT TOPO_DOM 294 642 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 643 662 Helical. {ECO:0000255}. FT TOPO_DOM 663 685 Extracellular. {ECO:0000255}. FT TRANSMEM 686 706 Helical. {ECO:0000255}. FT TOPO_DOM 707 724 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 725 747 Helical. {ECO:0000255}. FT TOPO_DOM 748 768 Extracellular. {ECO:0000255}. FT TRANSMEM 769 788 Helical. {ECO:0000255}. FT TOPO_DOM 789 801 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 802 824 Helical. {ECO:0000255}. FT TOPO_DOM 825 842 Extracellular. {ECO:0000255}. FT TRANSMEM 843 863 Helical. {ECO:0000255}. FT TOPO_DOM 864 872 Cytoplasmic. {ECO:0000255}. FT ACT_SITE 331 331 4-aspartylphosphate intermediate. FT {ECO:0000250}. FT METAL 587 587 Magnesium. {ECO:0000250}. FT METAL 591 591 Magnesium. {ECO:0000250}. SQ SEQUENCE 872 AA; 94968 MW; 42F8001C4798CAFE CRC64; MNKWTGLSAA AVLESRAQHG ANLIPTKKLT PFWLLFLEQF KSLVVILLLV ATILSLVVAI ISGVNANWLF DHNLVIEWTQ PFVILITVLA NSLIGSIQEF KAQKSAHTLK SLTQPFTRVF REEGLVSLPV GEVVVGDIIF LEAGDIIPAD GKVLQANHLR CMESFLTGES VPVDKSVVNT GGKGLLEQTN LLFSGAQVVF GSGVFEVTAV GLNTQVGQIV KTVDSSATKL SPLQQKLEKV GKWFSWFGLG LFVVVFLVQL GLLGFHNFSA NWSIALIGAI ALVVAIIPEG LVTFINVIFA LSVQKLTKQK AIIKYLAAIE TLGGVQIICT DKTGTLTQNK MKVVDYFCFS NTTQTDLARA LCLCNNATVN TNGDSTGDPT EIALLQWLDR DGLELNHYTR VYEKAFDSNR KLMSVVVQKD NRFIVIVKGA HDVLLPLCKG LDSNQIKPLI DERASNGLRN LAVGLKVLYC FDPENTQTVN ELESELDFLG SVSLQDPPRI ESKAAIMACH QANITPIMIT GDHLKTATAI AKELGILTDE RQAILGVDLD PAKIMEYRVF ARVTPQQKLE IVNAWKQAGY TVAVTGDGVN DAPALVTSDV GCCMGQTGVD IAKDAADVII SDDNFATIVN GIEQGRKTFL TCKRVLFNLF LTSIAGTIVV LLGLFVLGEV FREQLSKANH NFQVFTPTQL LIINLFVHGF PAVALAIQPV QEKLMLKPFS TKNLFYNRGG FDLIWQSLLL SFLTLLFYSL GMVYAINDPE LGKSGDLINR AGATCGFMVL GGSAALNSLN LMVDRPLVAT NPKHYGIVWL GALSSIFVFL LIIFINPLGL VFSTLKDLTA HPVLIGYSFG GVLLYMTINE VVKLIRLSYG SV // ID ATP6_MYCPN Reviewed; 293 AA. AC Q50326; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393}; DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393}; DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393}; GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; GN OrderedLocusNames=MPN_604; ORFNames=MP238; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Key component of the proton channel; it plays a direct CC role in the translocation of protons across the membrane. CC {ECO:0000255|HAMAP-Rule:MF_01393}. 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_01393}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01393}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000255|HAMAP-Rule:MF_01393}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43738; AAC43653.1; -; Genomic_DNA. DR EMBL; U00089; AAB95886.1; -; Genomic_DNA. DR PIR; S62843; S62843. DR RefSeq; NP_110293.1; NC_000912.1. DR RefSeq; WP_010874961.1; NC_000912.1. DR ProteinModelPortal; Q50326; -. DR EnsemblBacteria; AAB95886; AAB95886; MPN_604. DR GeneID; 876988; -. DR KEGG; mpn:MPN604; -. DR PATRIC; 20022689; VBIMycPne110_0667. DR KO; K02108; -. DR OMA; VQAYIFF; -. DR OrthoDB; EOG68DD2G; -. DR BioCyc; MPNE272634:GJ6Z-650-MONOMER; -. DR Proteomes; UP000000808; 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; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; SSF81336; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 293 ATP synthase subunit a. FT /FTId=PRO_0000082062. FT TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 73 93 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 102 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 172 192 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 198 218 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 224 244 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 245 265 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. SQ SEQUENCE 293 AA; 33004 MW; AFC833C49331E2EA CRC64; MSPRAIVLKE PNGVNLVPHE GIFDISPVAG WKPLLPTDQV FGIFVVFIVL LTLFLVYWIK LRKADPLRNH SSFVLLMQML FVWAQDTTAD LIGEENKKFT PYFLMLLLYL VSSNLIGLLG GISPPTSSLT FTFSLGLATF LGIVIMGIRY QRWSFFKSFT FNITIKGKKY STLIPNPLSF LGEFAPLFSI SLRLWGNILG GTLILALFYN FWFFAFSTLS NKPLALSLGA IFAGILTPAL HVYFDVVVGT LQGYVFVMLT YNYWAKMRNI GLEESQEAAQ RLQNLEVAKE IIN // ID ATPL_MYCPN Reviewed; 105 AA. AC Q59550; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396}; GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; GN OrderedLocusNames=MPN_603; ORFNames=MP239; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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_01396}. CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct CC role in translocation across the membrane. A homomeric c-ring of CC between 10-14 subunits forms the central stalk rotor element with CC the F(1) delta and epsilon subunits. {ECO:0000255|HAMAP- CC Rule:MF_01396}. 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_01396}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01396}. CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the CC active glutamate residue inhibits ATPase in vitro. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000255|HAMAP-Rule:MF_01396}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43738; AAC43654.1; -; Genomic_DNA. DR EMBL; U00089; AAB95887.1; -; Genomic_DNA. DR PIR; S62844; S62844. DR RefSeq; NP_110292.1; NC_000912.1. DR RefSeq; WP_010874960.1; NC_000912.1. DR ProteinModelPortal; Q59550; -. DR EnsemblBacteria; AAB95887; AAB95887; MPN_603. DR GeneID; 876820; -. DR KEGG; mpn:MPN603; -. DR PATRIC; 20022687; VBIMycPne110_0666. DR KO; K02110; -. DR OMA; CDAIARN; -. DR OrthoDB; EOG68H8G3; -. DR BioCyc; MPNE272634:GJ6Z-649-MONOMER; -. DR Proteomes; UP000000808; 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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR Gene3D; 1.20.20.10; -; 1. DR HAMAP; MF_01396; ATP_synth_c_bact; 1. DR InterPro; IPR000454; ATPase_F0-cplx_csu. 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 PROSITE; PS00605; ATPASE_C; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 105 ATP synthase subunit c. FT /FTId=PRO_0000112154. FT TRANSMEM 37 57 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT TRANSMEM 82 102 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT SITE 86 86 Reversibly protonated during proton FT transport. {ECO:0000255|HAMAP- FT Rule:MF_01396}. SQ SEQUENCE 105 AA; 11016 MW; D0BCE7DCFBCC5034 CRC64; MEHVNEILAT VGRILHETTT ANTNVANKST ERLGAYIGAG ITMVGGATVG LGQGYIFGKA VEAVARNPEV EKQVFKLIFI GSAISESSSI YSLLIAFILI FVSGA // ID ATPG_MYCPN Reviewed; 279 AA. AC Q50330; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. 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=MPN_599; ORFNames=MP243; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 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; U43738; AAC43658.1; -; Genomic_DNA. DR EMBL; U00089; AAB95891.1; -; Genomic_DNA. DR PIR; S62848; S62848. DR RefSeq; NP_110288.1; NC_000912.1. DR RefSeq; WP_010874956.1; NC_000912.1. DR ProteinModelPortal; Q50330; -. DR IntAct; Q50330; 3. DR EnsemblBacteria; AAB95891; AAB95891; MPN_599. DR GeneID; 876987; -. DR KEGG; mpn:MPN599; -. DR PATRIC; 20022679; VBIMycPne110_0662. DR KO; K02115; -. DR OMA; FLYTAQN; -. DR OrthoDB; EOG6R5C97; -. DR BioCyc; MPNE272634:GJ6Z-645-MONOMER; -. DR Proteomes; UP000000808; 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; 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. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 279 ATP synthase gamma chain. FT /FTId=PRO_0000073324. SQ SEQUENCE 279 AA; 32395 MW; D3093D376DE2C89E CRC64; MAFIQEIKRK MTTVQSTIKI TNAMKMVSRA KFVRFKKQFK EVNYFFNEFY KAVGQVVLSL KKMPKPLENP KTLWVMMSSS LGLCGQHNTN MNKLLQTKFQ PGDKIFFLGR KNQSFWNKGD TDNPTVGYVD IQDRDLSFDY CQQVSDQIME QFDLHQLDRI CIIYTQFKNP LIQHANSFQV FPFDVAMFKA FNPVKMEQKL DFEPDEETII KLISPQFFDI ALYGGLVETK LCESASRQNA MDAAAKNAKD LYEKYSIQFN KLRQNSITQE IIEIIGGIS // ID AZOR_MYCPN Reviewed; 197 AA. AC P75305; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 79. DE RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216}; DE EC=1.7.-.- {ECO:0000255|HAMAP-Rule:MF_01216}; DE AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216}; DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216}; GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216}; GN OrderedLocusNames=MPN_479; ORFNames=MP362; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic CC azo compounds to the corresponding amines. Requires NADH, but not CC NADPH, as an electron donor for its activity. {ECO:0000255|HAMAP- CC Rule:MF_01216}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216}. CC -!- INTERACTION: CC P75074:MPN_040; NbExp=1; IntAct=EBI-2260147, EBI-2260151; CC -!- SIMILARITY: Belongs to the azoreductase type 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01216}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96010.1; -; Genomic_DNA. DR PIR; S73688; S73688. DR RefSeq; NP_110167.1; NC_000912.1. DR RefSeq; WP_010874835.1; NC_000912.1. DR ProteinModelPortal; P75305; -. DR IntAct; P75305; 1. DR EnsemblBacteria; AAB96010; AAB96010; MPN_479. DR GeneID; 876744; -. DR KEGG; mpn:MPN479; -. DR PATRIC; 20022382; VBIMycPne110_0518. DR KO; K01118; -. DR OMA; ATTKNFF; -. DR OrthoDB; EOG6QRW9T; -. DR BioCyc; MPNE272634:GJ6Z-520-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_01216; Azoreductase_type1; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR023048; NADH-azoreductase_FMN-depdnt. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 1: Evidence at protein level; KW Complete proteome; Flavoprotein; FMN; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 197 FMN-dependent NADH-azoreductase. FT /FTId=PRO_0000166345. SQ SEQUENCE 197 AA; 21550 MW; B566B394F7936D31 CRC64; MKKVIIIDAS VSPSGSYTHL LLERFLATFQ AKNKDVELST WNLNELPVGQ ISYNTQNAGT FFSVENSDKY IDALKAAHGV IILAPMTNFN YPATLKNFID HVFVANKTFK DKYVTKGASS GMLGNLKVVV LGSQGAPLGW YPWGDHVNSL RGLFGFAGVA SFASVIIDGT KLLYKDKSKS EVVDMFAKQV DAIANEF // ID CARDS_MYCPN Reviewed; 591 AA. AC P75409; Q1PD42; Q1PD43; Q1PD44; Q1PD45; Q1PD46; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=ADP-ribosylating toxin CARDS; DE EC=2.4.2.-; DE AltName: Full=ADP-ribosyltransferase CARDS; DE AltName: Full=CARDX TX; GN OrderedLocusNames=MPN_372; ORFNames=MP464; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF GLU-132. RC STRAIN=ATCC 29342 / M129, JL, L2, RJL1, and S1; RX PubMed=16617115; DOI=10.1073/pnas.0510644103; RA Kannan T.R., Baseman J.B.; RT "ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae RT represents unique virulence determinant among bacterial pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6724-6729(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN SFTPA. RC STRAIN=B9, and S1; RX PubMed=15845487; DOI=10.1128/IAI.73.5.2828-2834.2005; RA Kannan T.R., Provenzano D., Wright J.R., Baseman J.B.; RT "Identification and characterization of human surfactant protein A RT binding protein of Mycoplasma pneumoniae."; RL Infect. Immun. 73:2828-2834(2005). CC -!- FUNCTION: Acts as an ADP-ribosylating toxin, which may transfer CC the ADP-ribosyl group from NAD(+) to specific amino acids in CC target proteins. Elicits cytopathic effects in mammalian cells, CC such as disorganization and disruption of respiratory epithelial CC integrity in tracheal epithelium and vacuolization in the CC cytoplasm of CHO and HeLa cells. {ECO:0000269|PubMed:16617115}. CC -!- SUBUNIT: Binds to the pulmonary surfactant-associated protein A CC (SFTPA/SP-A), the major mammalian protein component of pulmonary CC surfactant. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16617115}; CC Peripheral membrane protein {ECO:0000269|PubMed:16617115}; CC Extracellular side {ECO:0000269|PubMed:16617115}. Note=Surface- CC associated protein. CC -!- SIMILARITY: Belongs to the bacterial exotoxin subunit A 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; DQ447746; ABE27142.1; -; Genomic_DNA. DR EMBL; DQ447747; ABE27143.1; -; Genomic_DNA. DR EMBL; DQ447748; ABE27144.1; -; Genomic_DNA. DR EMBL; DQ447749; ABE27145.1; -; Genomic_DNA. DR EMBL; DQ447750; ABE27146.1; -; Genomic_DNA. DR EMBL; U00089; AAB96112.1; -; Genomic_DNA. DR PIR; S73790; S73790. DR RefSeq; NP_110060.1; NC_000912.1. DR RefSeq; WP_010874728.1; NC_000912.1. DR PDB; 4TLV; X-ray; 1.90 A; A/B/C/D/E/F=1-591. DR PDB; 4TLW; X-ray; 2.55 A; A=1-591. DR PDBsum; 4TLV; -. DR PDBsum; 4TLW; -. DR ProteinModelPortal; P75409; -. DR EnsemblBacteria; AAB96112; AAB96112; MPN_372. DR GeneID; 877260; -. DR KEGG; mpn:MPN372; -. DR PATRIC; 20022118; VBIMycPne110_0403. DR OMA; DECTTHA; -. DR OrthoDB; EOG6NKQZB; -. DR BioCyc; MPNE272634:GJ6Z-392-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR003898; Borpert_toxA. DR Pfam; PF02917; Pertussis_S1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Glycosyltransferase; KW Membrane; Reference proteome; Toxin; Transferase; Virulence. FT CHAIN 1 591 ADP-ribosylating toxin CARDS. FT /FTId=PRO_0000210665. FT VARIANT 38 38 L -> P (in strain: S1). FT VARIANT 245 245 D -> G (in strain: L2). FT VARIANT 308 308 S -> P (in strain: S1). FT VARIANT 371 371 I -> S (in strain: S1, L2, RJL1 and JL). FT VARIANT 391 391 F -> S (in strain: S1). FT VARIANT 392 392 W -> R (in strain: RJL1). FT MUTAGEN 132 132 E->A: Reduces ADP-ribosylation activity. FT Unable to elicit vacuolization in CHO FT cells at 5 ug/ml. FT {ECO:0000269|PubMed:16617115}. FT STRAND 7 14 {ECO:0000244|PDB:4TLV}. FT HELIX 16 22 {ECO:0000244|PDB:4TLV}. FT HELIX 33 38 {ECO:0000244|PDB:4TLV}. FT TURN 39 41 {ECO:0000244|PDB:4TLV}. FT STRAND 45 53 {ECO:0000244|PDB:4TLV}. FT HELIX 54 58 {ECO:0000244|PDB:4TLV}. FT HELIX 59 62 {ECO:0000244|PDB:4TLV}. FT STRAND 65 68 {ECO:0000244|PDB:4TLV}. FT STRAND 74 82 {ECO:0000244|PDB:4TLV}. FT STRAND 87 89 {ECO:0000244|PDB:4TLV}. FT HELIX 90 102 {ECO:0000244|PDB:4TLV}. FT STRAND 106 111 {ECO:0000244|PDB:4TLV}. FT HELIX 113 124 {ECO:0000244|PDB:4TLV}. FT TURN 125 127 {ECO:0000244|PDB:4TLV}. FT HELIX 128 130 {ECO:0000244|PDB:4TLV}. FT STRAND 132 137 {ECO:0000244|PDB:4TLV}. FT HELIX 141 143 {ECO:0000244|PDB:4TLV}. FT STRAND 144 156 {ECO:0000244|PDB:4TLV}. FT TURN 157 159 {ECO:0000244|PDB:4TLV}. FT HELIX 163 165 {ECO:0000244|PDB:4TLV}. FT STRAND 169 173 {ECO:0000244|PDB:4TLV}. FT STRAND 197 200 {ECO:0000244|PDB:4TLV}. FT STRAND 204 208 {ECO:0000244|PDB:4TLV}. FT STRAND 211 217 {ECO:0000244|PDB:4TLV}. FT HELIX 226 229 {ECO:0000244|PDB:4TLV}. FT HELIX 243 246 {ECO:0000244|PDB:4TLV}. FT STRAND 249 256 {ECO:0000244|PDB:4TLV}. FT HELIX 257 259 {ECO:0000244|PDB:4TLV}. FT HELIX 265 269 {ECO:0000244|PDB:4TLV}. FT STRAND 276 279 {ECO:0000244|PDB:4TLV}. FT TURN 280 282 {ECO:0000244|PDB:4TLV}. FT STRAND 285 290 {ECO:0000244|PDB:4TLV}. FT TURN 292 294 {ECO:0000244|PDB:4TLV}. FT STRAND 296 301 {ECO:0000244|PDB:4TLV}. FT STRAND 315 318 {ECO:0000244|PDB:4TLV}. FT STRAND 323 327 {ECO:0000244|PDB:4TLV}. FT STRAND 335 340 {ECO:0000244|PDB:4TLV}. FT STRAND 348 354 {ECO:0000244|PDB:4TLV}. FT HELIX 360 362 {ECO:0000244|PDB:4TLV}. FT STRAND 364 368 {ECO:0000244|PDB:4TLV}. FT STRAND 375 380 {ECO:0000244|PDB:4TLV}. FT HELIX 381 383 {ECO:0000244|PDB:4TLV}. FT STRAND 388 393 {ECO:0000244|PDB:4TLV}. FT STRAND 398 401 {ECO:0000244|PDB:4TLW}. FT STRAND 404 410 {ECO:0000244|PDB:4TLV}. FT STRAND 415 423 {ECO:0000244|PDB:4TLV}. FT HELIX 429 432 {ECO:0000244|PDB:4TLV}. FT STRAND 441 443 {ECO:0000244|PDB:4TLV}. FT STRAND 447 450 {ECO:0000244|PDB:4TLV}. FT STRAND 453 457 {ECO:0000244|PDB:4TLV}. FT STRAND 463 466 {ECO:0000244|PDB:4TLV}. FT STRAND 472 476 {ECO:0000244|PDB:4TLV}. FT TURN 477 479 {ECO:0000244|PDB:4TLV}. FT STRAND 481 487 {ECO:0000244|PDB:4TLV}. FT STRAND 490 495 {ECO:0000244|PDB:4TLV}. FT STRAND 502 508 {ECO:0000244|PDB:4TLV}. FT STRAND 510 512 {ECO:0000244|PDB:4TLV}. FT HELIX 522 524 {ECO:0000244|PDB:4TLV}. FT STRAND 525 529 {ECO:0000244|PDB:4TLV}. FT STRAND 543 548 {ECO:0000244|PDB:4TLV}. FT TURN 549 551 {ECO:0000244|PDB:4TLV}. FT STRAND 554 558 {ECO:0000244|PDB:4TLV}. FT TURN 562 565 {ECO:0000244|PDB:4TLV}. FT STRAND 567 571 {ECO:0000244|PDB:4TLV}. FT STRAND 576 579 {ECO:0000244|PDB:4TLV}. FT TURN 586 589 {ECO:0000244|PDB:4TLV}. SQ SEQUENCE 591 AA; 68057 MW; B958C85C9EE29E90 CRC64; MPNPVRFVYR VDLRSPEEIF EHGFSTLGDV RNFFEHILST NFGRSYFIST SETPTAAIRF FGSWLREYVP EHPRRAYLYE IRADQHFYNA RATGENLLDL MRQRQVVFDS GDREMAQMGI RALRTSFAYQ REWFTDGPIA AANVRSAWLV DAVPVEPGHA HHPAGRVVET TRINEPEMHN PHYQELQTQA NDQPWLPTPG IATPVHLSIP QAASVADVSE GTSASLSFAC PDWSPPSSNG ENPLDKCIAE KIDNYNLQSL PQYASSVKEL EDTPVYLRGI KTQKTFMLQA DPQNNNVFLV EVNPKQKSSF PQTIFFWDVY QRICLKDLTG AQISLSLTAF TTQYAGQLKV HLSVSAVNAV NQKWKMTPQD IAITQFRVSS ELLGQTENGL FWNTKSGGSQ HDLYVCPLKN PPSDLEELQI IVDECTTHAQ FVTMRAASTF FVDVQLGWYW RGYYYTPQLS GWSYQMKTPD GQIFYDLKTS KIFFVQDNQN VFFLHNKLNK QTGYSWDWVE WLKHDMNEDK DENFKWYFSR DDLTIPSVEG LNFRHIRCYA DNQQLKVIIS GSRWGGWYST YDKVESNVED KILVKDGFDR F // ID CH10_MYCPN Reviewed; 116 AA. AC P75205; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=10 kDa chaperonin; DE AltName: Full=GroES protein; DE AltName: Full=Protein Cpn10; GN Name=groS; Synonyms=groES, mopB; OrderedLocusNames=MPN_574; GN ORFNames=MP268; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses CC the ATPase activity of the latter. {ECO:0000250}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GroES chaperonin 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; U00089; AAB95916.1; -; Genomic_DNA. DR PIR; S73594; S73594. DR RefSeq; NP_110263.1; NC_000912.1. DR RefSeq; WP_010874931.1; NC_000912.1. DR ProteinModelPortal; P75205; -. DR IntAct; P75205; 4. DR EnsemblBacteria; AAB95916; AAB95916; MPN_574. DR GeneID; 876761; -. DR KEGG; mpn:MPN574; -. DR PATRIC; 20022627; VBIMycPne110_0636. DR KO; K04078; -. DR OMA; MNITPIH; -. DR OrthoDB; EOG6GFGSD; -. DR BioCyc; MPNE272634:GJ6Z-620-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IPR011032; GroES-like. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 116 10 kDa chaperonin. FT /FTId=PRO_0000174790. SQ SEQUENCE 116 AA; 12618 MW; DBC4C83372334E52 CRC64; MKITPIHDNI LVSLVESNKE EVSQKGIITA LANPDKNESA HKGTVVALGA GPAYGKSEKP KYAFGIGDTI YFKEYSGISF EEEGTKYKII SLEDVLAFEK HGNTKTTTVK KGAKKK // ID CDD_MYCPN Reviewed; 133 AA. AC P75051; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Cytidine deaminase; DE Short=CDA; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; GN Name=cdd; OrderedLocusNames=MPN_065; ORFNames=MP089; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine CC and 2'-deoxycytidine for UMP synthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- CATALYTIC ACTIVITY: 2'deoxycytidine + H(2)O = 2'-deoxyuridine + CC NH(3). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CMP/dCMP-type deaminase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01083}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95737.1; -; Genomic_DNA. DR PIR; S73415; S73415. DR RefSeq; NP_109753.1; NC_000912.1. DR RefSeq; WP_010874422.1; NC_000912.1. DR ProteinModelPortal; P75051; -. DR IntAct; P75051; 1. DR EnsemblBacteria; AAB95737; AAB95737; MPN_065. DR GeneID; 877155; -. DR KEGG; mpn:MPN065; -. DR PATRIC; 20021409; VBIMycPne110_0066. DR OMA; IISPCAG; -. DR OrthoDB; EOG6XDH25; -. DR BioCyc; MPNE272634:GJ6Z-67-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR006262; Cyt_deam_tetra. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR01354; cyt_deam_tetra; 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; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 133 Cytidine deaminase. FT /FTId=PRO_0000171681. FT DOMAIN 3 131 CMP/dCMP-type deaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT REGION 43 45 Substrate binding. {ECO:0000250}. FT ACT_SITE 56 56 Proton donor. {ECO:0000250}. FT METAL 54 54 Zinc; catalytic. {ECO:0000250}. FT METAL 89 89 Zinc; catalytic. {ECO:0000250}. FT METAL 92 92 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 133 AA; 15185 MW; EC87E73810DEA9C7 CRC64; MKVDLDWVHH KLQEVVNHAY TPFSKFKVAC MLVANNQAFY GVNIENASYP VTLCAERSAI ANMVTSIGKA TIDYVFVYFD TKTPTNSPCG MCRQNIFEFA TDKTQLFCIE KDKSFKQFTI PEILKGGFRS YEQ // ID CDSA_MYCPN Reviewed; 395 AA. AC P75160; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative phosphatidate cytidylyltransferase; DE EC=2.7.7.41; DE AltName: Full=CDP-DAG synthase; DE AltName: Full=CDP-DG synthase; DE AltName: Full=CDP-diacylglycerol synthase; DE Short=CDS; DE AltName: Full=CDP-diglyceride pyrophosphorylase; DE AltName: Full=CDP-diglyceride synthase; DE AltName: Full=CTP:phosphatidate cytidylyltransferase; GN Name=cdsA; OrderedLocusNames=MPN_637; ORFNames=MP205; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP- CC diacylglycerol. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDS 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; U00089; AAB95853.1; -; Genomic_DNA. DR PIR; S73531; S73531. DR RefSeq; NP_110326.1; NC_000912.1. DR RefSeq; WP_010874994.1; NC_000912.1. DR EnsemblBacteria; AAB95853; AAB95853; MPN_637. DR GeneID; 876996; -. DR KEGG; mpn:MPN637; -. DR PATRIC; 20022755; VBIMycPne110_0700. DR KO; K00981; -. DR OMA; GWTTIFL; -. DR OrthoDB; EOG6TBHJT; -. DR BioCyc; MPNE272634:GJ6Z-683-MONOMER; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000808; 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: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 Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Nucleotidyltransferase; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 395 Putative phosphatidate FT cytidylyltransferase. FT /FTId=PRO_0000090740. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TRANSMEM 242 262 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. SQ SEQUENCE 395 AA; 44644 MW; 4AB163423C2E9EFB CRC64; MDLKDNSFAK KRSTVFVVLL IVFCFFLMFS AFADGFNFWS PWSTDFNSRV IHIKSDGNIE TTSIVSHELH PDFKAVRFAF GLVIVLFISV IAVLMNWELS NSIFKNYEKL NLSLSLLSGI MVSGGMIPTF FVIYFREWNA TVNWIWTASF AGMIVFLWAV YMISTSFIKI RPSLQVIYSL GAVICFIACI GTIYFSVIRG WTTIFLLIAI GVCTDTFAYL FGKRFGKNPL IKISPSKTWE GAFFGVTGTV LTISIICVLY SIPNYVRQPS IKDASKTALQ TPQNYDVHNL ITNVFLISFI SGGSTFYIYW WVSTLALIFT ASIFAIGGDL FFSYIKRLTK IKDFSKLLGK HGGILDRFDS SSFLISFFFI YHVIAGISSN QRLLMEPNTY FSAVS // ID CH60_MYCPN Reviewed; 543 AA. AC P78012; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. 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}, mopA; GN OrderedLocusNames=MPN_573; ORFNames=MP269; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 -!- INTERACTION: CC P75104:mnmE; NbExp=3; IntAct=EBI-2258565, EBI-2259625; 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; U00089; AAB95917.1; -; Genomic_DNA. DR PIR; S73595; S73595. DR RefSeq; NP_110262.1; NC_000912.1. DR RefSeq; WP_010874930.1; NC_000912.1. DR ProteinModelPortal; P78012; -. DR IntAct; P78012; 11. DR EnsemblBacteria; AAB95917; AAB95917; MPN_573. DR GeneID; 876804; -. DR KEGG; mpn:MPN573; -. DR PATRIC; 20022625; VBIMycPne110_0635. DR KO; K04077; -. DR OMA; KKQMDET; -. DR OrthoDB; EOG6JDWBZ; -. DR BioCyc; MPNE272634:GJ6Z-619-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 543 60 kDa chaperonin. FT /FTId=PRO_0000063445. SQ SEQUENCE 543 AA; 58086 MW; 74310494DD99A5C3 CRC64; MAKELVFGKN ARNKLLAGIN KLADAVKVTV GPKGQNVILG RKFSNPLITN DGVTIAKEIE LTDPLENIGA KVISVAAVST NDIAGDGTTT ATILAQEMTN RGVEAVNNGA NPVNVRRGIE DASQLIITEL DKRSKKINTN EEIEQVAAIS SGSKEIGKLI AQAMALVGKN GVITTDDAKT INTTLETTEG IEFKGTYASP YMVSDQEKME VVLDQPKILV SAMKINTIKE ILPLLEGSME NGNPLLIVAP DFAEEVVTTL AVNKLRGTIN VVAVKCNEYG ERQKAALEDL AISTGTLAYN NELGGGFKDV TVNHLGEARR VQVAKEKTTV IGGKGSKETI QKHLDLLNGR LKQTTEKYDT DLLKERIAHL SQGVAVVRVG GATELAQKEL KLRIEDALNS TKAAVEEGII SGGGIALLNV STILNDSKLA DKYKAETSAE NLKEILVGYE IVRKSLEAPV RQIIENSGVN PVKVFAELRS EADGVGFDAE TKKKVDMIRS GIIDPTKVTK TALEKAASVA SSLITTSVAV YDIKENKEGS FQE // ID CLPB_MYCPN Reviewed; 715 AA. AC P75247; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Chaperone protein ClpB; GN Name=clpB; OrderedLocusNames=MPN_531; ORFNames=MP311; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is CC involved in the recovery of the cell from heat-induced damage, in CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the CC processing of protein aggregates. Protein binding stimulates the CC ATPase activity; ATP hydrolysis unfolds the denatured protein CC aggregates, which probably helps expose new hydrophobic binding CC sites on the surface of ClpB-bound aggregates, contributing to the CC solubilization and refolding of denatured protein aggregates by CC DnaK (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal domain probably functions as a substrate- CC discriminating domain, recruiting aggregated proteins to the ClpB CC hexamer and/or stabilizing bound proteins. The NBD2 domain is CC responsible for oligomerization, whereas the NBD1 domain CC stabilizes the hexamer probably in an ATP-dependent manner. The CC movement of the coiled-coil domain is essential for ClpB ability CC to rescue proteins from an aggregated state, probably by pulling CC apart large aggregated proteins, which are bound between the CC coiled-coils motifs of adjacent ClpB subunits in the functional CC hexamer (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95959.1; -; Genomic_DNA. DR PIR; S73637; S73637. DR RefSeq; NP_110220.1; NC_000912.1. DR RefSeq; WP_010874888.1; NC_000912.1. DR ProteinModelPortal; P75247; -. DR SMR; P75247; 13-207. DR IntAct; P75247; 1. DR PRIDE; P75247; -. DR EnsemblBacteria; AAB95959; AAB95959; MPN_531. DR GeneID; 877405; -. DR KEGG; mpn:MPN531; -. DR PATRIC; 20022537; VBIMycPne110_0592. DR OMA; PVERILM; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; MPNE272634:GJ6Z-576-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; 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; 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 PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; Repeat; Stress response. FT CHAIN 1 715 Chaperone protein ClpB. FT /FTId=PRO_0000191145. FT NP_BIND 60 67 ATP 1. {ECO:0000250}. FT NP_BIND 466 473 ATP 2. {ECO:0000250}. FT REGION 14 196 NBD1. {ECO:0000250}. FT REGION 197 406 Linker. {ECO:0000250}. FT REGION 416 618 NBD2. {ECO:0000250}. FT REGION 619 715 C-terminal. {ECO:0000250}. FT COILED 247 385 {ECO:0000250}. SQ SEQUENCE 715 AA; 81396 MW; 1F1C69E51201FDE2 CRC64; MDFSFTPTPD KRDFLKEMGR SINDEVLKNK VDPIIGRDNE IRRLIEILSR KNKNNPVLIG EPGVGKTAIV EGFVRRVVNN DVPLNLRDVE IYELSLSGLI AGTQYQGEFE KRVNGILKQV KESNGKIILF IDEIHQIVGL GRNSSSGAMD IANILKPMLA RGEIKVIGAT TLKEYREYVE KDGALERRFQ KILVSEPSQQ EALTIMRGLK TRWELFHNLT IFDSALVAAV EMSARYIPDR NLPDKAIDLI DEASAKIKTE MASEPVVIDT LKREIINLET EYAALKQDKE NADNKKKQGH LDNLKQQLDE LKKKRDSLTA EWKKEKTNFE SINKLKKEIE DLQTRLELYQ TEGNYEAASK ILYYDIPKLK NQLEQAQKKY VDSKHDLFKT EVSENEVAEV VSQATGIPLK KLLETEKEKL LHLGDEIKKR VKGQDAAVET VVNTVMRGRV NLNDPNRPIG SFIFLGSTGV GKTELAKSLA EVLFDNEKAM IRFDMSEYME KHSVAKLIGA PPGYVGYEQS GLLTEAVRRK PYCVLLFDEI EKAHPDVTNI LLQVLDDGTL KDSQGRLVNF KNTMIIMTSN LGSNYIMENK RDLAMEALKK HFRAEFINRI DEIVFFSVLQ KTTVLEIITN LLDQLNQRLA KQNLKFTFDP KLNEFIYKSS FDEQFGARPI KRFIDRQIAT LIAKQILEGI ITKDVSYNVI VEKDKVAIVA NKVKS // ID COAE_MYCPN Reviewed; 200 AA. AC P75400; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; GN Name=coaE; OrderedLocusNames=MPN_382; ORFNames=MP455; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group CC of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 5/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96103.1; -; Genomic_DNA. DR PIR; S73781; S73781. DR RefSeq; NP_110070.1; NC_000912.1. DR RefSeq; WP_010874738.1; NC_000912.1. DR ProteinModelPortal; P75400; -. DR EnsemblBacteria; AAB96103; AAB96103; MPN_382. DR GeneID; 877392; -. DR KEGG; mpn:MPN382; -. DR KO; K00859; -. DR OMA; AVMLNYW; -. DR OrthoDB; EOG6TR0JH; -. DR BioCyc; MPNE272634:GJ6Z-403-MONOMER; -. DR UniPathway; UPA00241; UER00356. DR Proteomes; UP000000808; 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 1 200 Dephospho-CoA kinase. FT /FTId=PRO_0000172962. FT DOMAIN 2 200 DPCK. FT NP_BIND 7 14 ATP. {ECO:0000255}. SQ SEQUENCE 200 AA; 22910 MW; 396EA0C4AA940589 CRC64; MLIAVVGKAG VGKTTVLQYI ADYFHFPVFF ADRFIHQQYA NGQAGYAIVK QQFGAQFVNH EAVDRKQLAQ YVFNQPDELK RLSNLTKPLV QEWLNQLKAQ FQDKIALVEI AVMLNYWNDY RPFFDEVIQI ERDAKIVKQA LKARGVDVEQ VQKLIADPTY PILTVINNST VAECALHVTQ FLESIAKSDK CHHGHYQTPK // ID CSD_MYCPN Reviewed; 408 AA. AC P75298; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable cysteine desulfurase; DE EC=2.8.1.7; GN Name=csd; OrderedLocusNames=MPN_487; ORFNames=MP355; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium CC atoms from L-cysteine, L-cystine, L-selenocysteine, and L- CC selenocystine to produce L-alanine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S- CC sulfanyl-acceptor. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. Csd 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; U00089; AAB96003.1; -; Genomic_DNA. DR PIR; S73681; S73681. DR RefSeq; NP_110175.1; NC_000912.1. DR RefSeq; WP_010874843.1; NC_000912.1. DR ProteinModelPortal; P75298; -. DR IntAct; P75298; 2. DR EnsemblBacteria; AAB96003; AAB96003; MPN_487. DR GeneID; 877233; -. DR KEGG; mpn:MPN487; -. DR PATRIC; 20022398; VBIMycPne110_0526. DR KO; K11717; -. DR OMA; HGRHDVQ; -. DR OrthoDB; EOG68DD0M; -. DR BioCyc; MPNE272634:GJ6Z-528-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. 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 SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 408 Probable cysteine desulfurase. FT /FTId=PRO_0000150300. FT MOD_RES 225 225 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 408 AA; 46483 MW; 0D0AF371A2AFE26F CRC64; MTKTKFNPYQ FRKQFKWFKN NPQWVNFDNA ATSIALDTVS QACKEYYELF SVNPHNKTPD LNNQIIAIIA ETRQLVADWF NVTALEIIFT SSATESINLF AHGLKPWIKP GDEIVLKGDE HSANVLPWVA LAKQTKARLV WVEKQANQSL EDTFKSLINP KTKVVAITAT SNLFGNSIDF AQIADYLKQV NPKAFVAVDA VQTVQHKQID IAKTQIDFLA FSTHKFYGPT GLGVAYIKKS LQPQLQPLKL GGDIFTQIDP DNTIHFKSTP LKFEAGTPNI MAIYALNKLL RFFKQKFNFA QMMAYGHQLK QQAYELLNSN PQIVLANHDQ DVPIFSFKHR QLATIDLATF LNINKIMVRQ GSICVGRYRN KDYFVRVSLM HYNTVKELQY LAKLLATDTK TIIKNVIK // ID DACB_MYCPN Reviewed; 202 AA. AC P75528; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_00838}; DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00838}; DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00838}; DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838}; DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838}; GN Name=dacB {ECO:0000255|HAMAP-Rule:MF_00838}; GN OrderedLocusNames=MPN_244; ORFNames=K04_orf202, MP588; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into CC cyclic di-AMP (c-di-AMP), a second messenger used to regulate CC differing processes in different bacteria. {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC -!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'- CC adenylate. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SUBUNIT: Probably oligomerizes. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00838}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacB/CdaS CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SIMILARITY: Contains 1 DAC domain. {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96236.1; -; Genomic_DNA. DR PIR; S73914; S73914. DR RefSeq; NP_109932.1; NC_000912.1. DR RefSeq; WP_010874601.1; NC_000912.1. DR ProteinModelPortal; P75528; -. DR EnsemblBacteria; AAB96236; AAB96236; MPN_244. DR GeneID; 876807; -. DR KEGG; mpn:MPN244; -. DR PATRIC; 20021813; VBIMycPne110_0263. DR OMA; NTNAGRV; -. DR OrthoDB; EOG6DRPM4; -. DR BioCyc; MPNE272634:GJ6Z-251-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR HAMAP; MF_00838; DacB; 1. DR InterPro; IPR014046; c-di-AMP_synthase-like. DR InterPro; IPR003390; DNA_integrity_scan_DisA_N. DR Pfam; PF02457; DisA_N; 1. DR PIRSF; PIRSF004793; UCP004793; 1. DR TIGRFAMs; TIGR00159; TIGR00159; 1. DR PROSITE; PS51794; DAC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 202 Diadenylate cyclase. FT /FTId=PRO_0000210418. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00838}. FT DOMAIN 29 185 DAC. {ECO:0000255|HAMAP-Rule:MF_00838}. SQ SEQUENCE 202 AA; 22733 MW; F2E3F12431ADCE18 CRC64; MMTVEVFSVI ILVLLFLILA LTLLFVLLNK RTRSFVIRTF TGLFRSKHTT SQKNFYDNLT STLLRLSTDK IGAIIAIENQ DSLESYVNIG YRVTSDFSPE LLVTIFYNKQ SPLHDGAVIV RDYQIVSVSS YFPMTRQLID VSYGSRHRSA LGLTEKCDAI VFIVSETTGK ISVAVRGVIK TLSSNSDRLQ DQIIHYLTVK PG // ID DEOC_MYCPN Reviewed; 224 AA. AC P09924; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=Deoxyribose-phosphate aldolase; DE Short=DERA; DE EC=4.1.2.4; DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase; DE AltName: Full=Phosphodeoxyriboaldolase; DE Short=Deoxyriboaldolase; GN Name=deoC; OrderedLocusNames=MPN_063; ORFNames=MP091; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=2492658; DOI=10.1093/nar/17.2.801; RA Loechel S., Inamine J.M., Hu P.-C.; RT "Nucleotide sequence of the deoC gene of Mycoplasma pneumoniae."; RL Nucleic Acids Res. 17:801-801(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes a reversible aldol reaction between CC acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- CC D-ribose 5-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D- CC glyceraldehyde 3-phosphate + acetaldehyde. CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2- CC deoxy-alpha-D-ribose 1-phosphate: step 2/2. CC -!- INTERACTION: CC P75067:MPN_047; NbExp=1; IntAct=EBI-2260368, EBI-2260365; CC P78030:MPN_307; NbExp=1; IntAct=EBI-2260368, EBI-2260448; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13544; CAA31897.1; -; Genomic_DNA. DR EMBL; U00089; AAB95739.1; -; Genomic_DNA. DR PIR; S02216; S02216. DR RefSeq; NP_109751.1; NC_000912.1. DR RefSeq; WP_010874420.1; NC_000912.1. DR ProteinModelPortal; P09924; -. DR IntAct; P09924; 2. DR EnsemblBacteria; AAB95739; AAB95739; MPN_063. DR GeneID; 876837; -. DR KEGG; mpn:MPN063; -. DR PATRIC; 20021405; VBIMycPne110_0064. DR KO; K01619; -. DR OMA; FFSVCVN; -. DR OrthoDB; EOG6QZMW5; -. DR BioCyc; MetaCyc:MONOMER-641; -. DR BioCyc; MPNE272634:GJ6Z-65-MONOMER; -. DR UniPathway; UPA00002; UER00468. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00114; DeoC_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase. DR InterPro; IPR028581; DeoC_typeI. DR PANTHER; PTHR10889; PTHR10889; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF001357; DeoC; 1. DR SMART; SM01133; DeoC; 1. DR TIGRFAMs; TIGR00126; deoC; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Lyase; Reference proteome; Schiff base. FT CHAIN 1 224 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057245. FT ACT_SITE 152 152 Schiff-base intermediate with FT acetaldehyde. {ECO:0000250}. FT ACT_SITE 181 181 {ECO:0000250}. SQ SEQUENCE 224 AA; 24878 MW; 73C3E4932E7881F7 CRC64; MKLEYNRIID STLLKADTLP HEIDALCADA HKYQFYAVCV NPSYVRYAKN ILKGTGVKLC TVVGFPLGQT TQRQKVYETK IAIKEGADEI DMVMNIAEFK KRCACVISEI RAVKKVCGKR TLKVIIETAL LNQDEIRDAV NVCIDGNADF VKTSTGFSMR GASLEDITIM REASGNLIKI KASGGVQTAQ QFLDFFNAGV SRIGTSNAVK IMEELHKLES HEHR // ID DEOD_MYCPN Reviewed; 238 AA. AC P75053; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 91. DE RecName: Full=Purine nucleoside phosphorylase DeoD-type; DE Short=PNP; DE EC=2.4.2.1; GN Name=deoD; OrderedLocusNames=MPN_062; ORFNames=MP092; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. CC -!- CATALYTIC ACTIVITY: Purine deoxynucleoside + phosphate = purine + CC 2'-deoxy-alpha-D-ribose 1-phosphate. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase 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; U00089; AAB95740.1; -; Genomic_DNA. DR PIR; S73418; S73418. DR RefSeq; NP_109750.1; NC_000912.1. DR RefSeq; WP_010874419.1; NC_000912.1. DR ProteinModelPortal; P75053; -. DR IntAct; P75053; 1. DR EnsemblBacteria; AAB95740; AAB95740; MPN_062. DR GeneID; 876955; -. DR KEGG; mpn:MPN062; -. DR PATRIC; 20021403; VBIMycPne110_0063. DR KO; K03784; -. DR OMA; ELTICST; -. DR OrthoDB; EOG6BKJC5; -. DR BioCyc; MetaCyc:MONOMER-561; -. DR BioCyc; MPNE272634:GJ6Z-64-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1580; -; 1. DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1. DR InterPro; IPR004402; DeoD-type. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR018016; Nucleoside_phosphorylase_CS. 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; TIGR00107; deoD; 1. DR PROSITE; PS01232; PNP_UDP_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 238 Purine nucleoside phosphorylase DeoD- FT type. FT /FTId=PRO_0000063148. FT REGION 87 90 Phosphate binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 181 183 Purine nucleoside binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 205 206 Purine nucleoside binding. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 4 4 Purine nucleoside; shared with dimeric FT partner. {ECO:0000250|UniProtKB:P50389}. FT BINDING 20 20 Phosphate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 24 24 Phosphate. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 43 43 Phosphate; shared with dimeric partner. FT {ECO:0000250|UniProtKB:P50389}. SQ SEQUENCE 238 AA; 26284 MW; 8F1A8E30F47FA5D9 CRC64; MTPHINAKKD DIAKVVLMPG DPLRAKWIAE QFMEKPRLVN EVRGMLAFTG QYKGKTITIM GHGMGIPSIG IYSYELMKFY EVNTIIRIGS CGALQGSLNL QDLIIAAKAW SESIYANDMG VEVPADKILM ASPQLVELAK KTANQLQLAF HEGLVFCEDA FHQIRKDVLK LAQEKHALAV EMEAHALYAN AMLLNKQALT MLTVSDSLVT HAALPAEQRQ ATFKNMAILS LEMASQLV // ID DEF_MYCPN Reviewed; 216 AA. AC P75527; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; OrderedLocusNames=MPN_245; ORFNames=MP587; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate + CC methionyl peptide. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000250}; CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2259869, EBI-2259869; CC -!- SIMILARITY: Belongs to the polypeptide deformylase 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; U00089; AAB96235.1; -; Genomic_DNA. DR PIR; S73913; S73913. DR RefSeq; NP_109933.1; NC_000912.1. DR RefSeq; WP_010874602.1; NC_000912.1. DR ProteinModelPortal; P75527; -. DR IntAct; P75527; 1. DR EnsemblBacteria; AAB96235; AAB96235; MPN_245. DR GeneID; 876781; -. DR KEGG; mpn:MPN245; -. DR PATRIC; 20021815; VBIMycPne110_0264. DR KO; K01462; -. DR OMA; YHYLLIN; -. DR OrthoDB; EOG6PZXGQ; -. DR BioCyc; MPNE272634:GJ6Z-252-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Hydrolase; Iron; Metal-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 216 Peptide deformylase. FT /FTId=PRO_0000082803. FT ACT_SITE 179 179 {ECO:0000250}. FT METAL 134 134 Iron. {ECO:0000250}. FT METAL 178 178 Iron. {ECO:0000250}. FT METAL 182 182 Iron. {ECO:0000250}. SQ SEQUENCE 216 AA; 24592 MW; 361F434048B505DF CRC64; MTKILPVSTI SIFRIILILP QINMELLPTK AWLVLDDVKE INEPTKPVQF PLDQASLDCI AKMMAYVDAS YNGDAEKYGI IPGIGIAANQ IGYWKQMFYI HLMDGGVEHK CLLINPKIIN LSANKSFLKS GEGCLSVPKM HQGYVIRHEW ITITGFDWLQ QKEITITATG LFGMCLQHEF DHLQGRFYYH RINPLNPLFT NKEWKVINPA LPSDSE // ID DNAG_MYCPN Reviewed; 620 AA. AC P75426; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974}; GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; Synonyms=dnaE; GN OrderedLocusNames=MPN_353; ORFNames=MP483; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA CC molecules used as primers for DNA polymerase during DNA CC replication. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core CC domain that contains the primase activity, and a C-terminal DnaB- CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Belongs to the DnaG primase family. CC {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96131.1; -; Genomic_DNA. DR PIR; S73809; S73809. DR RefSeq; NP_110041.1; NC_000912.1. DR RefSeq; WP_010874709.1; NC_000912.1. DR ProteinModelPortal; P75426; -. DR IntAct; P75426; 5. DR EnsemblBacteria; AAB96131; AAB96131; MPN_353. DR GeneID; 876866; -. DR KEGG; mpn:MPN353; -. DR PATRIC; 20022066; VBIMycPne110_0380. DR KO; K02316; -. DR OMA; MMESAIT; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; MPNE272634:GJ6Z-370-MONOMER; -. DR Proteomes; UP000000808; 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; 3.90.580.10; -; 1. DR Gene3D; 3.90.980.10; -; 1. DR HAMAP; MF_00974; DNA_primase_DnaG; 1. DR InterPro; IPR013264; DNA_primase_core_N. DR InterPro; IPR006295; DNA_primase_DnaG. DR InterPro; IPR030846; DnaG_bac. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR002694; Znf_CHC2. DR Pfam; PF08275; Toprim_N; 1. DR Pfam; PF01807; zf-CHC2; 1. DR SMART; SM00493; TOPRIM; 1. DR SMART; SM00400; ZnF_CHCC; 1. DR TIGRFAMs; TIGR01391; dnaG; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Primosome; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 620 DNA primase. FT /FTId=PRO_0000180502. FT DOMAIN 266 350 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT ZN_FING 38 62 CHC2-type. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 272 272 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 319 319 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 319 319 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 321 321 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. SQ SEQUENCE 620 AA; 71537 MW; 0250C70BD779CA58 CRC64; MTSPTSLDQL KQQIKIAPIV EHYAIKLKKK GKDFVALCPF HADQNPSMTV SVAKNIFKCF SCQVGGDGIA FIQKIDQVDW KTALNKALSI LNLDSQYAVN FYLKEVDPKL KRYWDLHSAL VDYYQTRLKL EPKEQGLTYL TETRKLSPQV IERFQLGLAF TLEDQYFLPS LLNYPWISPA IEKAELCFAT EKFPEALGFF NQQTHYATFK SRIMIPIHDL KGNPVGFSGR ALQKTEKIKY KNSAEHQWFK KSELLFNFHR IDKNTLKLYL VEGYFDVFAL TSAGIGDVVG LMGLALSESH IIAFQQQLKA LETVVLALDN DTAGHDATFK LLQELNAHGI IVEVVDWNQA AYKDWDELFL AEGSDAVKAK THRVLNLVEY LVAYFKTKGF DERITVNKVI DIIAQNQKVT ADTSFSRFLC QKLQQLLQYS DVETLFTQLQ QQKLKVKVNK TTTFTQRAPI YESVVGVVDN SFRNESQPVA ITKEFLVENN WKETKERVFH AEIFAYVLLD KQFLVELKQS DLDELFASLQ TPLFDVALFI DKARLYWAKV QEPDWAVFNS ILGEQQAMFP TTFLAQIKEF FLNKSLSYDP EDYEEDLQFF RQLIVKQKEL LKYFKSMVEH // ID DER_MYCPN Reviewed; 449 AA. AC P75309; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 20-JAN-2016, entry version 98. DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195}; DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195}; GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA; GN OrderedLocusNames=MPN_475; ORFNames=MP366; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngA (Der) GTPase family. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Contains 2 EngA-type G (guanine nucleotide-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00195}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34744.1; -; Genomic_DNA. DR PIR; S73692; S73692. DR RefSeq; NP_110163.1; NC_000912.1. DR RefSeq; WP_010874831.1; NC_000912.1. DR ProteinModelPortal; P75309; -. DR IntAct; P75309; 1. DR EnsemblBacteria; AAG34744; AAG34744; MPN_475. DR GeneID; 877196; -. DR KEGG; mpn:MPN475; -. DR PATRIC; 20022374; VBIMycPne110_0514. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; MPNE272634:GJ6Z-516-MONOMER; -. DR Proteomes; UP000000808; 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; 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 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 1 449 GTPase Der. FT /FTId=PRO_0000179014. FT DOMAIN 2 169 EngA-type G 1. FT DOMAIN 180 355 EngA-type G 2. FT DOMAIN 356 440 KH-like. {ECO:0000255|HAMAP- FT Rule:MF_00195}. FT NP_BIND 8 15 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 55 59 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 118 121 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 186 193 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 233 237 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 298 301 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. SQ SEQUENCE 449 AA; 50145 MW; 73BDC1A49AF1F8E5 CRC64; MFTVAIIGRP NVGKSSLFNR LIQKPYAIIS DTPNTTRDRI YGVGEWLTRQ IAFIDTGGLI SQKTPLQQQI EVQVRAALSQ ANAIIFLVSY QEQISSDDFY VAKVLKKIKD KPILLVVNKS ENLKPDAYEP NLQQFYSFGF GQPVCVSASH GIGIGNLMDR LVKDNQLPPY HGSSETNPEV RFCVIGKPNV GKSSLINQLV QQNRVLVSDE SGTTRDAIDI PLRVNGQNYL LIDTAGIRRK GKIAPGIEAA SYGKTQLAIA RSNIILLMVD GSKPLSEQDE IIGGLAQAAL IPVIILVNKW DLVQKDSNTM AKFKKQLQSQ FQHLSFAPIV FISVKNNKRL HTIFEQLQII QEQLTKKIST SLLNDVIQQA QLFNQAPLFK GGRLQVTYAV QTHSQTPHFV LFCNDPKFVH FSYARFLENK IRESFGFSAV PITLYFKSKN ARIRGVAKT // ID DNAJL_MYCPN Reviewed; 309 AA. AC Q50312; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=DnaJ-like protein MG002 homolog; GN OrderedLocusNames=MPN_002; ORFNames=MP152; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE- CC ProRule:PRU00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34816; AAC43644.1; -; Genomic_DNA. DR EMBL; U00089; AAG34740.1; -; Genomic_DNA. DR PIR; S62835; S62835. DR RefSeq; NP_109690.1; NC_000912.1. DR RefSeq; WP_010874359.1; NC_000912.1. DR ProteinModelPortal; Q50312; -. DR IntAct; Q50312; 7. DR EnsemblBacteria; AAG34740; AAG34740; MPN_002. DR GeneID; 877164; -. DR KEGG; mpn:MPN002; -. DR PATRIC; 20021277; VBIMycPne110_0002. DR OMA; EIWHEEL; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; MPNE272634:GJ6Z-2-MONOMER; -. DR Proteomes; UP000000808; Chromosome. 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 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 309 DnaJ-like protein MG002 homolog. FT /FTId=PRO_0000071001. FT DOMAIN 1 66 J. {ECO:0000255|PROSITE- FT ProRule:PRU00286}. SQ SEQUENCE 309 AA; 37132 MW; AF29BC4EABCF99AC CRC64; MTLYDLLELP QTATLQEIKT AYKRLAKRYH PDINKQGADT FVKINNAYAV LSDTTQKAEY DAMLRFSEFE DRVKRLDFSI KWHEQFMEEL QFHHNWDFDF IRNREYTQPT PTNNKYSSFL DKDVSLAFYQ LYSKGKLDFD LEDTLLRRHS IKQAFLKGKK LNDVLKEQYN YLGWLEAKRY FNIDVEIELT PKEVREGGVV NLPLKIKVIS NNYPGQMWYE LNKNYSFRLL WDIKNGEVAE FFGKGNRALG WRGDLIVRMR IVDKIKKRLR IFSSHFEQDK TKLWFLVPQD KQDNPNKWVF DYKTHEFIV // ID DNAA_MYCPN Reviewed; 439 AA. AC Q59549; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Chromosomal replication initiator protein DnaA; GN Name=dnaA; OrderedLocusNames=MPN_686; ORFNames=MP156; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Plays an important role in the initiation and regulation CC of chromosomal replication. Binds to the origin of replication; it CC binds specifically double-stranded DNA at a 9 bp consensus (dnaA CC box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic CC phospholipids (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34816; AAC43648.1; -; Genomic_DNA. DR EMBL; U00089; AAB95804.1; -; Genomic_DNA. DR PIR; S62793; S62793. DR RefSeq; NP_110375.1; NC_000912.1. DR RefSeq; WP_010875043.1; NC_000912.1. DR ProteinModelPortal; Q59549; -. DR SMR; Q59549; 1-100. DR IntAct; Q59549; 3. DR EnsemblBacteria; AAB95804; AAB95804; MPN_686. DR GeneID; 877037; -. DR KEGG; mpn:MPN686; -. DR PATRIC; 20022861; VBIMycPne110_0753. DR KO; K02313; -. DR OMA; AVGNSIM; -. DR OrthoDB; EOG689HR1; -. DR BioCyc; MPNE272634:GJ6Z-732-MONOMER; -. DR Proteomes; UP000000808; 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; 3.30.300.20; -; 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; IPR015946; KH_dom-like_a/b. 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 1 439 Chromosomal replication initiator protein FT DnaA. FT /FTId=PRO_0000114216. FT NP_BIND 141 148 ATP. {ECO:0000255}. SQ SEQUENCE 439 AA; 50624 MW; 931A42DEB2A07ECA CRC64; MEQFSAFKLL LKKQYETTLG FYDKYIKNLK RFALKNNVLF VIVDNEFARE TLNSNPDIVG LASKLYDDIR AVRFVNEQDF FINLAKLEED NRETLYQSSG LSKNFTFKNF VVGDGNRRVY EAGVRISETQ DADFSPLFIY GETGLGKTHL LQAIGNDKFF HFPNAKVKYV VSSDFAQEVV NAFYQKEKDQ GIEKLKAAYE SLDLLLIDDT QIFGKKEKTL EILFSIFNNL VSKGKQIVFV SDKTPDELAN IDPRMVSRFK SGLLLKIEKH NLSSLCEILA VKLKEKDPNI QITNEAREKA AQISGNDVRS LNGIATKLLF YVKTTKQNLI NNDNLKEILF EEFEKFHKKS FDPYLLIENV CRRFNVPVDS VLSENRKAEL VRVRDVCNYI LREKYKMQFQ QIGKIFKRNH STVVAAVKRV AKMIEKDDSL QDIITSLVI // ID DNAB_MYCPN Reviewed; 473 AA. AC P75539; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Replicative DNA helicase; DE EC=3.6.4.12; GN Name=dnaB; OrderedLocusNames=MPN_232; ORFNames=MP599; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Participates in initiation and elongation during CC chromosome replication; it exhibits DNA-dependent ATPase activity. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SF4 helicase domain. {ECO:0000255|PROSITE- CC ProRule:PRU00596}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96247.1; -; Genomic_DNA. DR PIR; S73925; S73925. DR RefSeq; NP_109920.1; NC_000912.1. DR RefSeq; WP_010874589.1; NC_000912.1. DR ProteinModelPortal; P75539; -. DR IntAct; P75539; 2. DR EnsemblBacteria; AAB96247; AAB96247; MPN_232. DR GeneID; 877069; -. DR KEGG; mpn:MPN232; -. DR PATRIC; 20021789; VBIMycPne110_0251. DR KO; K02314; -. DR OMA; KKASIFR; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; MPNE272634:GJ6Z-239-MONOMER; -. DR Proteomes; UP000000808; 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; 3.40.50.300; -; 1. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03796; DnaB_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; DNA-binding; KW Helicase; Hydrolase; Nucleotide-binding; Primosome; KW Reference proteome. FT CHAIN 1 473 Replicative DNA helicase. FT /FTId=PRO_0000102026. FT DOMAIN 191 469 SF4 helicase. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. FT NP_BIND 222 229 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. SQ SEQUENCE 473 AA; 54490 MW; 2E265A35D972C872 CRC64; MVSNKLEQTF KFANDKNIER AERVLMQALV QDAVGVDLIL TKLEPKDFFG FPFNFIFQTA QENYSEGNKL FGSALLEAVK FKLDTDSKTQ REIEGLFEDV LLKGLPFLER DIKVFVDVVK KASIFRQLKQ FAKKVEKEEF KVKDDRFEGY LQAIQNDFTK IIHSAFVSIP GLSYDEIVRE EEELIPKVYR GELTVKGLKS GFYPLDQLTS GWKEGELIVV AARPGRGKTA LLINFLQGAV NDSEKFDKNK DVLLFFSLEM RNREIYQRHL MLESQVNYTL TSRQRLANVY DDLIKASEVL RDLPIKIFDY STITLDEIRA QITEVSKTNN VKLVVIDYLQ LVNAFKNSYN ISRQQEVTMI SKSLKSFAKE FNVPIIAAAQ LSRRIEERKD SRPILSDLRE SGSIEQDADM VLFIHRVKDE DSENQEAIGH NNIFQVELIL EKNRSGPTGK VQFDFQSDVS TFRVREYNPD GYS // ID DLDH_MYCPN Reviewed; 457 AA. AC P75393; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Dihydrolipoyl dehydrogenase; DE EC=1.8.1.4; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE AltName: Full=E3 component of pyruvate complex; GN Name=pdhD; OrderedLocusNames=MPN_390; ORFNames=MP448; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha- CC ketoacid dehydrogenase complexes. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase 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; U00089; AAB96096.1; -; Genomic_DNA. DR PIR; S73774; S73774. DR RefSeq; NP_110078.1; NC_000912.1. DR RefSeq; WP_010874746.1; NC_000912.1. DR ProteinModelPortal; P75393; -. DR IntAct; P75393; 2. DR EnsemblBacteria; AAB96096; AAB96096; MPN_390. DR GeneID; 877059; -. DR KEGG; mpn:MPN390; -. DR PATRIC; 20022156; VBIMycPne110_0421. DR KO; K00382; -. DR OMA; VEVMPTI; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; MetaCyc:MONOMER-585; -. DR BioCyc; MPNE272634:GJ6Z-412-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; -; 2. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; KW Glycolysis; NAD; Oxidoreductase; Redox-active center; KW Reference proteome. FT CHAIN 1 457 Dihydrolipoyl dehydrogenase. FT /FTId=PRO_0000068032. FT NP_BIND 32 40 FAD. {ECO:0000250}. FT NP_BIND 178 182 NAD. {ECO:0000250}. FT NP_BIND 262 265 NAD. {ECO:0000250}. FT ACT_SITE 437 437 Proton acceptor. {ECO:0000250}. FT BINDING 49 49 FAD. {ECO:0000250}. FT BINDING 113 113 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 235 235 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 303 303 FAD. {ECO:0000250}. FT BINDING 311 311 FAD; via amide nitrogen. {ECO:0000250}. FT DISULFID 40 45 Redox-active. {ECO:0000250}. SQ SEQUENCE 457 AA; 49437 MW; EB044FD676F3F28E CRC64; MNYDLIIIGA GPAGYVAAEY AGKHKLKTLV VEKEYFGGVC LNVGCIPTKT LLKRAKIVDY LRHAQDYGIS INGQVALNWN QLLEQKGKVV SKLVGGVKAI IASAKAETVM GEAKVLDPNT VEVAGKTYTT KSIVVATGSR PRYLTLPGFA EARQNGFVID STQALSLEGV PRKLVVVGGG VIGIEFAFLY ASLGSEVTIL QGVDRILEIF DTEVSDLVAK LLQTKNVKII TNAQVTRANN NEVFYSQNGQ EGSVVGDRIL VSIGRIPNTE CLDGLNLQRD ERNRIVLNQD LQTSIPNIYI VGDANAQLML AHFAYQQGRY AVNHILNKKQ VKPAQKLTCP SCIYTNPEVA SVGYTEMELK KQGIPYVKTN LVLAHCGKAI ADNETNGFVK MMFDPQTGKI LGCCIIAATA SDMIAELALA MGAGLTVFDI ANSISPHPTI NEMIADVCKK ALFDHFK // ID DNAJM_MYCPN Reviewed; 910 AA. AC P75354; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=DnaJ-like protein MG200 homolog; GN OrderedLocusNames=MPN_119; ORFNames=MP035; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE- CC ProRule:PRU00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95683.1; -; Genomic_DNA. DR PIR; S73361; S73361. DR RefSeq; NP_109807.1; NC_000912.1. DR RefSeq; WP_010874476.1; NC_000912.1. DR ProteinModelPortal; P75354; -. DR EnsemblBacteria; AAB95683; AAB95683; MPN_119. DR GeneID; 876757; -. DR KEGG; mpn:MPN119; -. DR PATRIC; 20021537; VBIMycPne110_0126. DR OMA; TTSAVEM; -. DR OrthoDB; EOG6G20RQ; -. DR BioCyc; MPNE272634:GJ6Z-125-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR022466; AGR_box. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR022465; Termin_org_TopJ. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF16713; EAGR_box; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR TIGRFAMs; TIGR03834; EAGR_box; 1. DR TIGRFAMs; TIGR03835; termin_org_DnaJ; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 910 DnaJ-like protein MG200 homolog. FT /FTId=PRO_0000071003. FT DOMAIN 4 73 J. {ECO:0000255|PROSITE- FT ProRule:PRU00286}. SQ SEQUENCE 910 AA; 100191 MW; 125D0E37D2D221A7 CRC64; MAEAKRDYYE VLGLSRDADD NDIKKAFRKL AKKYHPDRNK APDAAQIFAE INEANDVLSN PKKRANYDKY GHDGVDNEGG FAFQADVFDS FFEEIEKSGA FDNLSESNTK KKEKTKTKKK GWFWGKSKQE ESTSDTTEYA DVDAGLEDYP PQSDYPDDIP DVDARIEEVD QSAYADDIPD VDAGMDWEQN AEVANSASEI IPDVDAGLAD EFNTSSAAPQ ASDWEAMIGN PEYGYFDAAG EWNWKGFFDE AGQWVWLEET EPSSVSNDET TTDSDAVTAA TTVEETDQDS WTANSAPEPV DVETPVELQP ETEPEPIITL SSEPVEAPAS VVIEPTPEIE ETTSAVEMDA SVKADVSDEA DATNEPTEQD TISEPEQETD AAALEEINHT TADLEPAEVS ATNDLEQDVV EKVNFSEPES TVDTAATDPV VEQATETSTN GFKFFNFSSF VLSDQNPNPQ TPTHHEEDAA APEPTVDETS GESTAPEVTI AESTVELETA AEINNPATFV EEYLQPTKTT VVDKLDEPTV AKPTVSDSEN SVAPEPEFVA GPEQTFSWKP AISETEEIPL TAVEPASETQ TLIAEDVTSP VTPTATAIPA PSINAVPTAP VAETFEAAVD FLKEAAKIEA QLPLVPTVPE QIDGTDPSLL TQWDEYLEKT RKLFHKLFLT EQLPFIVKTD QFEIVDPNLD EHNVNLIYTE HVPQICFLNE QLKEIRYTRK LVDPQTQVTT TESITLEVQL SHKSQTEAIA IFKGFGHDYG SGCGDLKVVL KVIPSVFFQL QADGLHTAAL VDPLVAYNGG LIDVFGPVNS FKVDIEGGIA NNDLIEFNQL GVLRTKTKRG SLYVHLYYSS VAKKGTKTNC QVQQFFDLVH VEYKLLNYNL KQLHNYHSAL TAQKKTLDRK SYQCLAVESH // ID DNAK_MYCPN Reviewed; 595 AA. AC P75344; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Chaperone protein DnaK; DE AltName: Full=HSP70; DE AltName: Full=Heat shock 70 kDa protein; DE AltName: Full=Heat shock protein 70; GN Name=dnaK; Synonyms=hsp70; OrderedLocusNames=MPN_434; ORFNames=MP407; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}. CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96055.1; -; Genomic_DNA. DR PIR; S73733; S73733. DR RefSeq; NP_110122.1; NC_000912.1. DR RefSeq; WP_010874790.1; NC_000912.1. DR ProteinModelPortal; P75344; -. DR SMR; P75344; 8-516. DR IntAct; P75344; 17. DR PRIDE; P75344; -. DR EnsemblBacteria; AAB96055; AAB96055; MPN_434. DR GeneID; 876838; -. DR KEGG; mpn:MPN434; -. DR PATRIC; 20022264; VBIMycPne110_0469. DR KO; K04043; -. DR OMA; MSEHKKS; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; MPNE272634:GJ6Z-463-MONOMER; -. DR Proteomes; UP000000808; 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 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 1 595 Chaperone protein DnaK. FT /FTId=PRO_0000078496. FT MOD_RES 182 182 Phosphothreonine; by autocatalysis. FT {ECO:0000250}. SQ SEQUENCE 595 AA; 65098 MW; 3F9F24F5F53AD447 CRC64; MSTDNGLIIG IDLGTTNSCV SVMENGRPVV LENPEGKRTT PSIVSYKNNE IIVGDAAKRQ MVTNPNTIVS IKRLMGTSNK VTVKNPDGST KELTPEEVSA QILSYLKDYA EKKIGKTISR AVITVPAYFN DAERNATKTA GKIAGLNVER IINEPTAAAL AYGIDKSNRE MKVLVYDLGG GTFDVSLLDI AEGTFEVLAT AGDNRLGGDD WDNKIIEFIL AHIAQEHNGL NLSNDKMAMQ RLKEAAERAK IELSAQLEAI ISLPFLTVTE KGPVNVELKL TRAKFEEITK QLLERTRNPI SDVLREAKIK PEEINEILLV GGSTRMPAVQ KLVESMVPGH SPNRSINPDE VVAIGAAIQG GVLRGDVKDV LLLDVTPLTL SIETLGGVAT PLIKRNTTIP VSKSQIFSTA QDNQESVDVV VCQGERPMAR DNKSLGRFNL GGIQPAPKGK PQIEITFSLD ANGILNVKAK DLTTQKENSI TISDNGNLSE EEIQKMIRDA EANKERDNVI RERIELRNEG ESIVSTIKEI LQSPEAKDFP KEEKEKLDKI TGGIDAAIKA NDYTKLKAEI ENFKKWREEM AKKYNPNGDQ GQPAQ // ID DPO3A_MYCPN Reviewed; 872 AA. AC P75404; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=DNA polymerase III subunit alpha; DE EC=2.7.7.7; GN Name=dnaE; OrderedLocusNames=MPN_378; ORFNames=MP459; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. CC This DNA polymerase also exhibits 3' to 5' exonuclease activity. CC The alpha chain is the DNA polymerase (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, CC epsilon and theta chains) that associates with a tau subunit. This CC core dimerizes to form the PolIII' complex. PolIII' associates CC with the gamma complex (composed of gamma, delta, delta', psi and CC chi chains) and with the beta chain to form the complete DNA CC polymerase III complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96107.1; -; Genomic_DNA. DR PIR; S73785; S73785. DR RefSeq; NP_110066.1; NC_000912.1. DR RefSeq; WP_010874734.1; NC_000912.1. DR ProteinModelPortal; P75404; -. DR IntAct; P75404; 4. DR EnsemblBacteria; AAB96107; AAB96107; MPN_378. DR GeneID; 876812; -. DR KEGG; mpn:MPN378; -. DR PATRIC; 20022132; VBIMycPne110_0409. DR KO; K02337; -. DR OMA; KNEVELH; -. DR OrthoDB; EOG6CZQGR; -. DR BioCyc; MPNE272634:GJ6Z-399-MONOMER; -. DR Proteomes; UP000000808; 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 InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR004805; PolC_alpha. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR TIGRFAMs; TIGR00594; polc; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 872 DNA polymerase III subunit alpha. FT /FTId=PRO_0000103327. SQ SEQUENCE 872 AA; 99257 MW; 25F8E365E2D058D7 CRC64; MFVNLHTNSY YNFLNSTLSP QKLVDLAVQD QQVAVCLTDP NLFGATEFFL ACQKAHIKPL IGLSVTVRHY EQNVNLLVIA QTNRGYQNLM CLALVKDQPD LQLEPFLDGN VVIICTQTEL RLNTANPVYL AHGLSGRYPK IAVTQKPVKC QNTNKDLTLL LTLKQISQIN SEHFQPLEWK LSRSLNEIQL DPPLLQQLRH QPFLSQKAAQ QIFSEEELGN LQKLVEQSQW DLTKLKASSL QVSHNDAQML SEQCQLALTE FLKLNPQLNK QLYEERLAKE LEIINSLHFA SYFLVVSDLV QFAHNNDILI GPGRGSAVGS LVAFLLKITQ IDPVANNLIF ERFISRHRQG LPDIDIDIME TKRDLVIDYV MQKYGREQCA QIVTFQKFKT RSALRDVGKV FNHIEGAEDL LGKLPKDKSL LELDVNGVTD PVLQLSLKSF RLLWEVAREI INFPRQPSIH ASGVVIVTEP LITTIPLMVG NNNNYVTQVS MDWLEWYNLN KFDLLGLINL TMIHEVVQAV KPKEVSVQQF LQQIPLDDEA TFTNLTNQAT LGVFQLESFG MKKVLKQIKP HNLHDLAIVL ALYRPGPQDN INTFIANRNL GFDTSDIDPR ILPILKETYG VLIFQEQVIN IAKTVANYSL ETADSFRRAI SKKNLQVIQD NMRSFYEGAL ANNFSLKAAT TIFNYIQRFA GYGFNLSHAL GYALLSYWTA WLKTHYFEQF NLWWLNHEQG KKEKQKQLLN EFISSGYEIC PPLINKAKSD FSVQDKKLYL GFKLINGIGD KQAHALEHVQ EVLKQNPNLS LIATVNLCLS KTVGGLELKD ITLLQQAGCF NCFNYTVDFN LAKSFWVQSN HELFPKIPLD QPPVINWKSF GF // ID DNAJ_MYCPN Reviewed; 390 AA. AC P78004; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=MPN_021; ORFNames=MP133; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95781.1; -; Genomic_DNA. DR PIR; S73459; S73459. DR RefSeq; NP_109709.1; NC_000912.1. DR RefSeq; WP_010874378.1; NC_000912.1. DR ProteinModelPortal; P78004; -. DR IntAct; P78004; 1. DR DNASU; 876982; -. DR EnsemblBacteria; AAB95781; AAB95781; MPN_021. DR GeneID; 876982; -. DR KEGG; mpn:MPN021; -. DR PATRIC; 20021317; VBIMycPne110_0020. DR KO; K03686; -. DR OMA; IKDPCNS; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; MPNE272634:GJ6Z-23-MONOMER; -. DR Proteomes; UP000000808; 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 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 1 390 Chaperone protein DnaJ. FT /FTId=PRO_0000070833. FT DOMAIN 5 79 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 165 172 CXXCXGXG motif. FT REPEAT 183 190 CXXCXGXG motif. FT REPEAT 209 216 CXXCXGXG motif. FT REPEAT 223 230 CXXCXGXG motif. FT ZN_FING 152 235 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 84 135 Gly-rich. FT METAL 165 165 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 168 168 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 183 183 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 186 186 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 209 209 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 212 212 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 223 223 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 226 226 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 390 AA; 43167 MW; 442E1A6304E8697E CRC64; MAAGKRDYYE VLGVSRSATA QDIKRAFRKL AMQYHPDRHK GEGETVQKQN EEKFKEVNEA YEVLSDTEKR GMYDRFGHEG LNASGFHETG FNPFDIFNSV FGEGFSFDMD GGSPFDFIFS RGKKSRQNRV VLPYDLEIAV GVDISFFEMT NGCTRTIEYT KRVTCSACDG FGAEGGETGM VSCNSCEGNG FILKNQRSIF GTVQSQMLCQ SCGGQGKQAK HKCKTCKGSK YKKVPTTKEI QIPAGIYHGD ALVDDHGGNE FGGHVGKLVV HVGVLPSKIF KRVDHNVVAN VLVDPMIAIT GGKIELPTLE GIKEFNLRAG TKSGEQIVIP GGGIKFTKNF RKKAGDLIII ISYARPSEYS APELRKLKEF IKPNQEVKQY LNALKNEYKS // ID DPO3_MYCPN Reviewed; 1443 AA. AC P75080; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356}; DE Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356}; DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356}; GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; GN OrderedLocusNames=MPN_034; ORFNames=MP120; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA CC polymerase also exhibits 3' to 5' exonuclease activity. CC {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- INTERACTION: CC P78014:recA; NbExp=3; IntAct=EBI-2258713, EBI-2258718; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- SIMILARITY: Contains 1 exonuclease 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; U00089; AAB95768.1; -; Genomic_DNA. DR PIR; S73446; S73446. DR RefSeq; NP_109722.1; NC_000912.1. DR RefSeq; WP_010874391.1; NC_000912.1. DR ProteinModelPortal; P75080; -. DR IntAct; P75080; 4. DR EnsemblBacteria; AAB95768; AAB95768; MPN_034. DR GeneID; 877158; -. DR KEGG; mpn:MPN034; -. DR PATRIC; 20021343; VBIMycPne110_0033. DR KO; K03763; -. DR OMA; QGCTGVK; -. DR OrthoDB; EOG6ZWJJS; -. DR BioCyc; MPNE272634:GJ6Z-36-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00356; DNApol_PolC; 1. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR006308; PolC_gram_pos. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF14579; HHH_6; 1. DR Pfam; PF02811; PHP; 1. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. DR TIGRFAMs; TIGR01405; polC_Gram_pos; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 1443 DNA polymerase III PolC-type. FT /FTId=PRO_0000204583. FT DOMAIN 408 567 Exonuclease. SQ SEQUENCE 1443 AA; 165102 MW; 5E8593E15B289C48 CRC64; MVFDTETEKG KRIWALSQFL VKKNILDHNE LHQLNNRIEL VYLENDRENA LFLVALTLKK PLTIDIWNAL YEGFQDAEGA ELRITFQEDA TFFKDGSTKS SVTLAIIKDY FKSFFGKDKK YRILLEQELT HPNFLSYSNH ELKANCQSQE LDQWLIEQRQ AFIKWMHQAG FTHFGFVSLF NPPAEKQLKV KSMKVSKYDK QFETEVFSTE FVPIHKINQQ MDEIKLMGQI FELKDFPGYN NLRNTLNIYV TDFQLGGSLI LKWFYKDPKT IEGIKIGTWV KATVKVERDA KTQLLQGIIK EISPIETPAY YRRPDQDKQK RVELVFHTKM SAFDGINSVQ EYAQFAKERD WKTIAVTDKD NIHIYPTLYE VAKKYGLKAI YGLECNLIDD HIKIVSNPDK TKLKDATFVI FDIETTGLHG RYDSVIEFAG IKVKHNREVE RMQFFLKIDG PLPAAVTEIT KITQAQLEDG MEQQAGLEKL RAWLDGCVMV AHNGLSFDLP FLQTQFEKYN IAPLTNPLID TLALSWALNP GFASHTLSNI CAKLKFDFDD ERLHRADYDT QALKKVFDYF KEQVELMGIT NLEQLDQELN QQCHFELLKR TFTNTGIIYI KSQSGFAKLY ELLSIALTDN NATRPLVLTS TLQKFAKSFV ITDNPVQGDI FKAALTKPLK ELEAAIKRVD FVLIAPPGAY AGYTIREGLK KEAIPNAIKL VVDTAQRLNK LVAVASDAYF IHPWENEYYK AIVCAKGLGG RWHRHFNYKE REQRVPNVFV RTTGEMLNEM SFLGEQLAYE LVVENTNKLA KQLTADDLVP VQTKLQPPVI EGSNENLAAK TWSQAKAIYG DPLPKLIEQR IQEELKAIID NGFGIIYWIS HLLVKQSVQD GYFVGPRGSI GSSLVANLIG ISEINPLVPH YLCESCQYFE VNEEVDDGYD LMVRDCPKCG AKAAFKGDGH NIPFATFMGF AGDKIPDIDL NFSSEYQAKA HAYVRELFGE QYTFRAGTIA TVAEKTAYGY ARNYFEIIKQ TELATAPEIE RFKQKLVGIK RTTGQHPGGI MIFPNHKSVY EFTPCGYPAD DTSSDWKTTH FEYDALGNTI LKLDILGQDD PTMLKHLGDL THVNPQNIPR FDKKLTEMFW SVNPLKLKPH YLDEPTGAIG IPEFGTKFVR KILEQTKPKG FGDLIRVSGL SHGKNVWADN AQKILKDQNL SLKDVIACRD DIMLYLIHKG MQAKDAFEIM EKVRKGIALN AKEVQLMQSN GVEQHWINSC LKISYLFPKA HAAAYVLMAW RIAWFKLYHP LSYYACLLSF KLKEHDVSGF KSGVSFVKQK LEELNTLYRI KRIKPKEAEL LTSYEVYLEM MARGIKLEQI SLTHSHATRF VEHNGMLIAP FITIPGMGEA VANSIIEARN EKPFSSLDDF KKRTKITKKH IEAFTQMQLL DEFREQDNQK KLF // ID DNLJ_MYCPN Reviewed; 658 AA. AC P78021; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 16-MAR-2016, entry version 108. 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}; Synonyms=lig; GN OrderedLocusNames=MPN_357; ORFNames=MP479; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96127.1; -; Genomic_DNA. DR PIR; S73805; S73805. DR RefSeq; NP_110045.1; NC_000912.1. DR RefSeq; WP_010874713.1; NC_000912.1. DR ProteinModelPortal; P78021; -. DR IntAct; P78021; 1. DR EnsemblBacteria; AAB96127; AAB96127; MPN_357. DR GeneID; 876856; -. DR KEGG; mpn:MPN357; -. DR PATRIC; 20022074; VBIMycPne110_0384. DR KO; K01972; -. DR OMA; YITKENF; -. DR OrthoDB; EOG6TTVM9; -. DR BioCyc; MPNE272634:GJ6Z-374-MONOMER; -. DR Proteomes; UP000000808; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. 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 PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00278; HhH1; 2. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 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 1 658 DNA ligase. FT /FTId=PRO_0000161750. FT DOMAIN 584 654 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 31 35 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 80 81 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 112 112 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 397 397 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 400 400 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 415 415 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 420 420 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 110 110 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 133 133 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 167 167 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 279 279 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 303 303 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. SQ SEQUENCE 658 AA; 73970 MW; AC316C46AF100331 CRC64; MAKVAQIRAI VEQLKRYDYH YYVLDDPLVS DFEYDQLYKQ LQALEQAHPE LIQPDSPTQR VGGIVVEAFN KFPHQNPMLS LDNAFDTATI ASFIANINNL TGVQNRFVVE PKIDGVSISL TYENGLLTRA LTRGDGLVGE DVLSNVKTIK SIPLTIPFHK QVEIRGEIFV DKKTFAQINE NLAKPFANAR NLAAGTLRNL NSEVSAKRKL KAFFYFVPNA LTLGCRSQSA VLAQLKQWNF PVSKAVASFD RPEALIEYLE QFDQTRDQLN FQVDGLVVKL DNFHFYDQLG FTSKFPRWAL AYKFKPKFVQ TKLRGVLVTV GRTGKINYTA QLDPVNLEGT VVSAATLHNF DYIKEKDIRL NDTVIIYKAG EIIPKVLEVC LPLRTAANQP IPEQTHCPAC QAPLVQYKDE VDQYCTNERC DQRNLEAINY FVSKTAMDIQ GLSIQTISKL YENNLVRSVV DLYHLKEHKA AVLALELKIG EVLFNKLISS IEQSKTKGMA RLLTGLGIKH VGQVLAKSLT KHFENIDALQ SASMETLLEL PDVGPTVAES LFNWFHNDNN LQLLAALKAV GVQMDALKSN TNFDTASIYF QKSFVITGSF PISRDTIKNL LVNKYDCRFT NNVTSKVDFV LAGIKATPRK LEQAKALNIP IINEPIWT // ID DYR_MYCPN Reviewed; 160 AA. AC P78028; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; Synonyms=dhfR; OrderedLocusNames=MPN_321; ORFNames=MP515; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential CC reaction for de novo glycine and purine synthesis, and for DNA CC precursor synthesis (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660}. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00660}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96163.1; -; Genomic_DNA. DR PIR; S73841; S73841. DR RefSeq; NP_110009.1; NC_000912.1. DR RefSeq; WP_010874677.1; NC_000912.1. DR ProteinModelPortal; P78028; -. DR IntAct; P78028; 5. DR EnsemblBacteria; AAB96163; AAB96163; MPN_321. DR GeneID; 876943; -. DR KEGG; mpn:MPN321; -. DR PATRIC; 20021996; VBIMycPne110_0345. DR KO; K00287; -. DR OMA; IISIWAM; -. DR OrthoDB; EOG6KT2V2; -. DR BioCyc; MetaCyc:MONOMER-579; -. DR BioCyc; MPNE272634:GJ6Z-338-MONOMER; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR012259; DHFR. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR017925; DHFR_CS. DR InterPro; IPR001796; DHFR_dom. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; One-carbon metabolism; Oxidoreductase; KW Reference proteome. FT CHAIN 1 160 Dihydrofolate reductase. FT /FTId=PRO_0000186396. FT DOMAIN 1 160 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT NP_BIND 6 7 NADP. {ECO:0000250}. FT NP_BIND 14 19 NADP. {ECO:0000250}. FT NP_BIND 43 46 NADP. {ECO:0000250}. FT NP_BIND 62 65 NADP. {ECO:0000250}. FT NP_BIND 101 106 NADP. {ECO:0000250}. FT REGION 5 7 Substrate binding. {ECO:0000250}. FT BINDING 27 27 Substrate. {ECO:0000250}. FT BINDING 32 32 Substrate. {ECO:0000250}. FT BINDING 57 57 Substrate. {ECO:0000250}. FT BINDING 120 120 Substrate. {ECO:0000250}. SQ SEQUENCE 160 AA; 18511 MW; 87C323433A3FABA4 CRC64; MVKAIWAMDQ NGLIGNGNSL PWRIKAELQH FRQTTLHQDV LMGSATYLSL PPVFSERNVY ILTRNLNFNP PDKGCLTKVI HEYENFIQPY LHHPDKHLYI CGGAQVYEQL IPRCDALIVS TIFGKYTGDK YLKVDFSPFE LTKEISFAEF KVAYYHKIAR // ID DPO3B_MYCPN Reviewed; 380 AA. AC Q50313; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=DNA polymerase III subunit beta; DE EC=2.7.7.7; GN Name=dnaN; OrderedLocusNames=MPN_001; ORFNames=MP153; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, CC epsilon and theta chains) that associates with a tau subunit. This CC core dimerizes to form the POLIII' complex. PolIII' associates CC with the gamma complex (composed of gamma, delta, delta', psi and CC chi chains) and with the beta chain to form the complete DNA CC polymerase III complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34816; AAC43645.1; -; Genomic_DNA. DR EMBL; U00089; AAG34739.1; -; Genomic_DNA. DR PIR; S62836; S62836. DR RefSeq; NP_109689.1; NC_000912.1. DR RefSeq; WP_010874358.1; NC_000912.1. DR ProteinModelPortal; Q50313; -. DR IntAct; Q50313; 1. DR EnsemblBacteria; AAG34739; AAG34739; MPN_001. DR GeneID; 877175; -. DR KEGG; mpn:MPN001; -. DR PATRIC; 20021275; VBIMycPne110_0001. DR KO; K02338; -. DR OMA; NADANFE; -. DR OrthoDB; EOG65J53F; -. DR BioCyc; MPNE272634:GJ6Z-1-MONOMER; -. DR Proteomes; UP000000808; 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 SMART; SM00480; POL3Bc; 1. DR TIGRFAMs; TIGR00663; dnan; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 380 DNA polymerase III subunit beta. FT /FTId=PRO_0000105446. SQ SEQUENCE 380 AA; 43856 MW; AE3F5717962D3DFB CRC64; MKVLINKNEL NKILKKLNNV IVSNNKMKPY HSYLLIEATE KEINFYANNE YFSAKCTLAE NIDVLEEGEV IVKGKIFSEL INGIKEDIIT IQEKDQTLLV KTKKTNINLN TIDKKEFPRI RFNQNVDLKE FDELKIQHSL LTKGLKKIAH AVSTFRESTR KFNGVNFNGS NGKQIFLEAS DSYKLSVYEI KQKTDPFNFI VETNLLSFIN SFNPEGGDLI SIFFRKEHKD DLSTELLIKL DNFLINYTSI NESFPRVMQL FDFEPETKVT IQKNELKDAL QRILTLAQNE RFFLCDMQVT NSHLKINSNV QNIGASLEEV TCLKFEGHKL NIAVNALSLL EHIDSFDTDE IELYFQGSNK YFLISSNNEP ELKEILVPSK // ID DPO3X_MYCPN Reviewed; 681 AA. AC P75177; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=DNA polymerase III subunit gamma/tau; DE EC=2.7.7.7; GN Name=dnaX; OrderedLocusNames=MPN_618; ORFNames=MP224; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, CC epsilon and theta chains) that associates with a tau subunit. This CC core dimerizes to form the POLIII' complex. PolIII' associates CC with the gamma complex (composed of gamma, delta, delta', psi and CC chi chains) and with the beta chain to form the complete DNA CC polymerase III complex (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DnaX/STICHEL 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; U00089; AAB95872.1; -; Genomic_DNA. DR PIR; S73550; S73550. DR RefSeq; NP_110307.1; NC_000912.1. DR RefSeq; WP_010874975.1; NC_000912.1. DR ProteinModelPortal; P75177; -. DR IntAct; P75177; 5. DR EnsemblBacteria; AAB95872; AAB95872; MPN_618. DR GeneID; 877276; -. DR KEGG; mpn:MPN618; -. DR PATRIC; 20022719; VBIMycPne110_0682. DR KO; K02343; -. DR OMA; VENTDFF; -. DR OrthoDB; EOG6WQD76; -. DR BioCyc; MPNE272634:GJ6Z-664-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR027417; P-loop_NTPase. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02397; dnaX_nterm; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; KW DNA-directed DNA polymerase; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 681 DNA polymerase III subunit gamma/tau. FT /FTId=PRO_0000105499. FT NP_BIND 44 51 ATP. {ECO:0000255}. SQ SEQUENCE 681 AA; 76213 MW; E3DDC6A580FFCBCC CRC64; MRKVLYQKYR PTKFSDTVGQ DSIKRIIVNA ITQDQLPHGY IFAGERGTGK TTFAKIIAKA INCLNWNGDV CNQCEACQAI NSNSAIDVFE IDAASKNGIN DIRELAENVF NLPFKFKKKV YILDEAHMLT PQSWSGLLKT LEEAPDYVLF IFATTEFNKI PITILSRCQS FFFKQITNDL IQQRLAEVAA KESIKITTDA LVKLADLAQG SLRDGLSLLD QISNFSESKT ISLADVEKTF NLLDKEQKFG FIEAVLSGDL KQSFHLIDNF ESQGINFVHF LRELFALTVD LYGYVKTGQI AVVKPSDQTM AAKLRFHPKQ YALLVQAIEA NTGYGPSQLS LSDQIKAIVI HYNNAVSKEP HIPAYTPVVQ TQSPAKEHVP SKTVEEAKPQ LPAKEPVLYK VIEEPKVSSF VKDPVASKLI EQPQTIVQPE AQQEITEVEQ PTETSPAPAT DLFGLAIKPE VVRKRGRRPL SVENTDFFQP AVKKLIQPVS KPAPIKLIEP SDNNPVSIPI KLNRAVIAVS VYGHNDPKLV AHFQQLLDSF KREFTQAEKT KDSSYLKQFS DKFTASDLSK VIKVLAASPF GLVLIFEDKE IATRLWKEAL TEATAQATLL EIFQQNLFLS SFTLSEYETK VLAKVEQLTH KPQVLQLQQL EQLSSTVVKK AQKTAAQEIA DTFFKGLYEE K // ID ECFA2_MYCPN Reviewed; 303 AA. AC Q50293; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO2; GN OrderedLocusNames=MPN_194; ORFNames=GT9_orf303, MP637; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling CC factor (ECF) ABC-transporter complex. Unlike classic ABC CC transporters this ECF transporter provides the energy necessary to CC transport a number of different substrates. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component), 2 ATP-binding proteins (A component) and 2 CC transmembrane proteins (T component). {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy- CC coupling factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43687.1; -; Genomic_DNA. DR EMBL; U00089; AAB96285.1; -; Genomic_DNA. DR PIR; S62814; S62814. DR RefSeq; NP_109882.1; NC_000912.1. DR RefSeq; WP_010874551.1; NC_000912.1. DR ProteinModelPortal; Q50293; -. DR IntAct; Q50293; 1. DR EnsemblBacteria; AAB96285; AAB96285; MPN_194. DR GeneID; 876933; -. DR KEGG; mpn:MPN194; -. DR PATRIC; 20021711; VBIMycPne110_0212. DR KO; K16787; -. DR OMA; LFDRTVY; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-201-MONOMER; -. DR Proteomes; UP000000808; 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:0006810; P:transport; 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; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR030946; EcfA2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04521; ECF_ATPase_2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 303 Energy-coupling factor transporter ATP- FT binding protein EcfA2. FT /FTId=PRO_0000092046. FT DOMAIN 17 260 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 54 61 ATP. {ECO:0000255|HAMAP-Rule:MF_01710}. SQ SEQUENCE 303 AA; 34357 MW; CCDED25FB41BAF19 CRC64; MKKIVELKNP LRDGEILSVS NLSCFFNEKT VHEVKVIDNF SYTFAKNKVY CIIGDSGSGK STLVNHFNGL IKPAYGDIWV KDIYIGQKQR KIKDFKRLRK TISIVFQFPE YQLFKDTVEK DIMFGPIALG QSKNEARQKA AYYLEKMGLK YTFLERNPFE LSGGQKRRVA IAGILAIEPE VLIFDEPTAG LDPEGEREMM RLIKDAKASG RTVFMITHQM ENVLEVADEV LVLSKGQLVK SGDPYEVFMD EAFLAHTTII MPPVIQVIKD LINLNPKFSC LLDFKPRNLD QLADAINNTI AHG // ID EFG_MYCPN Reviewed; 688 AA. AC P75544; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Elongation factor G; DE Short=EF-G; GN Name=fusA; Synonyms=fus; OrderedLocusNames=MPN_227; ORFNames=MP604; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000305}. 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; U00089; AAB96252.1; -; Genomic_DNA. DR PIR; S73930; S73930. DR RefSeq; NP_109915.1; NC_000912.1. DR RefSeq; WP_010874584.1; NC_000912.1. DR ProteinModelPortal; P75544; -. DR SMR; P75544; 6-684. DR EnsemblBacteria; AAB96252; AAB96252; MPN_227. DR GeneID; 877061; -. DR KEGG; mpn:MPN227; -. DR PATRIC; 20021779; VBIMycPne110_0246. DR KO; K02355; -. DR OMA; KLGVAIQ; -. DR OrthoDB; EOG6X6RBF; -. DR BioCyc; MPNE272634:GJ6Z-234-MONOMER; -. DR Proteomes; UP000000808; 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 1 688 Elongation factor G. FT /FTId=PRO_0000091163. FT DOMAIN 8 282 tr-type G. FT NP_BIND 17 24 GTP. {ECO:0000250}. FT NP_BIND 81 85 GTP. {ECO:0000250}. FT NP_BIND 135 138 GTP. {ECO:0000250}. SQ SEQUENCE 688 AA; 76500 MW; 762E430061A7DFA4 CRC64; MARTVDLINF RNFGIMAHID AGKTTTSERI LFHSGRIHKI GETHDGESVM DWMEQEKERG ITITSAATSV SWKNCSLNLI DTPGHVDFTV EVERSLRVLD GAIAVLDAQM GVEPQTETVW RQASRYEVPR IIFVNKMDKT GANFERSVQS IQQRLGVKAV PIQLPIGAEN DFNGIIDLIE EKVYFFDGGK EEKAEEKPIP DQFKDQVKQM RAHLVEEVAN FDDQLMADYL EGKEISIADI KRCIRKGVIG CQFFPVLCGS AFKNKGIKLL LDAVVDFLPS PVDVPQAKAY GEDGNEVLIS ASDDAPFVGL AFKVATDPFV GRLTFVRVYS GVLKSGSYVK NVRKNKKERV SRLVKMHAQN RNEIEEIRAG DICAIIGLKD TTTGETLVDD KIDVQLEAMQ FAQPVISLAV EPKTKADQEK MSIALSKLAE EDPTFKTFTD PETGQTIIAG MGELHLDILV DRMRREFKVE VNVGAPQVSF RETFNKESEV EGKYIKQSGG RGQYGHVKIR FEPNKDKGFE FVDKIVGGRI PREYIKPVQA GLENAMASGP LAGYPMIDIK ATLFDGSFHE VDSSEMAFKI AASLALKEAG KVCSPVLLEP IMAIEVTVPE QYFGDTMGDI SSRRGLIEGT EQRDNVQVIK AKVPLKEMFG YATDLRSFSQ GRGNYVMQFS HYAETPKSVV NEIIATKK // ID ECFA1_MYCPN Reviewed; 274 AA. AC Q50294; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO1; GN OrderedLocusNames=MPN_193; ORFNames=GT9_orf274, MP638; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling CC factor (ECF) ABC-transporter complex. Unlike classic ABC CC transporters this ECF transporter provides the energy necessary to CC transport a number of different substrates. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component), 2 ATP-binding proteins (A component) and 2 CC transmembrane proteins (T component). {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy- CC coupling factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43688.1; -; Genomic_DNA. DR EMBL; U00089; AAB96286.1; -; Genomic_DNA. DR PIR; S62815; S62815. DR RefSeq; NP_109881.1; NC_000912.1. DR RefSeq; WP_010874550.1; NC_000912.1. DR ProteinModelPortal; Q50294; -. DR EnsemblBacteria; AAB96286; AAB96286; MPN_193. DR GeneID; 876826; -. DR KEGG; mpn:MPN193; -. DR PATRIC; 20021709; VBIMycPne110_0211. DR KO; K16786; -. DR OMA; SIISITH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-200-MONOMER; -. DR Proteomes; UP000000808; 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:0006810; P:transport; 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; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR030947; EcfA_1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04520; ECF_ATPase_1; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 274 Energy-coupling factor transporter ATP- FT binding protein EcfA1. FT /FTId=PRO_0000092045. FT DOMAIN 10 241 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_01710}. SQ SEQUENCE 274 AA; 30535 MW; 83591C25C77B7552 CRC64; MLNTNKQAAA SFQGVYFSYS ELPLIRNLSF DVFEGEYVCI VGHNGSGKST ISKLLTGLLK PQAGTIKIFG KTISSENVTY LRNHIGIIFQ NPDNQFIGIT VEDDIAFGLE NRRYTREKMK SIIEDVAQQA GITELLQKEP HNLSGGQKQR VAIASVLALN PAIIIFDEST SMLDPKAKRT IKQFMVELRN QGKCVISITH DMEEVTKADK VLVMNEGRLI RQGKPKDVFN SAAELQKIRL DIPFSLSLST KVNGVTSTID YQQLIEAIGK LWKK // ID EFTU_MYCPN Reviewed; 394 AA. AC P23568; P75126; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 109. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=MPN_665; GN ORFNames=MP177; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2126326; DOI=10.1111/j.1365-2958.1990.tb00709.x; RA Yogev D., Sela S., Bercovier H., Razin S.; RT "Nucleotide sequence and codon usage of the elongation factor Tu(EF- RT Tu) gene from Mycoplasma pneumoniae."; RL Mol. Microbiol. 4:1303-1310(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; X55768; CAA39292.1; -; Genomic_DNA. DR EMBL; U00089; AAB95825.1; -; Genomic_DNA. DR PIR; S73503; S73503. DR RefSeq; NP_110354.1; NC_000912.1. DR RefSeq; WP_010875022.1; NC_000912.1. DR ProteinModelPortal; P23568; -. DR SMR; P23568; 2-393. DR IntAct; P23568; 21. DR EnsemblBacteria; AAB95825; AAB95825; MPN_665. DR GeneID; 877030; -. DR KEGG; mpn:MPN665; -. DR PATRIC; 20022815; VBIMycPne110_0730. DR KO; K02358; -. DR OMA; NIKMVVN; -. DR OrthoDB; EOG6R5C6X; -. DR BioCyc; MPNE272634:GJ6Z-711-MONOMER; -. DR Proteomes; UP000000808; 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_0000091350. FT DOMAIN 10 204 tr-type G. FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT REGION 19 26 G1. {ECO:0000250}. FT REGION 60 64 G2. {ECO:0000250}. FT REGION 81 84 G3. {ECO:0000250}. FT REGION 136 139 G4. {ECO:0000250}. FT REGION 174 176 G5. {ECO:0000250}. FT CONFLICT 12 13 HV -> QL (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 65 65 S -> I (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 122 122 L -> V (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 136 136 N -> F (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 198 209 EWIPTPEREVDK -> DGFQLLNVKWTN (in Ref. 1; FT CAA39292). {ECO:0000305}. FT CONFLICT 265 265 E -> V (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 360 360 T -> S (in Ref. 1; CAA39292). FT {ECO:0000305}. FT CONFLICT 391 394 EVLE -> KCLNSESRILSWLC (in Ref. 1; FT CAA39292). {ECO:0000305}. SQ SEQUENCE 394 AA; 43149 MW; 32818DA027954BD8 CRC64; MAREKFDRSK PHVNVGTIGH IDHGKTTLTA AICTVLAKEG KSAATRYDQI DKAPEEKARG ITINSAHVEY SSDKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSATD SVMPQTREHI LLARQVGVPR MVVFLNKCDI ATDEEVQELV AEEVRDLLTS YGFDGKNTPI IYGSALKALE GDPKWEAKIH DLMNAVDEWI PTPEREVDKP FLLAIEDTMT ITGRGTVVTG RVERGELKVG QEIEIVGLRP IRKAVVTGIE MFKKELDSAM AGDNAGVLLR GVDRKEVERG QVLAKPGSIK PHKKFKAEIY ALKKEEGGRH TGFLNGYRPQ FYFRTTDVTG SISLPENTEM VLPGDNTSIT VELIAPIACE KGSKFSIREG GRTVGAGSVT EVLE // ID EFP_MYCPN Reviewed; 190 AA. AC P75085; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Elongation factor P; DE Short=EF-P; GN Name=efp; OrderedLocusNames=MPN_029; ORFNames=MP125; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient CC translation and peptide-bond synthesis on native or reconstituted CC 70S ribosomes in vitro. Probably functions indirectly by altering CC the affinity of the ribosome for aminoacyl-tRNA, thus increasing CC their reactivity as acceptors for peptidyl transferase (By CC similarity). {ECO:0000250}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the elongation factor P 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; U00089; AAB95773.1; -; Genomic_DNA. DR PIR; S73451; S73451. DR RefSeq; NP_109717.1; NC_000912.1. DR RefSeq; WP_010874386.1; NC_000912.1. DR ProteinModelPortal; P75085; -. DR IntAct; P75085; 2. DR EnsemblBacteria; AAB95773; AAB95773; MPN_029. DR GeneID; 876940; -. DR KEGG; mpn:MPN029; -. DR PATRIC; 20021333; VBIMycPne110_0028. DR KO; K02356; -. DR OMA; ERHKGQF; -. DR OrthoDB; EOG6JQH6Q; -. DR BioCyc; MPNE272634:GJ6Z-31-MONOMER; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000000808; 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; IPR013852; Transl_elong_P/YeiP_CS. 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. DR PROSITE; PS01275; EFP; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 190 Elongation factor P. FT /FTId=PRO_0000094290. SQ SEQUENCE 190 AA; 21810 MW; 547284880C514BCA CRC64; MADMIEAKSL RSGQTIFGPN KEILLVLENT FNKTAMRQGI VKTKVKNLRT GAIVWIEFTG DKLEQVIIDK KKMTFLYKDG ANYVFMDQQD YSQIEIPEKQ LEWEKNFITE DSEVTIISYQ SEILGVNLPE LVPIEVEFAE EAVQGNTANM ARKRARLVSG YELDVPQFIR TGDKIVISTI DGSYRERYNK // ID ENGB_MYCPN Reviewed; 193 AA. AC P75303; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. 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=MPN_481; ORFNames=MP360; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96008.1; -; Genomic_DNA. DR PIR; S73686; S73686. DR RefSeq; NP_110169.1; NC_000912.1. DR RefSeq; WP_010874837.1; NC_000912.1. DR ProteinModelPortal; P75303; -. DR EnsemblBacteria; AAB96008; AAB96008; MPN_481. DR GeneID; 877162; -. DR KEGG; mpn:MPN481; -. DR PATRIC; 20022386; VBIMycPne110_0520. DR KO; K03978; -. DR OMA; TITLNYY; -. DR OrthoDB; EOG6ND0NG; -. DR BioCyc; MPNE272634:GJ6Z-522-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO: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 InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1. DR TIGRFAMs; TIGR00231; small_GTP; 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 1 193 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157764. FT DOMAIN 19 188 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT NP_BIND 27 34 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 53 57 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 70 73 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 167 169 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT METAL 34 34 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 55 55 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. SQ SEQUENCE 193 AA; 21818 MW; 38449ADD9E9B996A CRC64; MEARFLKSAS DLESCPQDSV KEVCFMGRSN VGKSSLINAF FQKKLAKTSA TPGRTQLLNF FEYNRKRFVD LPGYGFAKLS KVQKEAITNL LTQFLNFRQN LTGVVLVIDS GVVTVQDQEV VKTILQTGLN FLVIANKFDK LNQSERFHTQ NKLAHFLKVN PNKCLFVSAK TGYNLQVMHK QIFELFKADG QAI // ID END4_MYCPN Reviewed; 286 AA. AC P75457; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152}; DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; GN Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=MPN_328; GN ORFNames=MP508; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves CC phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) CC to produce new 5'-ends that are base-free deoxyribose 5-phosphate CC residues. It preferentially attacks modified AP sites created by CC bleomycin and neocarzinostatin. {ECO:0000255|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphooligonucleotide end-products. {ECO:0000255|HAMAP- CC Rule:MF_00152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152}; CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152}; CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96156.1; -; Genomic_DNA. DR PIR; S73834; S73834. DR RefSeq; NP_110016.1; NC_000912.1. DR RefSeq; WP_010874684.1; NC_000912.1. DR ProteinModelPortal; P75457; -. DR EnsemblBacteria; AAB96156; AAB96156; MPN_328. DR GeneID; 876950; -. DR KEGG; mpn:MPN328; -. DR PATRIC; 20022010; VBIMycPne110_0352. DR KO; K01151; -. DR OMA; MKYVGAH; -. DR OrthoDB; EOG6Z0QCM; -. DR BioCyc; MPNE272634:GJ6Z-345-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00152; Nfo; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR PANTHER; PTHR21445; PTHR21445; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR00587; nfo; 1. DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1. DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1. DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1. DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; Zinc. FT CHAIN 1 286 Probable endonuclease 4. FT /FTId=PRO_0000190858. FT METAL 72 72 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 112 112 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 147 147 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 147 147 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 181 181 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 184 184 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 215 215 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 228 228 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 230 230 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 260 260 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. SQ SEQUENCE 286 AA; 31890 MW; 540DE9F5B91B4552 CRC64; MPKLLGSFIS FKSPHYLVGS VRDAVSIKAQ AFMIFLGAPH TALRVDPNRM QIDEGHTLME QHNLSKSGMV VHAPYIINCA SKDPVKQTFA IDVLTREVKL CHAVGAKLIV LHPGSAVEQT QTQALDHLIK VLNTVIANTK EVIICLETMA GKGNEIGRDL DQLKYVINHI EQQERIGVCL DTCHFHDSGN DFNNTAEIME TIDTKLGFEF LKVIHLNESK NVCGSKKDRH ANLGEGMIGF DNLMRFIAQP QIKQIPIVLE TPSDKHNYPA VYGAEIERIR AWFGAR // ID EFTS_MYCPN Reviewed; 298 AA. AC P78009; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Elongation factor Ts; DE Short=EF-Ts; GN Name=tsf; OrderedLocusNames=MPN_631; ORFNames=MP211; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the EF-Ts 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; U00089; AAB95859.1; -; Genomic_DNA. DR PIR; S73537; S73537. DR RefSeq; NP_110320.1; NC_000912.1. DR RefSeq; WP_010874988.1; NC_000912.1. DR ProteinModelPortal; P78009; -. DR IntAct; P78009; 1. DR EnsemblBacteria; AAB95859; AAB95859; MPN_631. DR GeneID; 876992; -. DR KEGG; mpn:MPN631; -. DR PATRIC; 20022745; VBIMycPne110_0695. DR KO; K02357; -. DR OMA; FIMEPKK; -. DR OrthoDB; EOG66B42N; -. DR BioCyc; MPNE272634:GJ6Z-677-MONOMER; -. DR Proteomes; UP000000808; 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 1 298 Elongation factor Ts. FT /FTId=PRO_0000161157. FT REGION 79 82 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000250}. SQ SEQUENCE 298 AA; 33645 MW; A44F9AC67C23FAAF CRC64; MATKIELIKE LRKTTQASMM DCKKALEQNN DDLEKAIKWL RENGIVKSAK KLGKVAADGC IVLHSDHHKA VMVEINSQTD FVARSQELTD FAQLMISEVF KKATPTTTIE EVTQYELQGK EKVAERLALV ASKTDEKIVL RRLMVFESKT NHIFSYLHAN KRIGVILEVE GKFDEQDGKH LAMHIAANSP QFIDQDNVDQ TWLANETSII KSQAKLEVQD NPKKAAFLDK TIAGRVNKLL IDICLVNQKY LVDESKTVGQ FLKEKNSKVI HFVRFEVGEG IVKEAVDFAS EVSAQMKK // ID EX53_MYCPN Reviewed; 291 AA. AC P75403; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=5'-3' exonuclease; DE EC=3.1.11.-; GN Name=polA; OrderedLocusNames=MPN_379; ORFNames=MP458; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: 5'-3' exonuclease acting preferentially on double- CC stranded DNA. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 5'-3' exonuclease 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; U00089; AAB96106.1; -; Genomic_DNA. DR PIR; S73784; S73784. DR RefSeq; NP_110067.1; NC_000912.1. DR RefSeq; WP_010874735.1; NC_000912.1. DR ProteinModelPortal; P75403; -. DR IntAct; P75403; 3. DR EnsemblBacteria; AAB96106; AAB96106; MPN_379. DR GeneID; 877399; -. DR KEGG; mpn:MPN379; -. DR PATRIC; 20022134; VBIMycPne110_0410. DR KO; K02335; -. DR OMA; PEIIFEQ; -. DR OrthoDB; EOG6SJJH7; -. DR BioCyc; MPNE272634:GJ6Z-400-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1010; -; 1. 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; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 291 5'-3' exonuclease. FT /FTId=PRO_0000101287. SQ SEQUENCE 291 AA; 32972 MW; 57940FA7F3D852EC CRC64; MKNAILIDGN SLAYRAYFAT WQQVEFAKLH NLPFNNAIRT MLMMCWNLLQ SKQYDYGVIS FDTKAPTFRD QLYSEYKSKR SKTPSELLVQ IPVVKESLRH LGFLVCEQDG FEADDLIGSY ARLMTQNNVA VDIYSSDRDL LQLVDSMTSV WLCVKGTKEM KEYNTDNFAE QFFGLTPKQV IEYKGLVGDN SDNLTGIKGI GPKKGIDLLK QYGTIDNIFA NFDKLSKALQ TILQGQIDTA KKFSFLASIK TDIKLNDDIV HAALKPIDKQ ALLELLDKYG IKALAQKFSQ L // ID ESL3_MYCPN Reviewed; 272 AA. AC P75268; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative esterase/lipase 3; DE EC=3.1.-.-; GN OrderedLocusNames=MPN_519; ORFNames=MP323; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO 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; U00089; AAB95971.1; -; Genomic_DNA. DR PIR; S73649; S73649. DR RefSeq; NP_110207.1; NC_000912.1. DR RefSeq; WP_010874875.1; NC_000912.1. DR ProteinModelPortal; P75268; -. DR ESTHER; mycpn-esl3; AlphaBeta_hydrolase. DR EnsemblBacteria; AAB95971; AAB95971; MPN_519. DR GeneID; 876827; -. DR KEGG; mpn:MPN519; -. DR PATRIC; 20022496; VBIMycPne110_0575. DR OMA; TSNESWM; -. DR OrthoDB; EOG6PKFB7; -. DR BioCyc; MPNE272634:GJ6Z-560-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0052689; F:carboxylic ester 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 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 272 Putative esterase/lipase 3. FT /FTId=PRO_0000207079. FT ACT_SITE 34 34 {ECO:0000255}. FT ACT_SITE 100 100 Charge relay system. {ECO:0000250}. SQ SEQUENCE 272 AA; 31802 MW; 01F267919E22A4AB CRC64; MRDKVNINTV DISQLEVFFQ PAKKPAKQTI VFAHGFSVHH SYFKSFSETL VDYDYYAPLW PGHNHHGFTD KELSPIHYAH LLVAWIEKQD LENIVLIGHS MGGAVASYAL QFLKPQRVEK LVLLAPLSYS NLLNYYKIKK AFKKKDEKLS YFKRMFQPKF PDLQNDGQWQ MELDKHTAMC KKLTFQIFKE LSRLNSAYKT ITIPAFLLLA QHDDFMPTKA TLNYFNRFLI KKGNLQSGVI LHSQHQMFNS KHESFCKAMH DILKHNKLSK IY // ID ENO_MYCPN Reviewed; 456 AA. AC P75189; Q50324; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 113. 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=MPN_606; GN ORFNames=MP236; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-456. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). 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; U00089; AAB95884.1; -; Genomic_DNA. DR EMBL; U43738; AAC43651.1; -; Genomic_DNA. DR PIR; S73562; S73562. DR RefSeq; NP_110295.1; NC_000912.1. DR RefSeq; WP_010874963.1; NC_000912.1. DR ProteinModelPortal; P75189; -. DR SMR; P75189; 11-450. DR IntAct; P75189; 5. DR EnsemblBacteria; AAB95884; AAB95884; MPN_606. DR GeneID; 876984; -. DR KEGG; mpn:MPN606; -. DR PATRIC; 20022693; VBIMycPne110_0669. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR BioCyc; MetaCyc:MONOMER-551; -. DR BioCyc; MPNE272634:GJ6Z-652-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000808; 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 1 456 Enolase. FT /FTId=PRO_0000133930. FT REGION 389 392 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 219 219 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 362 362 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 256 256 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 310 310 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 337 337 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 178 178 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 310 310 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 337 337 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 362 362 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 413 413 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT CONFLICT 309 311 IED -> HRS (in Ref. 2). {ECO:0000305}. FT CONFLICT 327 332 TLGQHI -> HWSTH (in Ref. 2; AAC43651). FT {ECO:0000305}. SQ SEQUENCE 456 AA; 49228 MW; 5B4B5442ADDC0E86 CRC64; MSAQTGTDLF KIADLFAYQV FDSRGFPTVA CVVKLASGHT GEAMVPSGAS TGEKEAIELR DGDPKAYFGK GVSQAVQNVN QTIAPKLIGL NATDQAAIDA LMIQLDGTPN KAKLGANAIL AVSLAVAKAA ASAQKTSLFK YLANQVMGLN KTEFILTVPM LNVINGGAHA DNNIDFQEFM IMPLGANSMH QALKMASETF HALQKLLKQR GLNTNKGDEG GFAPNLKLAE EALDLMVEAI KAAGYQPGSD IAIALDVAAS EFYDDTTKRY VFKKGIKAKI LDEKEWSLTT AQMIAYLKKL TEQYPIISIE DGLSEHDWEG METLTKTLGQ HIQIVGDDLY CTNPAIAEKG VAHKATNSIL IKLNQIGTLT ETIKAINIAK DANWSQVISH RSGETEDTTI ADLAVAACTG QIKTGSMSRS ERIAKYNRLL QIELELGNNA KYLGWNTFKN IKPQKA // ID ERA_MYCPN Reviewed; 291 AA. AC P75210; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367}; GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; Synonyms=spg; GN OrderedLocusNames=MPN_568; ORFNames=MP274; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with CC rapid nucleotide exchange. Plays a role in 16S rRNA processing and CC 30S ribosomal subunit biogenesis and possibly also in cell cycle CC regulation and energy metabolism. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00367}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Contains 1 Era-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95922.1; -; Genomic_DNA. DR PIR; S73600; S73600. DR RefSeq; NP_110257.1; NC_000912.1. DR RefSeq; WP_010874925.1; NC_000912.1. DR ProteinModelPortal; P75210; -. DR IntAct; P75210; 1. DR EnsemblBacteria; AAB95922; AAB95922; MPN_568. DR GeneID; 876903; -. DR KEGG; mpn:MPN568; -. DR PATRIC; 20022615; VBIMycPne110_0630. DR KO; K03595; -. DR OMA; HIRTTIM; -. DR OrthoDB; EOG693GPD; -. DR BioCyc; MPNE272634:GJ6Z-614-MONOMER; -. DR Proteomes; UP000000808; 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 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 PROSITE; PS51713; G_ERA; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane; KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; KW RNA-binding; rRNA-binding. FT CHAIN 1 291 GTPase Era. FT /FTId=PRO_0000180028. FT DOMAIN 2 144 Era-type G. FT DOMAIN 201 279 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_00367}. FT NP_BIND 10 17 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 58 62 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. SQ SEQUENCE 291 AA; 33529 MW; 2E81B0406A9106E3 CRC64; MESIRIGVLG LTNAGKSTLV NQLHKANNLL VSPMNNTTLL AVSTNTITHE KQNITFIDVP GFSEKRHSSY ELISQEIRKA LSGIDVLLLV VRSDQQQKLP LLQTQLQPLK RYRDLTRVLL INNFFDVVLQ AEDKQAIVLD FKPQAVLETD LLHFDATSFW NQFNEVKLQA NEFRKDVEFL DADTDNFKIL EALREQIIKY CSEEIPHVVR LEIVDKSFDQ AKNLLKLHLS ISVPKLSQKK IIIGRNAQMV KKIGMQMRQK LLEYYDCNVF VELFVRTYDP KQKKSPYGSL I // ID ESL1_MYCPN Reviewed; 269 AA. AC P75333; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 88. DE RecName: Full=Putative esterase/lipase 1; DE EC=3.1.-.-; GN OrderedLocusNames=MPN_445; ORFNames=MP396; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96044.1; 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; U00089; AAB96044.1; ALT_INIT; Genomic_DNA. DR PIR; S73722; S73722. DR RefSeq; NP_110133.1; NC_000912.1. DR RefSeq; WP_010874801.1; NC_000912.1. DR ProteinModelPortal; P75333; -. DR IntAct; P75333; 1. DR ESTHER; mycpn-esl1; AlphaBeta_hydrolase. DR EnsemblBacteria; AAB96044; AAB96044; MPN_445. DR GeneID; 877058; -. DR KEGG; mpn:MPN445; -. DR PATRIC; 20022288; VBIMycPne110_0481. DR OMA; RALIYNI; -. DR OrthoDB; EOG6D2KXC; -. DR BioCyc; MPNE272634:GJ6Z-474-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 269 Putative esterase/lipase 1. FT /FTId=PRO_0000207075. FT ACT_SITE 27 27 {ECO:0000255}. FT ACT_SITE 94 94 Charge relay system. {ECO:0000250}. SQ SEQUENCE 269 AA; 30921 MW; FEFA2D02569723BC CRC64; MRLEIENGLE FVCDPFLNER GKIFFLHAFT GNITNKLSFR THFKDYSFYG INFPGHGNSV IHNQSELDFN FWIKLVQQFF NKYQLKNVVL FGHSIGGGLA IALTQVLTKE QIKGIILEAP LNPGIRATPP SIISALVPDT NEDFEAVQRA LIYNIEQRFG ANFKDFCAKQ KQKMIQKYAP LKVMLQPEQA EQRLQLIDAA FKRLSYPTLW IHGQEDGIVR YLPSKAYLES LHNPLIELVG LSNTAHTTFF EQPQQFLQLV EQFLNKLNK // ID ESL2_MYCPN Reviewed; 268 AA. AC P75311; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Putative esterase/lipase 2; DE EC=3.1.-.-; GN OrderedLocusNames=MPN_473; ORFNames=MP368; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO 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; U00089; AAB96016.1; -; Genomic_DNA. DR PIR; S73694; S73694. DR RefSeq; NP_110161.1; NC_000912.1. DR RefSeq; WP_010874829.1; NC_000912.1. DR ProteinModelPortal; P75311; -. DR ESTHER; mycpn-esl2; AlphaBeta_hydrolase. DR EnsemblBacteria; AAB96016; AAB96016; MPN_473. DR GeneID; 876746; -. DR KEGG; mpn:MPN473; -. DR PATRIC; 20022368; VBIMycPne110_0511. DR OMA; NIACPAL; -. DR OrthoDB; EOG6D2KXC; -. DR BioCyc; MPNE272634:GJ6Z-514-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR PRINTS; PR00111; ABHYDROLASE. DR SUPFAM; SSF53474; SSF53474; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 268 Putative esterase/lipase 2. FT /FTId=PRO_0000207077. FT ACT_SITE 28 28 {ECO:0000255}. FT ACT_SITE 96 96 Charge relay system. {ECO:0000250}. SQ SEQUENCE 268 AA; 30785 MW; 29D5F87E12090C9B CRC64; MASSKSDPFQ SIFAFKPHRK RHNFIFLHGF GSEYSSFKHV FKLFEKKRWS FFAFNFPGHG NNQSNSVDEL KLKHYVELVC DFIIQKRLKK VVLVGHSMGG AIAVLVNAVL RERIKALVLV APMNQTSFVV SKKRILDTLF TRSPKNQQDF IEHTDDKKSI VNFFVGAFKK RVNFKTLYSD MVQNAKYGND YLEAGYNAIK DKPTLVVLGS NDIVTPTKAS VEYLAKHSET IIFKIIDGVG HSPHYYAPKL FFDYIGEFLD NIKRNKDK // ID FMT_MYCPN Reviewed; 311 AA. AC P75235; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=Methionyl-tRNA formyltransferase; DE EC=2.1.2.9; GN Name=fmt; OrderedLocusNames=MPN_543; ORFNames=MP299; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl- CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). CC -!- SIMILARITY: Belongs to the Fmt 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; U00089; AAB95947.1; -; Genomic_DNA. DR PIR; S73625; S73625. DR RefSeq; NP_110232.1; NC_000912.1. DR RefSeq; WP_010874900.1; NC_000912.1. DR ProteinModelPortal; P75235; -. DR EnsemblBacteria; AAB95947; AAB95947; MPN_543. DR GeneID; 877235; -. DR KEGG; mpn:MPN543; -. DR PATRIC; 20022563; VBIMycPne110_0605. DR KO; K00604; -. DR OMA; SIIIKVR; -. DR OrthoDB; EOG6B09WV; -. DR BioCyc; MPNE272634:GJ6Z-588-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 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 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. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 311 Methionyl-tRNA formyltransferase. FT /FTId=PRO_0000082997. FT REGION 109 112 Tetrahydrofolate (THF) binding. FT {ECO:0000250}. SQ SEQUENCE 311 AA; 34905 MW; 62D7958C19DAB6E9 CRC64; MIKVVFFGTS TLSKCCLEAI FQDPEFVVCG VVTQPDKVNE RNNKINFSAV KQFCIENNIP CFQPEKNIQI KTELAQLQAD IGVCVAFGQY IHNDIINLFP YKIANLHPSK LPLLRGGAPL HWTIINGFTT SSLSVIELVQ KMDAGPIWKQ KDFKVNPNWN TGDLFEYVQT HAPQFLIQCL KEIVSGKSQW KEQINPPTFG LNIKKEQERL DLNLEPKAFI NWVKGLAPKP GGWLEFEGQN IKILQATYLG KMTSTTAVGQ ITKISKQGIE IALANDEIVL LQIIQIPGKR AMGVSEIING KHPFAEGKFF H // ID FOLD_MYCPN Reviewed; 269 AA. AC P75096; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 92. 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=MPN_017; ORFNames=MP137; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95785.1; -; Genomic_DNA. DR PIR; S73463; S73463. DR RefSeq; NP_109705.1; NC_000912.1. DR RefSeq; WP_010874374.1; NC_000912.1. DR ProteinModelPortal; P75096; -. DR EnsemblBacteria; AAB95785; AAB95785; MPN_017. DR GeneID; 876845; -. DR KEGG; mpn:MPN017; -. DR PATRIC; 20021305; VBIMycPne110_0016. DR KO; K01491; -. DR OMA; GQPMALM; -. DR OrthoDB; EOG6K6VBB; -. DR BioCyc; MetaCyc:MONOMER-580; -. DR BioCyc; MPNE272634:GJ6Z-17-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000808; 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 1 269 Bifunctional protein FolD. FT /FTId=PRO_0000199311. FT NP_BIND 149 151 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 215 215 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01576}. SQ SEQUENCE 269 AA; 30204 MW; 2976C0FF51B1FA7D CRC64; MSFDGKQLAH EILLTYKNRD WSQVKLVILQ TNNDVSSDAF IRQKMNACNT LGAQSELIKY HESVTEKELL EKIQQLNTDP EVTGIILQLP VYPHLKQNKL LKAIDPYKDV DYLTGNCPLP IRSCVVEAVL ILKEHFHHDF TNKQIVVVGL GVTGGGPIFH YLKETGHQVV GCDKHTPNTM ELIKTADVVI TAIGKPHFFK TTNFKPGVIL YDVGVSRNVL NKLCGDIDPN GIEKVAKWWS PTPGGVGPFT VLAIMKNLWV LYEAHQRRI // ID FPG_MYCPN Reviewed; 277 AA. AC P75402; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 115. DE RecName: Full=Formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM; DE Short=AP lyase MutM; DE EC=4.2.99.18; GN Name=mutM; Synonyms=fpg; OrderedLocusNames=MPN_380; ORFNames=MP457; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in base excision repair of DNA damaged by CC oxidation or by mutagenic agents. Acts as DNA glycosylase that CC recognizes and removes damaged bases. Has a preference for CC oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has CC AP (apurinic/apyrimidinic) lyase activity and introduces nicks in CC the DNA strand. Cleaves the DNA backbone by beta-delta elimination CC to generate a single-strand break at the site of the removed base CC with both 3'- and 5'-phosphates (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7- CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N- CC methyl)formamidopyrimidine. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96105.1; -; Genomic_DNA. DR PIR; S73783; S73783. DR RefSeq; NP_110068.1; NC_000912.1. DR RefSeq; WP_010874736.1; NC_000912.1. DR ProteinModelPortal; P75402; -. DR EnsemblBacteria; AAB96105; AAB96105; MPN_380. DR GeneID; 876793; -. DR KEGG; mpn:MPN380; -. DR PATRIC; 20022136; VBIMycPne110_0411. DR KO; K10563; -. DR OMA; CQKENYE; -. DR OrthoDB; EOG6QP131; -. DR BioCyc; MPNE272634:GJ6Z-401-MONOMER; -. DR Proteomes; UP000000808; 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 2 277 Formamidopyrimidine-DNA glycosylase. FT /FTId=PRO_0000170837. FT ZN_FING 241 275 FPG-type. FT ACT_SITE 2 2 Schiff-base intermediate with DNA. FT {ECO:0000250}. FT ACT_SITE 3 3 Proton donor. {ECO:0000250}. FT ACT_SITE 59 59 Proton donor; for beta-elimination FT activity. {ECO:0000250}. FT ACT_SITE 265 265 Proton donor; for delta-elimination FT activity. {ECO:0000250}. FT BINDING 94 94 DNA. {ECO:0000250}. FT BINDING 113 113 DNA. {ECO:0000250}. SQ SEQUENCE 277 AA; 31855 MW; 5039E39237229C17 CRC64; MPELPEVATV ITELKSCVLN KPVKQVKVHL DKVLKNTNVK QLNDALVNHS FVDIKRRGKY IIFCLSNGLF LVSHLRMEGK YFFEAKGSQF DLNHVLVEFL FQDGDQLNYH DTRQFGTFHL FNRYQFENAR ELNKLALDPL DQEFNHQAIF NKGHKSNKKI KTFILDQTNI SGIGNIYADE ILFASKIHPE TLAKNLNLSQ YQLICQNATD ILKKAVEMKG TTIGTFTFKK DHTGGYQHFL KIHGKKGKQC QSCNTTIIKK KINGRGSYIC EKCQIQR // ID FRUK_MYCPN Reviewed; 300 AA. AC P75038; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative 1-phosphofructokinase; DE EC=2.7.1.56; DE AltName: Full=Fructose 1-phosphate kinase; GN Name=fruK; OrderedLocusNames=MPN_079; ORFNames=MP076; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 1-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB 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; U00089; AAB95724.1; -; Genomic_DNA. DR PIR; S73402; S73402. DR RefSeq; NP_109767.1; NC_000912.1. DR RefSeq; WP_010874436.1; NC_000912.1. DR ProteinModelPortal; P75038; -. DR IntAct; P75038; 1. DR EnsemblBacteria; AAB95724; AAB95724; MPN_079. DR GeneID; 877096; -. DR KEGG; mpn:MPN079; -. DR PATRIC; 20021439; VBIMycPne110_0080. DR KO; K00882; -. DR OMA; HEMIAYL; -. DR OrthoDB; EOG61KBKF; -. DR BioCyc; MPNE272634:GJ6Z-82-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR017583; Tagatose/fructose_Pkinase. DR Pfam; PF00294; PfkB; 1. DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 300 Putative 1-phosphofructokinase. FT /FTId=PRO_0000080069. SQ SEQUENCE 300 AA; 33588 MW; 7CC8409ECD9BD48E CRC64; MLNHNSKVWI VNYACAIDYY LDKHKQQRGV LTPGGKGINM AIVMALFGIK PTVLTFLGQP TKDLFLQLLK PYQLDLVSFP ATTQTRINVK LLDGAQTTEI NDVTPLIEEQ AVHEMIAYLK ANVKPNDLLV LNGRFLQRDL VKLLDVAFSL TKYVVLDVDE PQLLQLLNQR QPWLMKPNRD EFVAMVNANN SNVDQQELVQ LIKQFQTTQN LLMSDGAQGA YFFDQQQLLF MEAIPPQQLV STTGAGDTLL GVFLANLLLD KDPVGSLKVA VNYASATISK LAVVNSNDQI VLKATNYYYL // ID FTSY_MYCPN Reviewed; 348 AA. AC P75362; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; GN OrderedLocusNames=MPN_425; ORFNames=MP416; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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). {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96064.1; -; Genomic_DNA. DR PIR; S73742; S73742. DR RefSeq; NP_110113.1; NC_000912.1. DR RefSeq; WP_010874781.1; NC_000912.1. DR ProteinModelPortal; P75362; -. DR EnsemblBacteria; AAB96064; AAB96064; MPN_425. DR GeneID; 876833; -. DR KEGG; mpn:MPN425; -. DR PATRIC; 20022246; VBIMycPne110_0460. DR KO; K03110; -. DR OMA; VRNENIE; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; MPNE272634:GJ6Z-454-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00920; FtsY; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004390; SR_rcpt_FtsY. DR InterPro; IPR000897; SRP54_GTPase_dom. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane; KW Nucleotide-binding; Receptor; Reference proteome. FT CHAIN 1 348 Signal recognition particle receptor FT FtsY. FT /FTId=PRO_0000101137. FT NP_BIND 143 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 225 229 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 289 292 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. SQ SEQUENCE 348 AA; 38776 MW; 8A14C4DB9E1EAE29 CRC64; MSFIHKLIQK FKPKKKLVDQ VQQAVQEKSF FQANQKSYYQ GLNKSANSFA NTINKLAANY VTVNEQFQES LFEELVLLDI GYHAATKICD AIVQELKLQR VSDPQLIQEI IVDKLIVYYI QDKLFETDLT VEANKTNVYL FVGVNGVGKT TSLAKLADQL TKQNKRVLMV AGDTFRAGAV AQLAEWAQRI GCDIVLPNPK EETPAVIFRG VQQGIQNEYD FVLCDTSGRL QNKTNLMNEL KKIYQIVQKV SSAKPQETLL VLDGTTGQSG LAQAKVFNEF TELTGIILTK MDSSSKGGII LAIKDLFNLP VKLIGFGETT ADLAAFDLEQ YVLGLTKNLS LNHEPNQT // ID G3P_MYCPN Reviewed; 337 AA. AC P75358; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 109. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83}; DE Short=GAPDH {ECO:0000250|UniProtKB:P9WN83}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P9WN83}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83}; GN Name=gapA; Synonyms=gap; OrderedLocusNames=MPN_430; ORFNames=MP411; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of CC glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) CC using the cofactor NAD. The first reaction step involves the CC formation of a hemiacetal intermediate between G3P and a cysteine CC residue, and this hemiacetal intermediate is then oxidized to a CC thioester, with concomitant reduction of NAD to NADH. The reduced CC NADH is then exchanged with the second NAD, and the thioester is CC attacked by a nucleophilic inorganic phosphate to produce BPG. CC {ECO:0000250|UniProtKB:P9WN83}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000250|UniProtKB:P9WN83}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase 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; U00089; AAB96059.1; -; Genomic_DNA. DR PIR; S73737; S73737. DR RefSeq; NP_110118.1; NC_000912.1. DR RefSeq; WP_010874786.1; NC_000912.1. DR ProteinModelPortal; P75358; -. DR SMR; P75358; 9-337. DR IntAct; P75358; 7. DR EnsemblBacteria; AAB96059; AAB96059; MPN_430. DR GeneID; 876854; -. DR KEGG; mpn:MPN430; -. DR PATRIC; 20022256; VBIMycPne110_0465. DR OMA; GIENGFM; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; MetaCyc:MONOMER-548; -. DR BioCyc; MPNE272634:GJ6Z-459-MONOMER; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. 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; Cytoplasm; Glycolysis; NAD; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145670. FT NP_BIND 17 18 NAD. {ECO:0000250|UniProtKB:P00362}. FT REGION 156 158 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P00362}. FT REGION 215 216 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P00362}. FT ACT_SITE 157 157 Nucleophile. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 39 39 NAD. {ECO:0000250|UniProtKB:P00362}. FT BINDING 83 83 NAD; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 125 125 NAD. {ECO:0000250|UniProtKB:P00362}. FT BINDING 187 187 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 202 202 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 238 238 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 319 319 NAD. {ECO:0000250|UniProtKB:P00362}. FT SITE 184 184 Activates thiol group during catalysis. FT {ECO:0000250|UniProtKB:P00362}. SQ SEQUENCE 337 AA; 36806 MW; 550747A529ABCA83 CRC64; MLAKSKTIRV AINGFGRIGR LVFRALLSQK NIEIVAVNDL THPDTLAHLL KYDSAHGEFK KKVVAKDNTL MIDKKKVLVF SEKDPANLPW AEHNIDIVVE STGRFVSEEG ASLHLQAGAK RVIISAPAKQ KTIKTVVYNV NHKIINAEDK IISAASCTTN CLAPMVHVLE KNFGILHGTM VTVHAYTADQ RLQDAPHSDL RRARAAACNI VPTTTGAAKA IGLVVPEATG KLNGMALRVP VLTGSIVELC VALEKDATVE QINQAMKKAA SASFRYCEDE IVSSDIVGSE HGSIFDSKLT NIIEVDGNKL YKVYAWYDNE SSYVNQLVRV VNYCAKL // ID GALE_MYCPN Reviewed; 338 AA. AC P75517; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=UDP-glucose 4-epimerase; DE EC=5.1.3.2; DE AltName: Full=Galactowaldenase; DE AltName: Full=UDP-galactose 4-epimerase; GN Name=galE; OrderedLocusNames=MPN_257; ORFNames=MP576; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) CC through a mechanism involving the transient reduction of NAD (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96224.1; -; Genomic_DNA. DR PIR; S73902; S73902. DR RefSeq; NP_109945.1; NC_000912.1. DR RefSeq; WP_010874614.1; NC_000912.1. DR ProteinModelPortal; P75517; -. DR IntAct; P75517; 3. DR EnsemblBacteria; AAB96224; AAB96224; MPN_257. DR GeneID; 876834; -. DR KEGG; mpn:MPN257; -. DR PATRIC; 20021839; VBIMycPne110_0276. DR KO; K01784; -. DR OMA; YGIKSVC; -. DR OrthoDB; EOG6WHNS9; -. DR BioCyc; MPNE272634:GJ6Z-264-MONOMER; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF16363; GDP_Man_Dehyd; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01179; galE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Isomerase; NAD; Reference proteome. FT CHAIN 1 338 UDP-glucose 4-epimerase. FT /FTId=PRO_0000183210. FT NP_BIND 16 17 NAD. {ECO:0000250}. FT NP_BIND 37 42 NAD. {ECO:0000250}. FT NP_BIND 59 60 NAD. {ECO:0000250}. FT NP_BIND 81 85 NAD. {ECO:0000250}. FT REGION 198 199 Substrate binding. {ECO:0000250}. FT REGION 215 217 Substrate binding. {ECO:0000250}. FT REGION 294 297 Substrate binding. {ECO:0000250}. FT ACT_SITE 153 153 Proton acceptor. {ECO:0000250}. FT BINDING 126 126 NAD. {ECO:0000250}. FT BINDING 126 126 Substrate. {ECO:0000250}. FT BINDING 153 153 NAD. {ECO:0000250}. FT BINDING 153 153 Substrate. {ECO:0000250}. FT BINDING 157 157 NAD. {ECO:0000250}. FT BINDING 181 181 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 182 182 Substrate. {ECO:0000250}. FT BINDING 230 230 Substrate. {ECO:0000250}. SQ SEQUENCE 338 AA; 38133 MW; 9C50FF3856E68C03 CRC64; MSETKSKVLV LGGLGYIGSC FIDQLLKQYP DVTVSVIDIN HTSLALQLLP RQVNVHFVNL LDRAQLTDTI AQINPDVVFH FAAKTSVKES TEQPLTYFDH NLVGTLNLLH ALKELQKPIQ LFFSSTAAVF GSASTLPIPE NLVLEETLAS NPYGISKFLS EIVLQTLTRS PHFQVIALRY FNVAGASNPF GNFNKNTTLL IPNLIKAFME KRTFFLYGDD YDTKDGSCIR DYIHVVDLCD AHLLAWKWLQ ANPKVRFESF NLGSGQGFSN WEVINTAQAI FAPEQLQLKI ESRRAGDPPV LVVDCTKAKR LLNFQPTRSL HKMLSDETIF YRDFYNRL // ID GALU_MYCPN Reviewed; 291 AA. AC P75124; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase; DE EC=2.7.7.9; DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase; DE AltName: Full=UDP-glucose pyrophosphorylase; DE Short=UDPGP; DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase; GN Name=galU; Synonyms=gtaB; OrderedLocusNames=MPN_667; ORFNames=MP175; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: May play a role in stationary phase survival. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate = CC diphosphate + UDP-glucose. CC -!- SIMILARITY: Belongs to the UDPGP type 2 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; U00089; AAB95823.1; -; Genomic_DNA. DR PIR; S73501; S73501. DR RefSeq; NP_110356.1; NC_000912.1. DR RefSeq; WP_010875024.1; NC_000912.1. DR ProteinModelPortal; P75124; -. DR EnsemblBacteria; AAB95823; AAB95823; MPN_667. DR GeneID; 877017; -. DR KEGG; mpn:MPN667; -. DR PATRIC; 20022819; VBIMycPne110_0732. DR KO; K00963; -. DR OMA; KGWLEAN; -. DR OrthoDB; EOG6Z9B3V; -. DR BioCyc; MetaCyc:MONOMER-642; -. DR BioCyc; MPNE272634:GJ6Z-713-MONOMER; -. DR Proteomes; UP000000808; 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; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 291 UTP--glucose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000201360. SQ SEQUENCE 291 AA; 32168 MW; B422FF63FD64F1CF CRC64; MPKIRKAVIP AAGLGTRLLP ATKAIPKEML PLVNKPTIQY IVEEAVASGI KEILVIVSSK KEAIIDHFDY DFILENALLQ KHKDQEHQEI KDIANLAHIY FVRQKHQHGL GDAILHAKSF VGNEDFAVLL GDDVVFGEQP ALAQCIQAYE QTDCQVIGVQ EVPHDQVNKY GIVTPEANWQ KQALVKILGM VEKPAVNEAK SNLAILSRYI LKPSIFTALK QVPFGVGGEL QLTDGLNYCL QQGEPFFAKH FGGTRFDVGT KNGFIKANLY TALKTDAITK DEVLAILKEF A // ID FTSZ_MYCPN Reviewed; 380 AA. AC P75464; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=MPN_317; ORFNames=MP519; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96167.1; -; Genomic_DNA. DR PIR; S73845; S73845. DR RefSeq; NP_110005.1; NC_000912.1. DR RefSeq; WP_010874673.1; NC_000912.1. DR ProteinModelPortal; P75464; -. DR IntAct; P75464; 4. DR EnsemblBacteria; AAB96167; AAB96167; MPN_317. DR GeneID; 876941; -. DR KEGG; mpn:MPN317; -. DR PATRIC; 20021986; VBIMycPne110_0340. DR KO; K03531; -. DR OMA; QNIDFED; -. DR OrthoDB; EOG6S7XZG; -. DR BioCyc; MPNE272634:GJ6Z-334-MONOMER; -. DR Proteomes; UP000000808; 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; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 380 Cell division protein FtsZ. FT /FTId=PRO_0000114361. FT NP_BIND 27 31 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 119 121 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 150 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 189 189 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. SQ SEQUENCE 380 AA; 42797 MW; 6C3B531C63F4997E CRC64; MDWIQTAGAG TQLPENNIKI AVFGIGGAGN NIIDDMLRMH PELQTANVQF FALNTDLQHL KTKRYVQNKA VIQFEESKGL GVGGDPQKGA VLAHHFLEQF HKLSDSFDFC ILVAGFGKGT GTGATPVFSK FLSNKGVLNL SIVSYPAMCE GLKAREKAAK GLERLNQATD SFMLFRNDRC TDGIYQLANV AIVKTIKNII ELINLPLQQN IDFEDIRSFF KKPAQRLENE ANLFRVTNTF TFSFDAHNTI EHFSHKLKNF EYEGFFDHKV EGAQKVILKV LVNQGLYPLD LTQIQEIIWA KIDNHNLEVQ LGVDFTDANP SVQLFFLMEK KQAVSSDFIQ KPAFISVKEV NQKPAKPFQV LNDLKELGLK YVKQQTGFNY // ID FTSH_MYCPN Reviewed; 709 AA. AC P75120; Q50345; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; GN OrderedLocusNames=MPN_671; ORFNames=MP171; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 530-585. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). 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:0000255|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000255|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; U00089; AAB95819.1; -; Genomic_DNA. DR EMBL; Z32663; CAA83582.1; -; Genomic_DNA. DR PIR; S73497; S73497. DR RefSeq; NP_110360.1; NC_000912.1. DR RefSeq; WP_010875028.1; NC_000912.1. DR ProteinModelPortal; P75120; -. DR SMR; P75120; 225-464. DR MEROPS; M41.009; -. DR EnsemblBacteria; AAB95819; AAB95819; MPN_671. DR GeneID; 877012; -. DR KEGG; mpn:MPN671; -. DR PATRIC; 20022829; VBIMycPne110_0737. DR KO; K03798; -. DR OMA; PLCKSQD; -. DR OrthoDB; EOG6PKFBJ; -. DR BioCyc; MPNE272634:GJ6Z-717-MONOMER; -. DR Proteomes; UP000000808; 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: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; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 709 ATP-dependent zinc metalloprotease FtsH. FT /FTId=PRO_0000084640. FT TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 47 171 Extracellular. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 172 192 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 193 709 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT NP_BIND 268 275 ATP. {ECO:0000255|HAMAP-Rule:MF_01458}. FT ACT_SITE 491 491 {ECO:0000255|HAMAP-Rule:MF_01458}. FT METAL 490 490 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 494 494 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 569 569 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. SQ SEQUENCE 709 AA; 77735 MW; D07585386C8B4C94 CRC64; MKKNKGLNEA TTSEKPQFPK RTAWKIFWWV VILAIIIGIL VYILMPRATT AVIEKWELSG TTLSAQIKGL SGKHTFQRIN NSTYVTDDIL QVSISFQGIN PIVVTAHKAT NGSGETIFNI ANLSINQSTG KAIVNGMMTQ DQKSNNGTEL ASIKGLHDIG TFVAPDTRAR DVLNIFFGLL PIIIFVIFFL LFWRSARGIS GGGRSEEDNI FSIGKTQAKL AKSSVRFDNI AGLQEEKHEL LEIVDYLKNP LKYAQMGARS PRGVILYGPP GTGKTLLAKA VAGEAGVPFF QSTGSGFEDM LVGVGAKRVR DLFNKAKKAA PCIIFIDEID SVGSKRGRVE LSSYSVVEQT LNQLLAEMDG FTSRTGVVVM AATNRLDVLD DALLRPGRFD RHIQINLPDI KEREGILQVH AKNKNLSSKI SLLDVAKRTP GFSGAQLENV INEATLLAVR DNRTTINMND IDEAIDRVIA GPAKKSRVVS DADRKLVAYH EAGHALVGLH VHSNDEVQKI TIIPRGQAGG YTLSTPKSGD LNLKRKSDLL AMIATAMGGR AAEEEIYGPL EITTGASSDF YKATNIARAM VTQLGMSKLG QVQYVPSQGT VPPGTKLFSE QTAKDIDFEI NAIIEEQYKK ARTIIKTNRK ELELLVEALL IAETILKSDI DYIHEHTKLP PEILAQKQEQ QAKQKAEAKE AKLNKKTEKD TEKDSETNS // ID G6PI_MYCPN Reviewed; 430 AA. AC P78033; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN Name=pgi; OrderedLocusNames=MPN_250; ORFNames=MP582; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96230.1; -; Genomic_DNA. DR PIR; S73908; S73908. DR RefSeq; NP_109938.1; NC_000912.1. DR RefSeq; WP_010874607.1; NC_000912.1. DR ProteinModelPortal; P78033; -. DR EnsemblBacteria; AAB96230; AAB96230; MPN_250. DR GeneID; 876909; -. DR KEGG; mpn:MPN250; -. DR PATRIC; 20021825; VBIMycPne110_0269. DR KO; K01810; -. DR OMA; FGYFYFW; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; MetaCyc:MONOMER-544; -. DR BioCyc; MPNE272634:GJ6Z-257-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000808; 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 HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. 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 1 430 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000180686. FT ACT_SITE 284 284 Proton donor. {ECO:0000250}. FT ACT_SITE 305 305 {ECO:0000250}. FT ACT_SITE 420 420 {ECO:0000250}. SQ SEQUENCE 430 AA; 48834 MW; BBF48166F3DCBA70 CRC64; MESKWLTVDT KHLYGFDEAI FIQKYQKKVN QIHQQFLNQQ LPDGHMNGWY SQPDQDHKGL LKQINTIAKQ FNALKVTDIV YLGIGGSYTG IRAILDFLKP EQKANIKVHF VPDISAFNIA AVARAIKGKS WALVVTSKSG RTLEPAVTFR YFRNLLHKQY KQKHALRTVV ITDAVKGLLV GMSNQYGYAH LTIPSNIGGR FSTLSPAGLL LAKLCGHDPK QLLLGTLTAK QELANSDLNT NSAYYYAALR HWLYTTKKLK IEVTVAYHSA YEYLLLQHRQ LFGESEGKGG KSLFPTFSLF TTDLHSMGQL YQEGEKNFFE TVIQVQTQFH DLELPPSDFN NDDQLDYLLA KSMNEISNTA LEAVVEAHFQ SNVNIIKLTL KERTTFMFGY FYFWLSMATM MSGSLLGHNV FDQPGVEVYK QLMFAKLGRE // ID GATA_MYCPN Reviewed; 478 AA. AC P75534; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A; DE Short=Glu-ADT subunit A; DE EC=6.3.5.7; GN Name=gatA; OrderedLocusNames=MPN_237; ORFNames=MP594; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96242.1; -; Genomic_DNA. DR PIR; S73920; S73920. DR RefSeq; NP_109925.1; NC_000912.1. DR RefSeq; WP_010874594.1; NC_000912.1. DR ProteinModelPortal; P75534; -. DR EnsemblBacteria; AAB96242; AAB96242; MPN_237. DR GeneID; 877201; -. DR KEGG; mpn:MPN237; -. DR PATRIC; 20021799; VBIMycPne110_0256. DR KO; K02433; -. DR OMA; TVARWIE; -. DR OrthoDB; EOG61P6R9; -. DR BioCyc; MPNE272634:GJ6Z-244-MONOMER; -. DR Proteomes; UP000000808; 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 1 478 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105179. FT ACT_SITE 68 68 Charge relay system. {ECO:0000250}. FT ACT_SITE 143 143 Charge relay system. {ECO:0000250}. FT ACT_SITE 167 167 Acyl-ester intermediate. {ECO:0000250}. SQ SEQUENCE 478 AA; 53230 MW; F228E9AE4F641071 CRC64; MKSQILKLQQ TLTKKPASIN PLLQQIDGAI NEHWSSNFLL KNTVEWAQAQ APKNRSKSPL NNIPFVLKDN IATKGIVTTG GSRFLEDYIP PFSATVFELL NNSGALLVGK ANLDEFGLGG TGLHSGFGFV HHPWNETLIP GGSSSGSAYA VARGIVPFSI GTDTGDSVRR PASICNIVGF KPTYGLISRN GVYPYAPSLD HVGIFARYVY DVALVSDEII KHDKADFSAQ KSPDAGKFTR SLKESFNKQI KIGYLKPLEE WFDIELSKKW NSLKERITLE GCELIPFHFP LELLEVIDPV YKLISYSEAV SCYSNLTGIV FGQKLFEPNQ ASDFSKTITA NRDRFFGEQL KRRFIIGAFG TDKNNFTKYF EKAQKIRRVM VDAYLNLFKE ADFIVSPSAS GFTKTIAAVQ KGESFTNLVD DFLQLANFAG NPSITIPWLV KQKDQTIGLS VNANCFHDKQ LLQVAAWLEE LFQIEHDD // ID GLF_MYCPN Reviewed; 399 AA. AC P75499; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=UDP-galactopyranose mutase; DE Short=UGM; DE EC=5.4.99.9; DE AltName: Full=UDP-GALP mutase; DE AltName: Full=Uridine 5-diphosphate galactopyranose mutase; GN Name=glf; OrderedLocusNames=MPN_278; ORFNames=MP557; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in the conversion of UDP-GalP into UDP-GalF CC through a 2-keto intermediate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactopyranose = UDP-alpha-D- CC galactofuranose. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose CC mutase 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; U00089; AAB96205.1; -; Genomic_DNA. DR PIR; S73883; S73883. DR RefSeq; NP_109966.1; NC_000912.1. DR RefSeq; WP_010874635.1; NC_000912.1. DR ProteinModelPortal; P75499; -. DR IntAct; P75499; 2. DR PRIDE; P75499; -. DR EnsemblBacteria; AAB96205; AAB96205; MPN_278. DR GeneID; 876844; -. DR KEGG; mpn:MPN278; -. DR PATRIC; 20021883; VBIMycPne110_0298. DR KO; K01854; -. DR OMA; MPENGYT; -. DR OrthoDB; EOG62K1X2; -. DR BioCyc; MPNE272634:GJ6Z-285-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 3. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR004379; UDP-GALP_mutase. DR InterPro; IPR015899; UDP-GalPyranose_mutase_C. DR PANTHER; PTHR21197; PTHR21197; 1. DR Pfam; PF03275; GLF; 1. DR TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Isomerase; Reference proteome. FT CHAIN 1 399 UDP-galactopyranose mutase. FT /FTId=PRO_0000087510. FT NP_BIND 44 45 FAD. {ECO:0000250}. FT NP_BIND 71 72 FAD. {ECO:0000250}. FT NP_BIND 381 386 FAD. {ECO:0000250}. FT BINDING 25 25 FAD. {ECO:0000250}. FT BINDING 52 52 FAD; via amide nitrogen. {ECO:0000250}. FT BINDING 171 171 UDP-GalP. {ECO:0000250}. FT BINDING 175 175 UDP-GalP. {ECO:0000250}. FT BINDING 200 200 UDP-GalP. {ECO:0000250}. FT BINDING 297 297 UDP-GalP. {ECO:0000250}. FT BINDING 306 306 UDP-GalP. {ECO:0000250}. FT BINDING 345 345 UDP-GalP. {ECO:0000250}. FT BINDING 374 374 FAD. {ECO:0000250}. FT BINDING 380 380 UDP-GalP. {ECO:0000250}. SQ SEQUENCE 399 AA; 45910 MW; 53ED30655351639A CRC64; MTLFSFPNYV NWNKFDFIVL GAGISGIVLS HVLAQHGKSV LLLEKRNQLG GNCYDKLDET TGLLFHQYGP HIFHTDNQKV MDFIQPFFEL NNYQHRVGLQ LDNNLDLTLP FDFSQMRKLL DTKTASSLIN FFQQHFPAEK HLTLMQLQTI NFAPVQQLYQ FLKIKVYGPY SVKMWGMPLE QIDPSVLGRV KISLSENSSY FPTATIQGLP KGGYTKAFTK MVDHPLIDLR LNCPANLISV NNNQLLFANQ PITKPVVYCG LIDQLFGYCF GRLQYRSLHF EWKRYAVKQH QAYPVMNWPL HPTITRQVEY KQLTQEGLES NQTIVSCETP GAFREGDPRF MEPYYPLNDV SNNALFARYL KLANAIPNIH LLGRLALYQY IDMDRAIAQS LAKAEQLLQ // ID GATB_MYCPN Reviewed; 477 AA. AC P75533; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; DE Short=Asp/Glu-ADT subunit B; DE EC=6.3.5.-; GN Name=gatB; OrderedLocusNames=MPN_238; ORFNames=MP593; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96241.1; 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; U00089; AAB96241.1; ALT_INIT; Genomic_DNA. DR PIR; S73919; S73919. DR RefSeq; NP_109926.1; NC_000912.1. DR RefSeq; WP_010874595.1; NC_000912.1. DR ProteinModelPortal; P75533; -. DR EnsemblBacteria; AAB96241; AAB96241; MPN_238. DR GeneID; 877221; -. DR KEGG; mpn:MPN238; -. DR PATRIC; 20021801; VBIMycPne110_0257. DR KO; K02434; -. DR OMA; CQLAIAN; -. DR OrthoDB; EOG6RJV5B; -. DR BioCyc; MPNE272634:GJ6Z-245-MONOMER; -. DR Proteomes; UP000000808; 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 1 477 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit B. FT /FTId=PRO_0000148811. SQ SEQUENCE 477 AA; 54431 MW; FAB5E8B5A9E60307 CRC64; MINFEAIIGI EVHVVLNTAT KMFSPAPNQA QNATPNQFIN AIDLGLPGTM PQVNEQAVQK ALILADALNM QRVQPVLVFD RKHYFYQDLP KGFQITQQNF PIAQNGYVEI VENNKAQRII IERFHLEEDT AKQHFVDGQI LLDFNRCGAP LIEVVTAPVI KSAKQSKAYL QKLRQILIVN NISNAKLEDG SMRSDCNVSV RLKGQTAFGT KVEIKNINSL NNVEKAIDLE IARQVKALIK GEPVQQVTLT YDDKTNTNVF MRKKDNSVDY RYFIEPNIMS SNIDELLQKP NKAFNLTEFF TKLKEAGVNE QLNQLVVDDL TLFNAYTKIN SVINSPQDTI RWLCIELMGQ LNKLQKPLKD KTIDHLIILI QMVQKGTVNQ KQAKQLIELM LDNGQDPQSL AKLHNLEQIT DEKQLTQIIQ QIFKENEGEI LKNLDRVERI QKLIIGQVMQ RTHNRANPQQ VFIIVEKLLH DFSERAS // ID GLPK_MYCPN Reviewed; 508 AA. AC P75064; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186}; DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00186}; GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; GN OrderedLocusNames=MPN_050; ORFNames=MP104; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and CC metabolism. Catalyzes the phosphorylation of glycerol to yield sn- CC glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00186}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95752.1; -; Genomic_DNA. DR PIR; S73430; S73430. DR RefSeq; NP_109738.1; NC_000912.1. DR RefSeq; WP_010874407.1; NC_000912.1. DR ProteinModelPortal; P75064; -. DR IntAct; P75064; 1. DR EnsemblBacteria; AAB95752; AAB95752; MPN_050. DR GeneID; 876741; -. DR KEGG; mpn:MPN050; -. DR PATRIC; 20021377; VBIMycPne110_0050. DR KO; K00864; -. DR OMA; GWVEHEP; -. DR OrthoDB; EOG6RZB46; -. DR BioCyc; MPNE272634:GJ6Z-52-MONOMER; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00186; Glycerol_kin; 1. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR005999; Glycerol_kin. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycerol metabolism; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 508 Glycerol kinase. FT /FTId=PRO_0000059468. FT NP_BIND 15 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 419 423 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 85 86 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT REGION 251 252 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 15 15 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 19 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 138 138 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 273 273 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 317 317 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 336 336 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 508 AA; 56591 MW; 8C60F0132DFD62A6 CRC64; MDLKQQYILA LDEGTSSCRT IVFDKDLNQV AIAQNEFNQF FPKSGWVEQD PLEIWSVQLA TMQSAKNKAQ IKSNNIAAVG ITNQRETIVL WNKENGLPVY NAIVWQDQRT ASLCDKLNQD TKIKEFVKKH TGLPINPYFS ATKIAWILEN VPLAQKMLKE DKLLAGTIDT WLIWKLTGGK MHVTDVSNAS RTLLFDITTM TWSQELGDIF KVPLSILPKV MPSNAHFGDI VPSHWSTSAT GMVPIRGVAG DQQAALFGQL CVEPAMVKNT YGTGCFMLMN IGNELKYSQH NLLTTVAWQL ENQKPVYALE GSVFVAGAAL KWLRDSLKVM YSAAESDFYA KLAQKEEQEV VFVPAFTGLG APYWDASARG AIFGIEANTK REHLVKATLE AIAFQANDLI KAMASDLNSS IKKIKADGGA CNSNYLMQFQ ADIANLEVII PKNVETTTMG AAFLAGLAVN YWKDTKQLEK LTGIAKQFKS QMNQTVREKK SKRWNEAVKR TLKWASLD // ID GLYA_MYCPN Reviewed; 406 AA. AC P78011; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 106. 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=MPN_576; ORFNames=MP266; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95914.1; -; Genomic_DNA. DR PIR; S73592; S73592. DR RefSeq; NP_110265.1; NC_000912.1. DR RefSeq; WP_010874933.1; NC_000912.1. DR ProteinModelPortal; P78011; -. DR SMR; P78011; 2-400. DR EnsemblBacteria; AAB95914; AAB95914; MPN_576. DR GeneID; 876801; -. DR KEGG; mpn:MPN576; -. DR PATRIC; 20022631; VBIMycPne110_0638. DR KO; K00600; -. DR OMA; FDTQSPM; -. DR OrthoDB; EOG6Z0QB2; -. DR BioCyc; MetaCyc:MONOMER-581; -. DR BioCyc; MPNE272634:GJ6Z-622-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000808; 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 1 406 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113616. FT REGION 115 117 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 25 25 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 45 45 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 47 47 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 54 54 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 89 89 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 111 111 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 166 166 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 194 194 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 219 219 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 226 226 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 252 252 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 348 348 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 220 220 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00051}. SQ SEQUENCE 406 AA; 45266 MW; 0460FEA4F730E356 CRC64; MEPKIRRILN KELQRQRDCI CLIASENYVS RDILEVTGSI LTNKYAEGYP TRRFYEGCEV VDESESLAIN TCKELFGAKW ANVQPHSGSS ANYAVYLALL KPGDAILGLD LNCGGHLTHG NKFNFSGKQY QPYSYTINPE TEMLDYDEVL RVAREVKPKL IICGFSNYSR TVDFERFSAI AKEVGAYLLA DIAHIAGLVA AGLHPNPLPY TDVVTSTTHK TLRGPRGGLI MSNNEAIIRK LDSGVFPGCQ GGPLQHVIAA KYVCFKEALQ PKYKQYIQNV KTNAASMASW FKQQGYRVIS NGTDTHLFSL DVGKGKDVSQ WLQQANIVLN MNTVPFDKNP AINPSGIRIG TPAMTTRGFK EKHFLYVAAL IDKIIKSDGN KKVIKEVKKA VLKLLERFPL YKGLEY // ID GRPE_MYCPN Reviewed; 217 AA. AC P78017; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. 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=MPN_120; ORFNames=MP034; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Participates actively in the response to hyperosmotic CC and heat shock by preventing the aggregation of stress-denatured CC proteins, in association with DnaK and GrpE. It is the nucleotide CC exchange factor for DnaK and may function as a thermosensor. CC Unfolded proteins bind initially to DnaJ; upon interaction with CC the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting CC in the formation of a stable complex. GrpE releases ADP from DnaK; CC ATP binding to DnaK triggers the release of the substrate protein, CC thus completing the reaction cycle. Several rounds of ATP- CC dependent interactions between DnaJ, DnaK and GrpE are required CC for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. 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; U00089; AAB95682.1; -; Genomic_DNA. DR PIR; S73360; S73360. DR RefSeq; NP_109808.1; NC_000912.1. DR RefSeq; WP_010874477.1; NC_000912.1. DR ProteinModelPortal; P78017; -. DR IntAct; P78017; 1. DR EnsemblBacteria; AAB95682; AAB95682; MPN_120. DR GeneID; 877237; -. DR KEGG; mpn:MPN120; -. DR PATRIC; 20021539; VBIMycPne110_0127. DR KO; K03687; -. DR OMA; QPFFEDF; -. DR OrthoDB; EOG64BQ6C; -. DR BioCyc; MPNE272634:GJ6Z-126-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Stress response. FT CHAIN 1 217 Protein GrpE. FT /FTId=PRO_0000113821. SQ SEQUENCE 217 AA; 24706 MW; 3C66757AF4BEBEC3 CRC64; MSENSLTITE ILSSIRTLLV KHNKAKVTQI EKELLQAVAE LEKKFKQQVQ NFNELQQKIP NLQKVNEEFR LKVEKIQEEA QKKIQEKVAE LTIKSKEELE NAKKYVIEKS IDQPLIIIDQ FEIALSYAQK DPQVKNYTTG FNMVLDAFSR WLEGFGVTKI AIEPGAQFDE KVMAALEVVP SDQPANTVVK VSKSGYKLHD KVIRFASVVV SQGNKTE // ID GLPF_MYCPN Reviewed; 264 AA. AC P75071; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Probable glycerol uptake facilitator protein; GN Name=glpF; OrderedLocusNames=MPN_043; ORFNames=MP111; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Glycerol enters the cell via the glycerol diffusion CC facilitator protein. This membrane protein facilitates the CC movement of glycerol across the cytoplasmic membrane (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing CC three membrane-spanning domains and a pore-forming loop with the CC signature motif Asn-Pro-Ala (NPA). CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) 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; U00089; AAB95759.1; -; Genomic_DNA. DR PIR; S73437; S73437. DR RefSeq; NP_109731.1; NC_000912.1. DR RefSeq; WP_010874400.1; NC_000912.1. DR ProteinModelPortal; P75071; -. DR EnsemblBacteria; AAB95759; AAB95759; MPN_043. DR GeneID; 877407; -. DR KEGG; mpn:MPN043; -. DR PATRIC; 20021361; VBIMycPne110_0042. DR KO; K02440; -. DR OMA; LSYQSGW; -. DR OrthoDB; EOG6P8TRZ; -. DR BioCyc; MPNE272634:GJ6Z-45-MONOMER; -. DR Proteomes; UP000000808; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000425; MIP. DR InterPro; IPR022357; MIP_CS. DR PANTHER; PTHR19139; PTHR19139; 2. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; SSF81338; 1. DR PROSITE; PS00221; MIP; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Glycerol metabolism; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 264 Probable glycerol uptake facilitator FT protein. FT /FTId=PRO_0000064088. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 244 264 Helical. {ECO:0000255}. FT MOTIF 78 80 NPA 1. FT MOTIF 216 218 NPA 2. SQ SEQUENCE 264 AA; 28305 MW; 56A3FBD375A059CC CRC64; MFNLSDFSEL PRWIGAEFLG TFFLILSGNG AGSQLTLNKM FAKESKAKLL TAAFAWGIAV LVGVLIANSL FEGAGNINPA VSLFYAVSGT IQKALYPLHV NFSIPLLWVA LLLAWVAQFA GAMLAQALLN FLFWKHIEQT DPQSVLVTHC TNPAIFNIPR NFATEFVATS VLIASLLVAG SFGANRFDQS PRGVVPMLVV TGLIMSFGAA TGTAINPARD LGPRIVYWLS PIKNKDPNLK YSWIPVAAPL SASVILGVLV AVIV // ID GREA_MYCPN Reviewed; 160 AA. AC P78019; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Transcription elongation factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; DE AltName: Full=Transcript cleavage factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; GN Name=greA {ECO:0000255|HAMAP-Rule:MF_00105}; GN OrderedLocusNames=MPN_401; ORFNames=MP437; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription CC elongation past template-encoded arresting sites. The arresting CC sites in DNA have the property of trapping a certain fraction of CC elongating RNA polymerases that pass through, resulting in locked CC ternary complexes. Cleavage of the nascent transcript by cleavage CC factors such as GreA or GreB allows the resumption of elongation CC from the new 3'terminus. GreA releases sequences of 2 to 3 CC nucleotides. {ECO:0000255|HAMAP-Rule:MF_00105}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000255|HAMAP- CC Rule:MF_00105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96085.1; -; Genomic_DNA. DR PIR; S73763; S73763. DR RefSeq; NP_110089.1; NC_000912.1. DR RefSeq; WP_010874757.1; NC_000912.1. DR ProteinModelPortal; P78019; -. DR IntAct; P78019; 2. DR EnsemblBacteria; AAB96085; AAB96085; MPN_401. DR GeneID; 877111; -. DR KEGG; mpn:MPN401; -. DR PATRIC; 20022190; VBIMycPne110_0433. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; MPNE272634:GJ6Z-429-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.180; -; 1. DR Gene3D; 3.10.50.30; -; 1. DR HAMAP; MF_00105; GreA_GreB; 1. DR InterPro; IPR018151; TF_GreA/GreB_CS. DR InterPro; IPR006359; Tscrpt_elong_fac_GreA. DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B. DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C. DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam. DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N. DR Pfam; PF01272; GreA_GreB; 1. DR Pfam; PF03449; GreA_GreB_N; 1. DR PIRSF; PIRSF006092; GreA_GreB; 1. DR SUPFAM; SSF46557; SSF46557; 1. DR TIGRFAMs; TIGR01462; greA; 1. DR PROSITE; PS00829; GREAB_1; 1. DR PROSITE; PS00830; GREAB_2; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 160 Transcription elongation factor GreA. FT /FTId=PRO_0000176941. FT COILED 8 28 {ECO:0000255|HAMAP-Rule:MF_00105}. SQ SEQUENCE 160 AA; 18101 MW; 32448C91712A19C2 CRC64; MELNKNYLTE EGLKQLEAEL EHLIQVKRPA IIKLLQEARD QGDLSENADY DAAKAQQGEI ETRIAEIQDI LANVKLINES QTKKANKVTL GSTVEIYDYS SKTHEKYTIV GALEANPEEH RISNESPLAH AIYGRLVDDE CDVVGIEVPY RVKIVKIINW // ID GYRA_MYCPN Reviewed; 839 AA. AC P22446; P75108; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 16-MAR-2016, entry version 107. DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; GN OrderedLocusNames=MPN_004; ORFNames=MP150; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. RX PubMed=2172693; DOI=10.1111/j.1365-2958.1990.tb00687.x; RA Colman S.D., Hu P.C., Bott K.F.; RT "Mycoplasma pneumoniae DNA gyrase genes."; RL Mol. Microbiol. 4:1129-1134(1990). RN [3] RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01897}. 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:0000255|HAMAP- CC Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. {ECO:0000255|HAMAP-Rule:MF_01897}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95798.1; -; Genomic_DNA. DR EMBL; X53555; CAA37623.1; -; Genomic_DNA. DR PIR; S73476; S73476. DR RefSeq; NP_109692.1; NC_000912.1. DR RefSeq; WP_010874361.1; NC_000912.1. DR ProteinModelPortal; P22446; -. DR IntAct; P22446; 6. DR PRIDE; P22446; -. DR EnsemblBacteria; AAB95798; AAB95798; MPN_004. DR GeneID; 877234; -. DR KEGG; mpn:MPN004; -. DR PATRIC; 20021281; VBIMycPne110_0004. DR KO; K02469; -. DR OMA; ESYLAYS; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; MPNE272634:GJ6Z-4-MONOMER; -. DR Proteomes; UP000000808; 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; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. 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 Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; KW DNA-binding; Isomerase; Nucleotide-binding; Reference proteome; KW Topoisomerase. FT CHAIN 1 839 DNA gyrase subunit A. FT /FTId=PRO_0000145241. FT MOTIF 537 543 GyrA-box. {ECO:0000255|HAMAP- FT Rule:MF_01897}. FT ACT_SITE 134 134 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01897}. SQ SEQUENCE 839 AA; 93357 MW; C499618577714AFE CRC64; MAKQQDQIDK IRQELAQSAI KNISLSSELE RSFMEYAMSV IVARALPDAR DGLKPVHRRV LYGAYTGGMH HDRPFKKSAR IVGDVMSKFH PHGDMAIYDT MSRMAQDFSL RYLLIDGHGN FGSIDGDRPA AQRYTEARLS KLAGELLRDI DKDTVDFVAN YDGEEQEPTV LPAAFPNLLA NGSSGIAVGM STSIPSHNLS ELIQGLILLI DNPDCTINDL LGVIKGPDFP TGANIIYTKG IESYFETGKG NVVIRSKVSI EQLPTRAALV VTEIPYMVNK TSLIEKIVEL VKAEEITGIA DIRDESSREG IRLVIEVKRD TVPEVLLNQL FKSTRLQVRF PVNMLALVKG APKLLNMKQA LTVYLEHQLD VLIRKTQFNL KKYQERFHIL SGLLIAALNI DEVIAIIKKS ANNQVAMEAL HERFGLDEIQ ARAVLDMRLR SLSVLEVNKL QTEQQELKAL IEFCQQVLAD KQLQLKLIKE QLTKINEQFG DPRRSEILYG ISEDIDDEDL ITQENVVITM STNGYLKRIG VDAYNLQHRG GVGVKGLTTY TDDSISQLLV CSTHSDLLFF TDKGKVYRIR AHQIPPGFRT NKGIPAVNLI KIDKDEKICA LISVNDYQNG YFFFCTKNGT IKRTSLSEFA NILSIGKRAI LFKENDVLFS VIRTSGQDDI FIGSTAGFVV RFHEDTVRPL SRAAMGVLGI NLNQCEFVNG LSTSSNGSLL LSVGQNGIGK LTSIDKYRLT KRNAKGVKTL RVTAKTGPVV TTTTVFGNED LLMISSAGKI VRISLEQLSE QRKNTSGVKL IKLKEKERLE TVTIFKKEEA IKTTTATETD DVGSKQITQ // ID GPMI_MYCPN Reviewed; 508 AA. AC P75167; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038}; DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038}; GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm; GN OrderedLocusNames=MPN_628; ORFNames=MP214; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01038}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01038}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01038}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000255|HAMAP-Rule:MF_01038}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95862.1; -; Genomic_DNA. DR PIR; S73540; S73540. DR RefSeq; NP_110317.1; NC_000912.1. DR RefSeq; WP_010874985.1; NC_000912.1. DR ProteinModelPortal; P75167; -. DR IntAct; P75167; 4. DR EnsemblBacteria; AAB95862; AAB95862; MPN_628. DR GeneID; 877355; -. DR KEGG; mpn:MPN628; -. DR PATRIC; 20022739; VBIMycPne110_0692. DR KO; K15633; -. DR OMA; LHIATMT; -. DR OrthoDB; EOG6HJ22X; -. DR BioCyc; MetaCyc:MONOMER-550; -. DR BioCyc; MPNE272634:GJ6Z-674-MONOMER; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1450.10; -; 1. DR Gene3D; 3.40.720.10; -; 2. DR HAMAP; MF_01038; GpmI; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR011258; BPG-indep_PGM_N. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR005995; Pgm_bpd_ind. DR Pfam; PF06415; iPGM_N; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001492; IPGAM; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR SUPFAM; SSF64158; SSF64158; 1. DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 508 2,3-bisphosphoglycerate-independent FT phosphoglycerate mutase. FT /FTId=PRO_0000212175. FT REGION 150 151 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT REGION 257 260 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT ACT_SITE 61 61 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01038}. FT METAL 11 11 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 61 61 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 397 397 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 401 401 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 438 438 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 439 439 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 456 456 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 182 182 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 188 188 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 332 332 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. SQ SEQUENCE 508 AA; 56375 MW; A856375375B09F5E CRC64; MHKKVLLAIL DGYGISNKQH GNAVYHAKTP ALDSLIKDYP CVMLEASGEA VGLPQGQIGN SEVGHLNIGA GRIVYTGLSL INQNIKTGAF HHNQVLLEAI ARAKANNAKL HLIGLFSHGG VHSHMDHLYA LIKLAAPQVK MVLHLFGDGR DVAPCTMKSD LEAFMVFLKD YHNVIIGTLG GRYYGMDRDQ RWDREEIAYN AILGNSKASF TDPVAYVQSA YDQKVTDEFL YPAVNGNVDK EQFALKDHDS VIFFNFRPDR ARQMSHMLFQ TDYYDYTPKA GRKYNLFFVT MMNYEGIKPS AVVFPPETIP NTFGEVIAHN KLKQLRIAET EKYAHVTFFF DGGVEVDLPN ETKCMVPSLK VATYDLAPEM ACKGITDQLL NQINQFDLTV LNFANPDMVG HTGNYAACVQ GLEALDVQIQ RIIDFCKANH ITLFLTADHG NAEEMIDSNN NPVTKHTVNK VPFVCTDTNI DLQQDSASLA NIAPTILAYL GLKQPAEMTA NSLLISKK // ID GYRB_MYCPN Reviewed; 650 AA. AC P22447; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 16-MAR-2016, entry version 107. DE RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01898}; GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; GN OrderedLocusNames=MPN_003; ORFNames=MP151; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2172693; DOI=10.1111/j.1365-2958.1990.tb00687.x; RA Colman S.D., Hu P.C., Bott K.F.; RT "Mycoplasma pneumoniae DNA gyrase genes."; RL Mol. Microbiol. 4:1129-1134(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-637. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP- CC Rule:MF_01898}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|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; X53555; CAA37622.1; -; Genomic_DNA. DR EMBL; U00089; AAB95799.1; -; Genomic_DNA. DR EMBL; U34816; AAC43643.1; -; Genomic_DNA. DR PIR; S11767; ISYMBP. DR RefSeq; NP_109691.1; NC_000912.1. DR RefSeq; WP_010874360.1; NC_000912.1. DR ProteinModelPortal; P22447; -. DR IntAct; P22447; 5. DR EnsemblBacteria; AAB95799; AAB95799; MPN_003. DR GeneID; 877190; -. DR KEGG; mpn:MPN003; -. DR PATRIC; 20021279; VBIMycPne110_0003. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; MPNE272634:GJ6Z-3-MONOMER; -. DR Proteomes; UP000000808; 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; -; 1. 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; 1. DR TIGRFAMs; TIGR01059; gyrB; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; KW Topoisomerase. FT CHAIN 1 650 DNA gyrase subunit B. FT /FTId=PRO_0000145323. FT DOMAIN 435 549 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 441 441 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 514 514 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 514 514 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 516 516 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 466 466 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 469 469 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. SQ SEQUENCE 650 AA; 73810 MW; 2882D0BE1B7A349D CRC64; MEDNNKTQAY DSSSIKILEG LEAVRKRPGM YIGSTGEEGL HHMIWEIIDN SIDEAMGGFA STVKLTLKDN FVTIVEDDGR GIPVDIHPKT NRSTVETVFT VLHAGGKFDN DSYKVSGGLH GVGASVVNAL SSSFKVWVAR EHQQYFLAFH NGGEVIGDLV NEGKCDKEHG TKVEFVPDFT VMEKSDYKQT VIASRLQQLA FLNKGIQIDF VDERRQNPQS FSWKYDGGLV QYIHHLNNEK EPLFEDIIFG EKTDTVKSVS RDESYTIKVE VAFQYNKTYN QSIFSFCNNI NTTEGGTHVE GFRNALVKII NRFAVENKFL KETDEKITRD DICEGLTAII SIKHPNPQYE GQTKKKLGNT EVRPLVNSIV SEIFERFMLE NPQEANAIIR KTLLAQEARR RSQEARELTR RKSPFDSGSL PGKLADCTTR DPSISELYIV EGDSAGGTAK TGRDRYFQAI LPLRGKILNV EKSHFEQIFN NVEISALVMA VGCGIKPDFE LEKLRYNKII IMTDADVDGA HIRTLLLTFF FRFMYPLVEQ GNIYIAQPPL YKVSYSNKDL YMQTDVQLEE WKQQHPNLKY NLQRYKGLGE MDAIQLWETT MDPKVRTLLK VTVEDASIAD KAFSLLMGDE VPPRREFIEQ NARNVKNIDI // ID HMW1_MYCPN Reviewed; 1018 AA. AC Q50365; Q50348; Q50349; Q9R5R4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Cytadherence high molecular weight protein 1; DE AltName: Full=Cytadherence accessory protein 1; GN Name=hmw1; OrderedLocusNames=MPN_447; ORFNames=MP394; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-180. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). RN [4] RP PROTEIN SEQUENCE OF 176-182 AND 188-198. RX PubMed=1743522; DOI=10.1016/0378-1119(91)90300-Z; RA Krause D.C., Lee K.K.; RT "Juxtaposition of the genes encoding Mycoplasma pneumoniae RT cytadherence-accessory proteins HMW1 and HMW3."; RL Gene 107:83-89(1991). RN [5] RP PHOSPHORYLATION. RX PubMed=7635846; RA Krebes K.A., Dirksen L.B., Krause D.C.; RT "Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory RT proteins in cell extracts."; RL J. Bacteriol. 177:4571-4574(1995). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less Mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane. Note=Localizes specifically to the attachment membrane. CC -!- PTM: Phosphorylated mainly on serine residues. CC {ECO:0000269|PubMed:7635846}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38997; AAA61697.1; -; Genomic_DNA. DR EMBL; U00089; AAB96042.1; -; Genomic_DNA. DR EMBL; Z32661; CAA83580.1; -; Genomic_DNA. DR EMBL; Z32662; CAA83581.1; -; Genomic_DNA. DR PIR; S73720; S73720. DR RefSeq; NP_110135.1; NC_000912.1. DR RefSeq; WP_010874803.1; NC_000912.1. DR EnsemblBacteria; AAB96042; AAB96042; MPN_447. DR GeneID; 877120; -. DR KEGG; mpn:MPN447; -. DR PATRIC; 20022292; VBIMycPne110_0483. DR OMA; EMVQPEV; -. DR OrthoDB; EOG6DVJQC; -. DR BioCyc; MPNE272634:GJ6Z-476-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR022466; AGR_box. DR InterPro; IPR021199; Cytadherence_HMW-1_N. DR Pfam; PF16713; EAGR_box; 1. DR TIGRFAMs; TIGR03834; EAGR_box; 1. DR TIGRFAMs; TIGR03836; termin_org_HMW1; 1. PE 1: Evidence at protein level; KW Cell membrane; Cell projection; Coiled coil; Complete proteome; KW Cytadherence; Direct protein sequencing; Membrane; Phosphoprotein; KW Reference proteome; Virulence. FT CHAIN 1 1018 Cytadherence high molecular weight FT protein 1. FT /FTId=PRO_0000084012. FT COILED 782 815 {ECO:0000255}. FT COILED 849 880 {ECO:0000255}. FT COMPBIAS 91 465 Glu-rich. FT CONFLICT 198 198 E -> I (in Ref. 4; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 1018 AA; 112215 MW; 3C3DEB273F9ABDE7 CRC64; MKKSKEAVFE DKDYTEENPE QIFGNLYDGK LTVQDGKVKI AYDGDGNGYY IAFNSETGVY YDPYGDTEYD ISVLFDANGN SFVFADAPTV EVLAGEQEQT EAEPDYLQYV GNEAYGYYDE AGEWVWSGYF EGDQWISTLP QTEAEEKQFG FEDNIETTPT ASEDFGLEAD VPAPEVAEPS YEVQPEVAAE PVYDVQPEVA VEPVGETTAT VEPQAVEIQP EVVVEPIVES QLEQPVEVQA EMVQPEVAVE PQLEVSLDPI GETAPILEQV EPQAVQTQPE IPAEQSAVEL QPEPVAEVQS EMVQPEAAAE PVTEAQQTEP TPVVETIAEI TPQVVTEPVV AVVEHQPEAV AEPLPVEPAV AGVSELIPTE QVQPEVVVES TPVAEVQSEM VQPEVAVEPI VEPQPEQPVE VQPEVITTPE VASVLEVQPE NPVVEVEQVV EPQPETPVEV QPEPVVETVQ EAVAEPTQVV EPQPQAAPQP AVYEWNLTPE AAPVEQPEVI PVTVVESQAT ATAEPQPAVA PVADMDYVLH LTDTVKNQPQ TAPVQPTTPI KIEVAESTPT VTTSPVEPTI APPLFEIELN NTTSSDLPLV EVVDFKHNQH GAVGTHSFDD FTPPEVGMES KTHCHSNSEV VWRVSEPKTV PVPPAVSSIN IQTVNRVVEP TISTPTTPVV ESAPAIEIFV DTPPVETKEA SSNVDVVQQP VKPLMPVMVE QLRTTELQPT TEINLFANSD INSIIAELKQ GRSNPAINFD DIFKMSSYQM VVKKSFVQIS DFITNSKTDI TNRFLLIKKE LQAELTRLIE ENEQLKAEFL NAKDLSVYQK DELLRSLSND FTIAHRPSDS YEQLQKSGEL VRNIQKAILE NESKIKNIQI TLKELKAVYK LCSDTVLNGM AKLDSVLRFN KKEKDPLLLN SMETLSSFET EPQAIIEDLL DFSSSFDKMS NEQLDEFVYQ NLDSGLNLDL DGFDHQLSSM NIHGLEPLDP MKLDDFDFET LTPDKTSNLS SILDDELMEN GGDFNLDY // ID HMW2_MYCPN Reviewed; 1818 AA. AC P75471; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Cytadherence high molecular weight protein 2; DE AltName: Full=Cytadherence accessory protein 2; GN Name=hmw2; OrderedLocusNames=MPN_310; ORFNames=MP526; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). RN [3] RP PHOSPHORYLATION. RX PubMed=7635846; RA Krebes K.A., Dirksen L.B., Krause D.C.; RT "Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory RT proteins in cell extracts."; RL J. Bacteriol. 177:4571-4574(1995). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less Mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle (By CC similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated mainly on serine residues. CC {ECO:0000269|PubMed:7635846}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96174.1; -; Genomic_DNA. DR EMBL; U59896; AAB52527.1; -; Genomic_DNA. DR PIR; S73852; S73852. DR RefSeq; NP_109998.1; NC_000912.1. DR RefSeq; WP_010874666.1; NC_000912.1. DR ProteinModelPortal; P75471; -. DR IntAct; P75471; 1. DR PRIDE; P75471; -. DR EnsemblBacteria; AAB96174; AAB96174; MPN_310. DR GeneID; 876917; -. DR KEGG; mpn:MPN310; -. DR PATRIC; 20021972; VBIMycPne110_0334. DR OMA; QAFNQIN; -. DR OrthoDB; EOG6N3CNZ; -. DR BioCyc; MPNE272634:GJ6Z-326-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR016430; Cytadherence_Hmw2. DR PIRSF; PIRSF004800; Hmw2; 1. PE 1: Evidence at protein level; KW Coiled coil; Complete proteome; Cytadherence; Phosphoprotein; KW Reference proteome; Virulence. FT CHAIN 1 1818 Cytadherence high molecular weight FT protein 2. FT /FTId=PRO_0000084014. FT COILED 31 880 {ECO:0000255}. FT COILED 919 1607 {ECO:0000255}. FT COILED 1644 1755 {ECO:0000255}. FT COILED 1786 1817 {ECO:0000255}. SQ SEQUENCE 1818 AA; 215622 MW; 66DF4B08F0FCFBC0 CRC64; MNDTDKKFPL QPVYDTGFDD GYLQRDYEKC LESAAANDAQ TVELQTQLLA EIKNLENEIK ALKAQESRQP DPHNNARIQS LEASLNRLVN EYNNFEFQKN YMVDRVAELN NKARFFKDEL KRLQQENAAF VNSRYANWAD FQSNYQLKLD QFQALIDQQN QTIKQLNEQI AANQGLIDQN VQRLQQNHSL DQQERDALLY EVDHLYNELY ELENQKRLVG IEYEATYQDL VSADAELQNV YETIAQNQAN FQKQCDAYWA QLKQVEQQIQ TTKQELVDEE STLKVRLNDA DFYINSRLAE LDDLTSKINE RDFVSKEQAQ DVKASLANLT KEKERLSAEK DSFERLRNTA LNDINRMEQE NALFAKHLEQ QQYEFERKQQ ESLLKLETEH KQLQKRIGEF KIESEAKSEA LLIQERELLE KRREIDDLLT QASLEYEQQR RTNQVLKEKH RQVQQHFQNL VHAKKKLDQK RHYLAEQKRI DEEQIFKLKE KIATERRELE KLYLVKKQKQ DQKENDLLIF EKQLRQYQAD FENEIEEKQN ELFASQKSLQ KSFTQLKNKE AELNQKAQKI AEDWAHLKQN KHHHADLEIF LEGEFNHLQQ EKHKLLEART QFDNRVSLLS ARFKQKQAEL VKQKQSLEQL TAAFNKEQEA VERDWKDRLA NLEKQKEMLG DKVHQFDENS LNISKKLAER ELAIKFKEKE LEAAQKQLSL DNNNNAGLKL QLDKLSESLK TERLELEASK ERILDFYDES SRRIADYESD LQARLAEVKT LEKNQQETAA KSERELKVAL EKLNQAKKAF LQIRKQQLLE IASVKQQLAQ KANLLKNQQA ELDKQTEELE AAFLEQDTDK KELEKALHSV KSKQELLERE RSFLLQKQRE FAEHVAGFKR QVHFKTTQMQ RLSEFNKQQQ SEQIKRETEL KIAFADLKKD YQLFELQKNQ EFQQIEQKHK ELELLAQKQA ELKQELEQKA TALASQDQDT VQAKLDLARQ QHELELRQNA FNQASLSLNK QREQLTNQVK VLHGELKKRH EKLTLKDRLL AEKEKDQHKK DAEINQRFKQ FENEYADFDQ AKKRELQELN QIRRNLEQSN ASLLKKRNQL TLDFALLRKV QHNTQTNRVQ LNTQIKEFLL EKKNFQKASD EAALQKALLI KRLRSFASKL QLQREALAIQ KLEFDKRDEQ QKSEINNAKL QLEQFKLEKQ NFDEAKQKQL IEFKDQCQRL DVEKRLLKQK LVQLKNLSKS YLTYKNRADL SQQQLQHKYA NLLELKEKLQ TAKRALDKKH RAIYGKMAQF VSELRQEKKQ LLSAQKQVDD KSRLLEQNQR HLQNLSSETK KKRQSLEHDI NKFDQRRKEA VSSILNSHKK LKQKEGELQG ILQKLSLKKT QIEQEFSKLY QQREKLDRQR TTLSKLHREL KAQNEATAHK NREVLEIENY YKKELQRLTT EKSEFDNNKN RLFEYFRKIR NEIEKKEAHI KTVLEETQKK RHLVETEAVK LHLQKQSIIS KGQELKEIKE RVSRDISHTN KQREELNSLL HQNKLLQKNL AEREREINNK DSLLTQKIQT AKQKLSEKEA RILKLLEKMR AVEQQYQAEI TRLKTRNADL EKNDNKHLFP PLFKINGNDM NYPYPYPWFY PQQKQEDSSN QIRHLFEQQL QFMQQRYENE LTELRRQRAL LEKKLDQIQL ESQLSAKKND FEKVEQMMQK LLEKTEQKLS AFDQKINALA EQINTQKAEH ADSEKQQLLL RIEQLEKQNL AQAVQTPQPV QPVVQAPAVV PQVIQPQVVQ SQPAFLATQQ SISKQQQIAQ LNAEINSIKK LIAQKAAK // ID HMW3_MYCPN Reviewed; 672 AA. AC Q50360; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Cytadherence high molecular weight protein 3; DE AltName: Full=Accessory adhesin protein 3; DE AltName: Full=Cytadherence accessory protein 3; GN Name=hmw3; OrderedLocusNames=MPN_452; ORFNames=MP389; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29. RC STRAIN=ATCC 29342 / M129-B17; RX PubMed=1548085; RA Ogle K.F., Lee K.K., Krause D.C.; RT "Nucleotide sequence analysis reveals novel features of the phase- RT variable cytadherence accessory protein HMW3 of Mycoplasma RT pneumoniae."; RL Infect. Immun. 60:1633-1641(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP PROTEIN SEQUENCE OF 279-290. RC STRAIN=ATCC 29342 / M129-B17; RX PubMed=1899847; DOI=10.1016/0378-1119(91)90011-Y; RA Ogle K.F., Lee K.K., Krause D.C.; RT "Cloning and analysis of the gene encoding the cytadherence phase- RT variable protein HMW3 from Mycoplasma pneumoniae."; RL Gene 97:69-75(1991). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle. Essential CC for successful surface parasitism. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane. Note=Localizes specifically to the attachment membrane. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38997; AAA61692.1; -; Genomic_DNA. DR EMBL; U00089; AAB96037.1; -; Genomic_DNA. DR PIR; S73715; S73715. DR RefSeq; NP_110140.1; NC_000912.1. DR RefSeq; WP_010874808.1; NC_000912.1. DR ProteinModelPortal; Q50360; -. DR IntAct; Q50360; 2. DR EnsemblBacteria; AAB96037; AAB96037; MPN_452. DR GeneID; 877094; -. DR KEGG; mpn:MPN452; -. DR PATRIC; 20022302; VBIMycPne110_0488. DR OMA; PLPKYTP; -. DR BioCyc; MPNE272634:GJ6Z-481-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Cell membrane; Cell projection; Complete proteome; Cytadherence; KW Direct protein sequencing; Membrane; Reference proteome; Repeat; KW Virulence. FT CHAIN 1 672 Cytadherence high molecular weight FT protein 3. FT /FTId=PRO_0000084016. FT REPEAT 98 100 1-1. FT REPEAT 106 108 1-2. FT REPEAT 160 162 2-1. FT REPEAT 197 199 1-3. FT REPEAT 206 208 1-4. FT REPEAT 211 213 1-5. FT REPEAT 221 223 1-6. FT REPEAT 226 228 1-7. FT REPEAT 235 237 1-8. FT REPEAT 249 251 1-9. FT REPEAT 288 290 2-2. FT REPEAT 310 319 3-1. FT REPEAT 312 316 4-1. FT REPEAT 316 318 2-3. FT REPEAT 322 324 2-4. FT REPEAT 330 339 3-2. FT REPEAT 332 336 4-2. FT REPEAT 336 338 2-5. FT REPEAT 354 358 4-3. FT REPEAT 385 389 4-4. FT REPEAT 396 400 4-5. FT REPEAT 402 404 2-6. FT REPEAT 413 415 2-7. FT REPEAT 424 428 4-6. FT REPEAT 454 456 2-8. FT REGION 98 251 9 X 3 AA repeats OF Y-D-Q. FT REGION 160 456 8 X 3 AA repeats of P-V-V. FT REGION 310 339 2 X 10 AA repeats of V-E-P-T-P-T-P-V-V-E. FT REGION 312 428 6 X 5 AA repeats of P-X-P-X-P. FT COMPBIAS 275 488 Pro-rich. FT CONFLICT 288 288 P -> R (in Ref. 3; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 672 AA; 73721 MW; 1FD2345F5850777D CRC64; MTDKERAKLA KAYGKLAQKI QKSYPDINVV YGRDAKNKLH ALYQDPETGN IFSLEKRKQL PADYPLFELD SDEPISFAPK IIPLTAFDGN NNEVIVQYDQ VNNTFYDQDG NVLDVSGYRD GENIPLVDYL NYGGSTASAD TTTSEPLSGE GYPDIDAGLP VVDPDATPEQ QADQLFGLDP LPQAPDEYQD TTAPPAYDQT FDQATYDQQA YDQNYDPNAY YDQQAYDQSF DQQAYDQAYD ANAYNTQNYD QAHDPNAYYD SQAYSDPDQA SAVAPIEVAP LQPEPVAPVV EPTAVPIVES APIVEVTPTV EPTPTPVVET APVVEAPKVV EPTPTPVVEA TPAPKVEPKV VEQPQPTPVT VEVDSPKVEI PKVVTAKVAL QVAQPTPVPA VPKVAPQPTP APVVVQPTAV VQPVVKAEPK VVTPTPAPQV VVTPQVATPK VTPKVVQTTP AVPPVVVQPE VVVQPIIRPT QPEPEWKPSP ASVVEPQPCQ SACVNNESGA ITIHTTNRSL LLEKLASLGH LHDASTRTPL PHERYQLAPP SEYVATKYNE PLFNLPAIRN SWARFTRPTV ESTPIASRFT GVTPMAVNYR NPASLNFDSL NSFGAYRSPS SFYPLRRPLE LSSLRRNRSS FFNTHRFDLG SNYTSFTPRY RSPLRGGLSQ RFPLRSSWSK EF // ID HPRR_MYCPN Reviewed; 141 AA. AC P75170; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Hydroperoxide reductase; DE EC=1.11.1.-; GN OrderedLocusNames=MPN_625; ORFNames=C12_orf141, MP217; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT. RX PubMed=12943365; DOI=10.1023/A:1024625122089; RA Choi I.G., Shin D.H., Brandsen J., Jancarik J., Busso D., Yokota H., RA Kim R., Kim S.H.; RT "Crystal structure of a stress inducible protein from Mycoplasma RT pneumoniae at 2.85 A resolution."; RL J. Struct. Funct. Genomics 4:31-34(2003). CC -!- FUNCTION: Reduces organic and inorganic peroxide substrates. CC Protects the cell against oxidative stress (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12943365}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the OsmC/Ohr 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; U00089; AAB95865.1; -; Genomic_DNA. DR PIR; S73543; S73543. DR RefSeq; NP_110314.1; NC_000912.1. DR RefSeq; WP_010874982.1; NC_000912.1. DR PDB; 1LQL; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=1-141. DR PDBsum; 1LQL; -. DR ProteinModelPortal; P75170; -. DR SMR; P75170; 1-141. DR EnsemblBacteria; AAB95865; AAB95865; MPN_625. DR GeneID; 877343; -. DR KEGG; mpn:MPN625; -. DR PATRIC; 20022733; VBIMycPne110_0689. DR OMA; ELSVISY; -. DR OrthoDB; EOG6Z9B4B; -. DR BioCyc; MPNE272634:GJ6Z-671-MONOMER; -. DR EvolutionaryTrace; P75170; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Oxidoreductase; KW Peroxidase; Reference proteome. FT CHAIN 1 141 Hydroperoxide reductase. FT /FTId=PRO_0000210607. FT STRAND 3 11 {ECO:0000244|PDB:1LQL}. FT HELIX 13 15 {ECO:0000244|PDB:1LQL}. FT STRAND 17 21 {ECO:0000244|PDB:1LQL}. FT STRAND 24 28 {ECO:0000244|PDB:1LQL}. FT TURN 33 35 {ECO:0000244|PDB:1LQL}. FT HELIX 41 64 {ECO:0000244|PDB:1LQL}. FT STRAND 69 79 {ECO:0000244|PDB:1LQL}. FT STRAND 84 86 {ECO:0000244|PDB:1LQL}. FT STRAND 89 100 {ECO:0000244|PDB:1LQL}. FT HELIX 105 118 {ECO:0000244|PDB:1LQL}. FT HELIX 120 126 {ECO:0000244|PDB:1LQL}. FT STRAND 132 140 {ECO:0000244|PDB:1LQL}. SQ SEQUENCE 141 AA; 15469 MW; 07958C371E69A0A4 CRC64; MDKKYDITAV LNEDSSMTAI SDQFQITLDA RPKHTAKGFG PLAALLSGLA ACELATANLM APAKMITINK LLMNVTGSRS TNPTDGYFGL REINLHWEIH SPNSETEIKE FIDFVSKRCP AHNTLQGVSQ LKINVNVTLV H // ID HRCA_MYCPN Reviewed; 351 AA. AC P75351; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Heat-inducible transcription repressor HrcA {ECO:0000255|HAMAP-Rule:MF_00081}; GN Name=hrcA {ECO:0000255|HAMAP-Rule:MF_00081}; GN OrderedLocusNames=MPN_124; ORFNames=MP030; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Negative regulator of class I heat shock genes (grpE- CC dnaK-dnaJ and groELS operons). Prevents heat-shock induction of CC these operons. {ECO:0000255|HAMAP-Rule:MF_00081}. CC -!- INTERACTION: CC P75344:dnaK; NbExp=1; IntAct=EBI-2259440, EBI-2258839; CC -!- SIMILARITY: Belongs to the HrcA family. {ECO:0000255|HAMAP- CC Rule:MF_00081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95678.1; -; Genomic_DNA. DR PIR; S73356; S73356. DR RefSeq; NP_109812.1; NC_000912.1. DR RefSeq; WP_010874481.1; NC_000912.1. DR ProteinModelPortal; P75351; -. DR IntAct; P75351; 1. DR EnsemblBacteria; AAB95678; AAB95678; MPN_124. DR GeneID; 877265; -. DR KEGG; mpn:MPN124; -. DR PATRIC; 20021549; VBIMycPne110_0131. DR KO; K03705; -. DR OMA; IENESIW; -. DR OrthoDB; EOG632D4G; -. DR BioCyc; MPNE272634:GJ6Z-131-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.450.40; -; 1. DR HAMAP; MF_00081; HrcA; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR002571; HrcA. DR InterPro; IPR021153; HrcA_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01628; HrcA; 1. DR PIRSF; PIRSF005485; HrcA; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR TIGRFAMs; TIGR00331; hrcA; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Repressor; Stress response; KW Transcription; Transcription regulation. FT CHAIN 1 351 Heat-inducible transcription repressor FT HrcA. FT /FTId=PRO_0000182510. SQ SEQUENCE 351 AA; 40462 MW; 96E27CA5924E76E7 CRC64; MKNLTTRQAQ ILKAIINEYI AYPVPVGSKL LTKKYFKNLS GGTLRNEMAV LEKEGYLKKN HISSGRIPSQ LGYQYYVKLL TKNDDKSNLK TRLRAIILQK HKTIDEIIEL GVKFINEMVN LPVVLTHFSS DEVLKKIDLI MLDQSCALLL LVSASGNVFK KTISYANQRQ FEDIMVCVRI FNDRIIDTRF CDIAQHLDVL KEIIRSKVHE YQYVIDEILF KLFNFEEFQQ ARKQVYGIHY LAQQPEFANQ ERLTRILNLL EDTSVWQQMA FMNQNNQTTN ITFGDKLGLE GEEVSVASTL INTTNESKHQ LAIVGPTRMD YQKVKALLLT LKEEIEEYDK QLHGGKTTSS T // ID HPRK_MYCPN Reviewed; 312 AA. AC P75548; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 111. DE RecName: Full=HPr kinase/phosphorylase; DE Short=HPrK/P; DE EC=2.7.11.-; DE EC=2.7.4.-; DE AltName: Full=HPr kinase/phosphatase; DE AltName: Full=HPr(Ser) kinase/phosphorylase; GN Name=hprK; Synonyms=ptsK; OrderedLocusNames=MPN_223; ORFNames=MP608; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP CHARACTERIZATION, AND MUTAGENESIS OF RESIDUES IN THE WALKER MOTIF A RP AND IN THE HPRK/P SIGNATURE SEQUENCE. RX PubMed=12368461; RA Steinhauer K., Jepp T., Hillen W., Stuelke J.; RT "A novel mode of control of Mycoplasma pneumoniae HPr RT kinase/phosphatase activity reflects its parasitic lifestyle."; RL Microbiology 148:3277-3284(2002). RN [3] RP CHARACTERIZATION, AND MUTAGENESIS OF GLY-154; GLY-159; LYS-160; RP SER-161; ARG-204 AND GLY-207. RX PubMed=14717704; DOI=10.1046/j.1432-1033.2003.03935.x; RA Merzbacher M., Detsch C., Hillen W., Stuelke J.; RT "Mycoplasma pneumoniae HPr kinase/phosphorylase."; RL Eur. J. Biochem. 271:367-374(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=12589763; DOI=10.1016/S0022-2836(02)01378-5; RA Allen G.S., Steinhauer K., Hillen W., Stuelke J., Brennan R.G.; RT "Crystal structure of HPr kinase/phosphatase from Mycoplasma RT pneumoniae."; RL J. Mol. Biol. 326:1203-1217(2003). CC -!- FUNCTION: Is a metabolite-sensitive enzyme that catalyzes the ATP- CC as well as probably the pyrophosphate-dependent phosphorylation of CC Ser-47 in HPr, a phosphocarrier protein of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (PTS). HprK/P also catalyzes the pyrophosphate-producing, CC inorganic phosphate-dependent dephosphorylation (phosphorolysis) CC of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of CC HPrK/P in the physiology of M.pneumoniae is not known yet. CC -!- CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr. CC -!- CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Contrary to HPrK/P of B.subtilis and other CC bacteria, that of M.pneumoniae is active as a kinase at very low CC ATP concentrations in the absence of fructose 1,6-bisphosphate CC (FBP). Kinase activity is slightly activated by FBP, and inhibited CC by inorganic phosphate (Pi), but FBP prevents kinase inhibition by CC Pi. Dephosphorylation of P-Ser-HPr by M.pneumoniae HPrK/P is CC strictly dependent on the presence of Pi, and is inhibited by FBP. CC This unique mode of control of HPrK/P activity is proposed to CC reflect the parasitic lifestyle of M.pneumoniae, that is strictly CC adapted to its ecological niche on nutrient-rich human mucous CC membranes. CC -!- SUBUNIT: Homohexamer, arranged as bilayered trimers. CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi. CC -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried CC out by the same active site and suggest a common mechanism for CC both reactions. CC -!- MISCELLANEOUS: Contrary to HPrK/P of other bacteria, that of CC M.pneumoniae has a very high affinity for ATP (Kd=5.3 microM), CC explaining kinase activity even at low ATP concentrations. CC -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000305}. CC -!- CAUTION: Was originally (PubMed:12368461 and PubMed:12589763) CC called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was CC shown in several bacteria to follow a quite unique mechanism, in CC which Pi instead of H(2)O is used for the nucleophilic attack on CC the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not CC a phosphohydrolysis but a phosphophosphorolysis reaction, and the CC bifunctional enzyme was dubbed HPr kinase/phosphorylase. 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; U00089; AAB96256.1; -; Genomic_DNA. DR PIR; S73934; S73934. DR RefSeq; NP_109911.1; NC_000912.1. DR RefSeq; WP_010874580.1; NC_000912.1. DR PDB; 1KNX; X-ray; 2.50 A; A/B/C/D/E/F=1-312. DR PDBsum; 1KNX; -. DR ProteinModelPortal; P75548; -. DR SMR; P75548; 1-311. DR IntAct; P75548; 4. DR EnsemblBacteria; AAB96256; AAB96256; MPN_223. DR GeneID; 877117; -. DR KEGG; mpn:MPN223; -. DR PATRIC; 20021771; VBIMycPne110_0242. DR KO; K06023; -. DR OMA; AVRRKMR; -. DR OrthoDB; EOG6F55HT; -. DR BioCyc; MPNE272634:GJ6Z-230-MONOMER; -. DR EvolutionaryTrace; P75548; -. DR Proteomes; UP000000808; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Carbohydrate metabolism; Complete proteome; KW Kinase; Magnesium; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 312 HPr kinase/phosphorylase. FT /FTId=PRO_0000058973. FT NP_BIND 154 161 ATP. {ECO:0000305}. FT REGION 201 210 Important for the catalytic mechanism of FT both phosphorylation and FT dephosphorylation. FT REGION 266 271 Important for the catalytic mechanism of FT dephosphorylation. {ECO:0000250}. FT ACT_SITE 139 139 {ECO:0000250}. FT ACT_SITE 160 160 {ECO:0000250}. FT ACT_SITE 178 178 Proton acceptor; for phosphorylation FT activity. Proton donor; for FT dephosphorylation activity. FT {ECO:0000250}. FT ACT_SITE 245 245 {ECO:0000250}. FT METAL 161 161 Magnesium. {ECO:0000305}. FT METAL 202 202 Magnesium. {ECO:0000255}. FT MUTAGEN 140 140 G->A: Kinase activity not affected and 6- FT fold increase in phosphorylase activity. FT {ECO:0000269|PubMed:12368461}. FT MUTAGEN 154 154 G->A: 4-fold reduction in kinase activity FT and loss of phosphorylase activity; 8- FT fold reduction in ATP affinity. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 156 156 S->A: Kinase activity not affected and 4- FT fold increase in phosphorylase activity. FT {ECO:0000269|PubMed:12368461}. FT MUTAGEN 156 156 S->T: 4-fold reduction in kinase activity FT and loss of phosphorylase activity. FT {ECO:0000269|PubMed:12368461}. FT MUTAGEN 157 157 G->A: 4-fold reduction in kinase activity FT and strongly reduced phosphorylase FT activity. {ECO:0000269|PubMed:12368461}. FT MUTAGEN 159 159 G->A: Loss of both kinase and FT phosphorylase activities; no ATP binding. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 160 160 K->A: Loss of both kinase and FT phosphorylase activities; no ATP binding. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 160 160 K->R: Loss of both kinase and FT phosphorylase activities. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 161 161 S->A: 10-fold reduction in kinase FT activity and loss of phosphorylase FT activity; affinity for ATP is only FT slightly affected. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 161 161 S->T: 2-fold reduction in kinase activity FT and strongly reduced phosphorylase FT activity; binds ATP with high affinity. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 162 162 E->D: Kinase activity not affected and FT loss of phosphorylase activity. FT {ECO:0000269|PubMed:12368461}. FT MUTAGEN 204 204 R->K: Kinase activity not affected and FT strongly reduced phosphorylase activity; FT ATP binding not affected. FT {ECO:0000269|PubMed:14717704}. FT MUTAGEN 207 207 G->A: Loss of both kinase and FT phosphorylase activities; ATP binding not FT affected. {ECO:0000269|PubMed:14717704}. FT HELIX 6 10 {ECO:0000244|PDB:1KNX}. FT TURN 14 16 {ECO:0000244|PDB:1KNX}. FT HELIX 39 42 {ECO:0000244|PDB:1KNX}. FT STRAND 54 56 {ECO:0000244|PDB:1KNX}. FT HELIX 58 64 {ECO:0000244|PDB:1KNX}. FT HELIX 69 72 {ECO:0000244|PDB:1KNX}. FT TURN 73 75 {ECO:0000244|PDB:1KNX}. FT HELIX 76 80 {ECO:0000244|PDB:1KNX}. FT STRAND 87 90 {ECO:0000244|PDB:1KNX}. FT TURN 91 93 {ECO:0000244|PDB:1KNX}. FT HELIX 97 102 {ECO:0000244|PDB:1KNX}. FT HELIX 103 105 {ECO:0000244|PDB:1KNX}. FT STRAND 110 115 {ECO:0000244|PDB:1KNX}. FT HELIX 117 120 {ECO:0000244|PDB:1KNX}. FT TURN 121 123 {ECO:0000244|PDB:1KNX}. FT HELIX 124 131 {ECO:0000244|PDB:1KNX}. FT STRAND 136 145 {ECO:0000244|PDB:1KNX}. FT STRAND 148 159 {ECO:0000244|PDB:1KNX}. FT HELIX 160 168 {ECO:0000244|PDB:1KNX}. FT TURN 169 171 {ECO:0000244|PDB:1KNX}. FT STRAND 173 185 {ECO:0000244|PDB:1KNX}. FT STRAND 188 193 {ECO:0000244|PDB:1KNX}. FT TURN 195 199 {ECO:0000244|PDB:1KNX}. FT STRAND 200 203 {ECO:0000244|PDB:1KNX}. FT TURN 204 206 {ECO:0000244|PDB:1KNX}. FT STRAND 207 210 {ECO:0000244|PDB:1KNX}. FT HELIX 211 215 {ECO:0000244|PDB:1KNX}. FT HELIX 217 219 {ECO:0000244|PDB:1KNX}. FT STRAND 224 233 {ECO:0000244|PDB:1KNX}. FT STRAND 252 255 {ECO:0000244|PDB:1KNX}. FT STRAND 258 266 {ECO:0000244|PDB:1KNX}. FT HELIX 273 288 {ECO:0000244|PDB:1KNX}. FT HELIX 293 304 {ECO:0000244|PDB:1KNX}. FT HELIX 305 308 {ECO:0000244|PDB:1KNX}. SQ SEQUENCE 312 AA; 35234 MW; 475F6B73587517C1 CRC64; MKKLLVKELI EQFQDCVNLI DGHTNTSNVI RVPGLKRVVF EMLGLFSSQI GSVAILGKRE FGFLSQKTLV EQQQILHNLL KLNPPAIILT KSFTDPTVLL QVNQTYQVPI LKTDFFSTEL SFTVETYINE QFATVAQIHG VLLEVFGVGV LLTGRSGIGK SECALDLINK NHLFVGDDAI EIYRLGNRLF GRAQEVAKKF MEIRGLGIIN VERFYGLQIT KQRTEIQLMV NLLSLEKQTT VTFERLGTEL KKQRLLGVDL SFYEIPISPG RKTSEIIESA VIDFKLKHSG YNSALDFIEN QKAILKRKKD ES // ID HPRT_MYCPN Reviewed; 175 AA. AC P75119; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE EC=2.4.2.8; GN Name=hpt; OrderedLocusNames=MPN_672; ORFNames=MP170; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho- CC alpha-D-ribose 1-diphosphate. CC -!- CATALYTIC ACTIVITY: GMP + diphosphate = guanine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. The magnesium ions are CC essentially bound to the substrate and have few direct CC interactions with the protein. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; CC IMP from hypoxanthine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase 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; U00089; AAB95818.1; -; Genomic_DNA. DR PIR; S73496; S73496. DR RefSeq; NP_110361.1; NC_000912.1. DR RefSeq; WP_010875029.1; NC_000912.1. DR ProteinModelPortal; P75119; -. DR EnsemblBacteria; AAB95818; AAB95818; MPN_672. DR GeneID; 877019; -. DR KEGG; mpn:MPN672; -. DR PATRIC; 20022833; VBIMycPne110_0739. DR KO; K00760; -. DR OMA; NEHFAGK; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; MPNE272634:GJ6Z-718-MONOMER; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR005904; Hxn_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01203; HGPRTase; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 175 Hypoxanthine-guanine FT phosphoribosyltransferase. FT /FTId=PRO_0000139606. FT NP_BIND 96 105 IMP. {ECO:0000250}. FT NP_BIND 155 156 IMP. {ECO:0000250}. FT ACT_SITE 100 100 Proton acceptor. {ECO:0000250}. FT METAL 156 156 Magnesium. {ECO:0000250}. FT BINDING 128 128 IMP. {ECO:0000250}. SQ SEQUENCE 175 AA; 19620 MW; 1E5A9FAA01D69854 CRC64; MGIKSIIIDQ KQVEAGCNAA LKWCNEHFAG KQVIVLGILK GCIPFLGKLI SQFTFDLQLD FVAVASYHGG SRQQEAPKIV LDMSHDPKGK DILLIEDIVD SGRSIKLVLD LLHTRKAKSV ILVSFIEKLK PREADIKVDY SCFKNQDEFL VGFGLDYQGF YRNLPYVGVF DPEDN // ID IF1_MYCPN Reviewed; 78 AA. AC Q50298; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 97. 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=MPN_187; ORFNames=MP644; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the CC 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently CC binds. Helps modulate mRNA selection, yielding the 30S pre- CC initiation complex (PIC). Upon addition of the 50S ribosomal CC subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S CC translation initation complex. {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation CC complex which assembles on the 30S ribosome in the order IF-2 and CC IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can CC occur at any time during PIC assembly. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SIMILARITY: Contains 1 S1-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43694.1; -; Genomic_DNA. DR EMBL; U00089; AAB96292.1; -; Genomic_DNA. DR PIR; S62821; S62821. DR RefSeq; NP_109875.1; NC_000912.1. DR RefSeq; WP_010874544.1; NC_000912.1. DR ProteinModelPortal; Q50298; -. DR IntAct; Q50298; 7. DR EnsemblBacteria; AAB96292; AAB96292; MPN_187. DR GeneID; 877185; -. DR KEGG; mpn:MPN187; -. DR PATRIC; 20021697; VBIMycPne110_0205. DR KO; K02518; -. DR OMA; DERAPHT; -. DR OrthoDB; EOG6384SC; -. DR BioCyc; MPNE272634:GJ6Z-194-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1 78 Translation initiation factor IF-1. FT /FTId=PRO_0000095825. FT DOMAIN 4 78 S1-like. {ECO:0000255|HAMAP- FT Rule:MF_00075}. SQ SEQUENCE 78 AA; 9025 MW; CA9908B1B6FEDACF CRC64; MQPKFNNQAK QDKLVLTGKI LEIIHGDKFR VLLENNVEVD AHLAGKMRMR RLRILPGDLV EVEFSPYDLK LGRIIGRK // ID IF2_MYCPN Reviewed; 617 AA. AC P75590; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Translation initiation factor IF-2; GN Name=infB; OrderedLocusNames=MPN_155; ORFNames=MP676; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 CC subfamily. {ECO:0000305}. 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; U00089; AAB96324.1; -; Genomic_DNA. DR PIR; S74002; S74002. DR RefSeq; NP_109843.1; NC_000912.1. DR RefSeq; WP_010874512.1; NC_000912.1. DR ProteinModelPortal; P75590; -. DR IntAct; P75590; 8. DR EnsemblBacteria; AAB96324; AAB96324; MPN_155. DR GeneID; 877346; -. DR KEGG; mpn:MPN155; -. DR PATRIC; 20021633; VBIMycPne110_0173. DR KO; K02519; -. DR OMA; LWYHSKV; -. DR OrthoDB; EOG67HJSV; -. DR BioCyc; MPNE272634:GJ6Z-162-MONOMER; -. DR Proteomes; UP000000808; 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; 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 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 1 617 Translation initiation factor IF-2. FT /FTId=PRO_0000137222. FT DOMAIN 119 288 tr-type G. FT NP_BIND 128 135 GTP. {ECO:0000250}. FT NP_BIND 175 179 GTP. {ECO:0000250}. FT NP_BIND 229 232 GTP. {ECO:0000250}. FT REGION 128 135 G1. {ECO:0000250}. FT REGION 153 157 G2. {ECO:0000250}. FT REGION 175 178 G3. {ECO:0000250}. FT REGION 229 232 G4. {ECO:0000250}. FT REGION 265 267 G5. {ECO:0000250}. SQ SEQUENCE 617 AA; 67897 MW; B658142123D70133 CRC64; MSKHKPRHFQ KNKFDNRAKT SAKQQFRQVK TGVKDGVFVY KGPLTVSEFC LKTNIPTANI IKHFFLNGVP LTLNSVLSTE QLADACVNFG FDFKVETEIT HDNIISNIKF DDDPTQLSPR PPIVTIMGHV DHGKTSLLDA IRQTNTAAKE FGGITQKIGA YQVKNQEGKT ITFIDTPGHE AFTGMRARGA QVTDIVVLVV AGDDGLKQQT EEAISHAKSA KTPIIVFINK MDKPTANPDM VIQQLNKFDL VPEEWGGDTI FVKGSALTKE GIQELLDSIL LVAEVEDYKA NFNAHSSGYA IEVQTTKGLG PTATIIVKRG TLKIGDIVVL GPAWGKVRTM QDENGVHLQE AMPSKPVQIS GFDIVPVAGE KFIVFDDEKD AKLIANKFRE QQKQKLNTTQ INEELKQKIK SKEIKVLNLI FKVDSDGSLA AIKQAMQSID VPGMSVNIIH SGVGLISEND IMLAKASGAL LFSLNLGLSQ VVKNIASLQG VKVDVHYHIP KLAEEIENIL KGQLEPVYED VELGRAEVLQ LWYHSKVGHI AGTLVKTGKV KRGALCKLLR RNETIYEGRV DSLKSEKNPV NQMEAGKNCG IVINGCEDIQ VCDIILVYEK QEVKSKS // ID IF3_MYCPN Reviewed; 201 AA. AC P78024; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. 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=MPN_115; ORFNames=MP039; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAG34732.1; -; Genomic_DNA. DR PIR; S73365; S73365. DR RefSeq; NP_109803.1; NC_000912.1. DR RefSeq; WP_010874472.1; NC_000912.1. DR ProteinModelPortal; P78024; -. DR IntAct; P78024; 3. DR EnsemblBacteria; AAG34732; AAG34732; MPN_115. DR GeneID; 877368; -. DR KEGG; mpn:MPN115; -. DR PATRIC; 20021529; VBIMycPne110_0122. DR KO; K02520; -. DR OMA; EFILIDE; -. DR OrthoDB; EOG63JRGJ; -. DR BioCyc; MPNE272634:GJ6Z-121-MONOMER; -. DR Proteomes; UP000000808; 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 1 201 Translation initiation factor IF-3. FT /FTId=PRO_0000177543. SQ SEQUENCE 201 AA; 23145 MW; 3E14B9FA797C80C8 CRC64; MPLILDQGCF VSESRFHRLA QNIKQGSRRE REQKPLINDK IGFNEFILID ENGSNLGTVR RTDALKMAEE KQLDLVLIGS NPAKPIVKLL DFGRYTYDLK RKKRQSKKNQ TIIQIKEVVV KPTIAKHDLE FKAKQTTGWA EKGYHVKFVV RAFGRVSTRI ELIEKVFNDF YLLVEPAVEV QKPLTASSKT MYSALLVPRK K // ID IPYR_MYCPN Reviewed; 184 AA. AC P75250; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Inorganic pyrophosphatase; DE EC=3.6.1.1; DE AltName: Full=Pyrophosphate phospho-hydrolase; DE Short=PPase; GN Name=ppa; OrderedLocusNames=MPN_528; ORFNames=MP314; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; 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:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PPase 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; U00089; AAB95962.1; -; Genomic_DNA. DR PIR; S73640; S73640. DR RefSeq; NP_110216.1; NC_000912.1. DR RefSeq; WP_010874884.1; NC_000912.1. DR ProteinModelPortal; P75250; -. DR EnsemblBacteria; AAB95962; AAB95962; MPN_528. DR GeneID; 876725; -. DR KEGG; mpn:MPN528; -. DR PATRIC; 20022526; VBIMycPne110_0587. DR KO; K01507; -. DR OMA; PVALMKM; -. DR OrthoDB; EOG6NKR4X; -. DR BioCyc; MetaCyc:MONOMER-644; -. DR BioCyc; MPNE272634:GJ6Z-572-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.90.80.10; -; 1. DR HAMAP; MF_00209; Inorganic_PPase; 1. DR InterPro; IPR008162; Pyrophosphatase. DR PANTHER; PTHR10286; PTHR10286; 1. DR Pfam; PF00719; Pyrophosphatase; 1. DR SUPFAM; SSF50324; SSF50324; 1. DR PROSITE; PS00387; PPASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 184 Inorganic pyrophosphatase. FT /FTId=PRO_0000137509. FT METAL 55 55 Magnesium 1. {ECO:0000250}. FT METAL 60 60 Magnesium 1. {ECO:0000250}. FT METAL 60 60 Magnesium 2. {ECO:0000250}. FT METAL 92 92 Magnesium 1. {ECO:0000250}. SQ SEQUENCE 184 AA; 21369 MW; 804E3952966DF0C6 CRC64; MDKFLIDVTV EIPKSSKIKY EYDRKTSQIR VDRILFGSES YPQNYGFIAN TLDWDGDELD CFIFADQAFL PGVVVPTRIV GALEMVDDGE LDTKLLGVID CDPRYKEINS VNDLPKHRVD EIIGFLKTYK LLQKKEVIIK GVQSLEWAKK EYQVCVDLMK QYGKLPKDEF IAKMQKLHPE HYQK // ID KCY_MYCPN Reviewed; 217 AA. AC P75308; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. 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=MPN_476; GN ORFNames=MP365; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- INTERACTION: CC P75322:MPN_461; NbExp=1; IntAct=EBI-2260403, EBI-2260400; 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; U00089; AAB96013.1; -; Genomic_DNA. DR PIR; S73691; S73691. DR RefSeq; NP_110164.1; NC_000912.1. DR RefSeq; WP_010874832.1; NC_000912.1. DR ProteinModelPortal; P75308; -. DR IntAct; P75308; 1. DR EnsemblBacteria; AAB96013; AAB96013; MPN_476. DR GeneID; 877402; -. DR KEGG; mpn:MPN476; -. DR PATRIC; 20022376; VBIMycPne110_0515. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; MetaCyc:MONOMER-573; -. DR BioCyc; MPNE272634:GJ6Z-517-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 217 Cytidylate kinase. FT /FTId=PRO_0000131941. FT NP_BIND 9 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 217 AA; 24567 MW; 5FCA216DC77FDAB2 CRC64; MYFQIAIDGP SSSGKSSVAK TVARQLGFEY FSTGKMYRAF AYVMQVNRLD VNLLLKVINQ INWRFEHEKV FYNNADISEV ILNQEIAQLA SNLATNPEVR KMAVLRQQAL AKNTNIVMDG RDIGTVVLKD AQLKYFLDAK PEIRAQRRAQ DLGIAYDSDK AFQELVAEIK HRDAVDTSRT ADPLVQAPDA IYIDSSNLTF QQVVELMVQQ ARTVFKL // ID KGUA_MYCPN Reviewed; 239 AA. AC P75526; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=MPN_246; ORFNames=MP586; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96234.1; -; Genomic_DNA. DR PIR; S73912; S73912. DR RefSeq; NP_109934.1; NC_000912.1. DR RefSeq; WP_010874603.1; NC_000912.1. DR ProteinModelPortal; P75526; -. DR IntAct; P75526; 2. DR EnsemblBacteria; AAB96234; AAB96234; MPN_246. DR GeneID; 876860; -. DR KEGG; mpn:MPN246; -. DR PATRIC; 20021817; VBIMycPne110_0265. DR KO; K00942; -. DR OMA; MELQSIV; -. DR OrthoDB; EOG6CP410; -. DR BioCyc; MPNE272634:GJ6Z-253-MONOMER; -. DR Proteomes; UP000000808; 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 1 239 Guanylate kinase. FT /FTId=PRO_0000170568. FT DOMAIN 55 235 Guanylate kinase-like. FT NP_BIND 62 69 ATP. {ECO:0000250}. SQ SEQUENCE 239 AA; 27002 MW; 59247177879BE2F6 CRC64; MQSRLAWSKG NWTGLVGSLI SLTSSSTSHA LVGNNSILIC GKIKIILNIE MVDTGRIFVI TGPSGVGKSS LVRCLIDHFK DKLRYSISAT TRKMRNSETE GVDYFFKDKA EFEKLIAADA FVEWAMYNDN YYGTLKSQAE QIIHNGGNLV LEIEYQGALQ VKQKYPNDVV LIFIKPPSME ELLVRLKKRN DEDAITIQNR LKQAEKECQQ IGHFKYVVTN NEFDKTLAEL QAILLAEFN // ID KAD_MYCPN Reviewed; 215 AA. AC Q50299; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 104. 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=MPN_185; GN ORFNames=MP646; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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. 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. Some bacteria have CC evolved a zinc-coordinating structure that stabilizes the LID CC domain. {ECO:0000255|HAMAP-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; U34795; AAC43696.1; -; Genomic_DNA. DR EMBL; U00089; AAB96294.1; -; Genomic_DNA. DR PIR; S62823; S62823. DR RefSeq; NP_109873.1; NC_000912.1. DR RefSeq; WP_010874542.1; NC_000912.1. DR ProteinModelPortal; Q50299; -. DR IntAct; Q50299; 1. DR EnsemblBacteria; AAB96294; AAB96294; MPN_185. DR GeneID; 876756; -. DR KEGG; mpn:MPN185; -. DR PATRIC; 20021693; VBIMycPne110_0203. DR KO; K00939; -. DR OMA; NCESKLI; -. DR OrthoDB; EOG679TH4; -. DR BioCyc; MPNE272634:GJ6Z-192-MONOMER; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000808; 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:0046872; F:metal ion 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; 2. DR SUPFAM; SSF57774; SSF57774; 1. DR TIGRFAMs; TIGR01351; adk; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Metal-binding; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase; Zinc. FT CHAIN 1 215 Adenylate kinase. FT /FTId=PRO_0000158804. FT NP_BIND 14 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 61 63 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 91 94 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 138 139 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT REGION 34 63 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT REGION 128 165 LID. {ECO:0000255|HAMAP-Rule:MF_00235}. FT METAL 132 132 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 135 135 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 152 152 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 155 155 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT BINDING 35 35 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 40 40 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 98 98 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 129 129 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 162 162 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 173 173 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 211 211 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00235}. SQ SEQUENCE 215 AA; 24255 MW; 3F4258BEFA24E8E8 CRC64; MVMENKFLFL GAPGVGKGTL AKQVANTTGL FHLSTGDIFR SVMQEQGALS QTLAHYMNQG LYVPDELTNQ TFWHFVTTHQ NELHKGFILD GYPRTLNQLE FLQSKLQLDQ VFHLKLSDPQ VLVARILNRL VCPSCGSVYN KQSKPPLKAN QCDRCHATLQ ARNDDTEAVI LKRLTLYEDT VKPLIEAFTK QGILTVIEAQ LPLEQQVNLV QQLVH // ID KITH_MYCPN Reviewed; 191 AA. AC P75070; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; OrderedLocusNames=MPN_044; GN ORFNames=MP110; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00124}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95758.1; -; Genomic_DNA. DR PIR; S73436; S73436. DR RefSeq; NP_109732.1; NC_000912.1. DR RefSeq; WP_010874401.1; NC_000912.1. DR ProteinModelPortal; P75070; -. DR IntAct; P75070; 1. DR EnsemblBacteria; AAB95758; AAB95758; MPN_044. DR GeneID; 877408; -. DR KEGG; mpn:MPN044; -. DR PATRIC; 20021365; VBIMycPne110_0044. DR KO; K00857; -. DR OMA; KEQFGWI; -. DR OrthoDB; EOG69D3J2; -. DR BioCyc; MPNE272634:GJ6Z-46-MONOMER; -. DR BRENDA; 2.7.1.21; 3534. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 191 Thymidine kinase. FT /FTId=PRO_0000174999. FT NP_BIND 20 27 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT NP_BIND 93 96 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00124}. FT METAL 150 150 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 153 153 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 183 183 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 186 186 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. SQ SEQUENCE 191 AA; 21500 MW; C333AF82EFC21F15 CRC64; MSFSQVFHQS PRGWIEVICG PMFSGKTEEL LRKIKRWKLA KIPVIIFKPK IDTRQQHLVK SRNGHSDEAI EINSPLEIYD YLTKDRFDVV AIDEAQFFSS EIVEVVKSLN DLGINVIVSG LDTDFRAEPF GSIPQLLAIA DKICKLDAVC NVCGQLAQRT QRIVSKSNET VLIGDIEAYE PRCKLHQPSA G // ID KPYK_MYCPN Reviewed; 508 AA. AC P78031; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=MPN_303; ORFNames=MP533; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC -!- ENZYME REGULATION: Regulated by phosphoenolpyruvate substrate and CC is allosterically activated by ribose-5-phosphate, AMP and other CC nucleoside monophosphates but not by fructose-1,6-bisphosphate. CC {ECO:0000250}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96181.1; -; Genomic_DNA. DR PIR; S73859; S73859. DR RefSeq; NP_109991.1; NC_000912.1. DR RefSeq; WP_010874660.1; NC_000912.1. DR ProteinModelPortal; P78031; -. DR IntAct; P78031; 2. DR EnsemblBacteria; AAB96181; AAB96181; MPN_303. DR GeneID; 877217; -. DR KEGG; mpn:MPN303; -. DR PATRIC; 20021941; VBIMycPne110_0327. DR KO; K00873; -. DR OMA; NSIDMIA; -. DR OrthoDB; EOG6GBMB0; -. DR BioCyc; MPNE272634:GJ6Z-310-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000808; Chromosome. 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: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; IPR018209; Pyrv_Knase_AS. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR015806; Pyrv_Knase_insert_dom. DR PANTHER; PTHR11817; PTHR11817; 2. DR Pfam; PF00224; PK; 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. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1 508 Pyruvate kinase. FT /FTId=PRO_0000112081. FT METAL 58 58 Potassium. {ECO:0000250}. FT METAL 60 60 Potassium. {ECO:0000250}. FT METAL 90 90 Potassium. {ECO:0000250}. FT METAL 91 91 Potassium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 251 251 Magnesium. {ECO:0000250}. FT METAL 275 275 Magnesium. {ECO:0000250}. FT BINDING 56 56 Substrate. {ECO:0000250}. FT BINDING 274 274 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 275 275 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 307 307 Substrate. {ECO:0000250}. FT SITE 249 249 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 508 AA; 57268 MW; 011D97377F8BB527 CRC64; MIHHLKRTKI IATCGPALTK KLWTLAMLDD PAYAAMKAEA YANIENIIKN GVTVIRLNFS HGNHEEQAVR IKIVRDVAKK LNLPVSIMLD TNGPEIRVFE TAPEGLKILK DSEVVINTTT KEVAKNNQFS VSDASGTYNM VNDVKVGQKI LVDDGKLSLV VKRIDTKNNQ VICVAQNDHT IFTKKRLNLP NADYSIPFLS AKDLRDIDFG LTHQIDYIAA SFVNTTENIK QLRDYLASKN AKHVKLIAKI ESNHALNNID GIIKASDGIM VARGDLGLEI PYYKVPYWQR YMIKACRFFN KRVITATQML DSLEKNIQPT RAEVTDVYFA VDRGNDATML SGETANGAFP LNAVYVMKMI DKQSETFFDY QYNLNYYMAN SKARHSEFWK QVVLPLAQKT APKRKLINSD FKYDFVVHAT NNLNEIYALS NARLAAAVII LTNDPQVYTG HGVDYGIFPY LIDQKPQSLS KAEFKSLANV AIKHYQQHGE ISQLKQCLGV FHNKIISL // ID LEPA_MYCPN Reviewed; 598 AA. AC P75498; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 2. DT 11-MAY-2016, entry version 103. 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=MPN_279; ORFNames=MP556; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION OF PROBABLE FRAMESHIFT. RA Sinan C.; RL Unpublished observations (FEB-2002). 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 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 -!- SEQUENCE CAUTION: CC Sequence=AAB96204.1; Type=Frameshift; Positions=540; 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; U00089; AAB96204.1; ALT_FRAME; Genomic_DNA. DR PIR; S73882; S73882. DR RefSeq; NP_109967.1; NC_000912.1. DR ProteinModelPortal; P75498; -. DR EnsemblBacteria; AAB96204; AAB96204; MPN_279. DR GeneID; 876840; -. DR KEGG; mpn:MPN279; -. DR PATRIC; 20021885; VBIMycPne110_0299. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR BioCyc; MPNE272634:GJ6Z-286-MONOMER; -. DR Proteomes; UP000000808; 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 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 membrane; Complete proteome; GTP-binding; Hydrolase; Membrane; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 598 Elongation factor 4. FT /FTId=PRO_0000176305. FT DOMAIN 4 185 tr-type G. FT NP_BIND 16 21 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT NP_BIND 132 135 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. SQ SEQUENCE 598 AA; 68025 MW; 4E5A1A230763B57C CRC64; MEQQKIRNFS IIAHIDHGKS TLSDRLIERS IGFEKRLLQA QMLDTMAIER ERGITIKLNA VQLKMAQGNQ QYLFHLVDTP GHVDFTYEVS RSLAACEGVL LLVDATQGIQ AQTISNTYLA LENNLEIIPV INKVDMESAD VEKTKQAFHQ LLGVDPNTIP LVSAKTGLGI DQLITTIIEK VPPPKGDESK PLKALLFDSY YDPYKGVVCF IRIFEGSLKL NDKIRFARSN SVYQIVELGI KNPFFEKQDV LKAGEIGWFS AGIKKLRDVT VGDTIVHAED TTTPPLPGYK KVLPMIYCGL YPIDNNDYQN LKMAMEKIIL SDVALEYEYE TSQALGFGVR CGFLGLLHMD VIKERLEREY NLKLISAPPS VRYKVLLTNG EELELDNPSL LPERSRIKSI SEPFVRVYID LPDHYLGTVI DLCQNFRGQY EKLEEIDIDR KRLVYLMPLG EIIYSFFDKL KSITKGYASL NYEFDQYQVS QLAKVEIMLN KQKVDALSFI AHHDFAFQRA KKFCVKLKEL IPKHLFEIPI QATIGSKVIA RETIKAVRKD VTAKLYGGDV TRKKKLLEKQ KEGKKRLKAI GSVELPQELF SHLLKDED // ID KPRS_MYCPN Reviewed; 328 AA. AC P75044; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 3. DT 11-MAY-2016, entry version 102. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; Synonyms=prsA; GN OrderedLocusNames=MPN_073; ORFNames=MP082; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00583}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route I): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95730.1; 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; U00089; AAB95730.1; ALT_INIT; Genomic_DNA. DR PIR; S73408; S73408. DR RefSeq; NP_109761.1; NC_000912.1. DR RefSeq; WP_010874430.1; NC_000912.1. DR ProteinModelPortal; P75044; -. DR IntAct; P75044; 2. DR EnsemblBacteria; AAB95730; AAB95730; MPN_073. DR GeneID; 877326; -. DR KEGG; mpn:MPN073; -. DR PATRIC; 20021425; VBIMycPne110_0074. DR KO; K00948; -. DR OMA; HENVRGQ; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; MetaCyc:MONOMER-576; -. DR BioCyc; MPNE272634:GJ6Z-75-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000808; 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:0009116; P:nucleoside metabolic process; IEA:InterPro. 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; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF00156; Pribosyltran; 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; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 328 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141162. FT NP_BIND 39 41 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 98 101 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 195 197 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 222 229 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 312 314 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 130 130 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 132 132 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 141 141 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 145 145 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 106 106 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 132 132 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 137 137 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 172 172 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 328 AA; 36742 MW; 200FA5FB9648701D CRC64; MDRHNHVVFS LSKTHDLVSR ICQKLKMPMG LITHNEFADG ETYIRFEESV RNKDVFIFQS TCAPVNDSLM ELLIAIDALK RGSAKSITAI LPYYGYARQD RKTMGREPIT SKLVADLLTT AGVSRVALTD IHSDQTQGFF NIPVDTLRTY HVFLTRTVEL LGKKDLVVVS PDYGGVKRAR LIATSLELPL AIIDKRRPAH NVAESINVLG EVANKNCLIV DDMIDTGGTV IAAAKLLREH HAKKVCVMAT HGLFNGEAPQ RFQKAFNEGL VDYLFVSNSI PQTKFDQCPQ FQVIDLAPLF EEVLLCYANN SSISAIYTRH IEWIKKHV // ID KTHY_MYCPN Reviewed; 210 AA. AC P75106; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=MPN_006; ORFNames=MP148; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95796.1; -; Genomic_DNA. DR PIR; S73474; S73474. DR RefSeq; NP_109694.1; NC_000912.1. DR RefSeq; WP_010874363.1; NC_000912.1. DR ProteinModelPortal; P75106; -. DR IntAct; P75106; 4. DR EnsemblBacteria; AAB95796; AAB95796; MPN_006. DR GeneID; 877298; -. DR KEGG; mpn:MPN006; -. DR PATRIC; 20021285; VBIMycPne110_0006. DR KO; K00943; -. DR OMA; QGASLPM; -. DR OrthoDB; EOG64JFSH; -. DR BioCyc; MPNE272634:GJ6Z-6-MONOMER; -. DR Proteomes; UP000000808; 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; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 210 Thymidylate kinase. FT /FTId=PRO_0000155307. FT NP_BIND 11 18 ATP. {ECO:0000255}. SQ SEQUENCE 210 AA; 23711 MW; 911F50922BA06FB0 CRC64; MKQGVFVAIE GVDGAGKTVL LEAFKQRFPQ SFLGFKTLFS REPGGTPLAE KIRALLLHEA MEPLTEAYLF AASRTEHVRQ LIQPALQQKQ LVIVDRFVWS SYAYQGLIKK VGLDVVKKLN ADAVGDSMPD FTFIVDCDFE TALNRMAKRG QDNLLDNTVK KQADFNTMRQ YYHSLVDNKR VFLLDGQNQT GCLEQFIEQL SQCLTQPTLS // ID LDH_MYCPN Reviewed; 312 AA. AC P78007; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 112. DE RecName: Full=L-lactate dehydrogenase; DE Short=L-LDH; DE EC=1.1.1.27; GN Name=ldh; OrderedLocusNames=MPN_674; ORFNames=MP168; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH 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; U00089; AAB95816.1; -; Genomic_DNA. DR PIR; S73494; S73494. DR RefSeq; NP_110363.1; NC_000912.1. DR RefSeq; WP_010875031.1; NC_000912.1. DR ProteinModelPortal; P78007; -. DR IntAct; P78007; 6. DR PRIDE; P78007; -. DR EnsemblBacteria; AAB95816; AAB95816; MPN_674. DR GeneID; 877032; -. DR KEGG; mpn:MPN674; -. DR PATRIC; 20022837; VBIMycPne110_0741. DR KO; K00016; -. DR OMA; AGDYEDC; -. DR OrthoDB; EOG6091FG; -. DR BioCyc; MetaCyc:MONOMER-601; -. DR BioCyc; MPNE272634:GJ6Z-720-MONOMER; -. DR UniPathway; UPA00554; UER00611. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT CHAIN 1 312 L-lactate dehydrogenase. FT /FTId=PRO_0000168374. FT NP_BIND 12 40 NAD. {ECO:0000250}. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT BINDING 122 122 NAD or substrate. {ECO:0000250}. FT BINDING 153 153 Substrate. {ECO:0000250}. FT BINDING 229 229 Substrate. {ECO:0000250}. FT MOD_RES 220 220 Phosphotyrosine. {ECO:0000250}. SQ SEQUENCE 312 AA; 33888 MW; 604F58CD3B6C273A CRC64; MKSLKVALIG SGAVGTSFLY AAMSRGLASE YMVIDINEKS QVGNVFDLQD AVPSSPQYSK VIAGDYKQLK DYDFIFIGAG RPQKQGGETR LQLLEGNVEI MKNIAKAVKE SGFKGITLIA SNPVDIMAYT YLKVTGFEPN KVIGSGTLLD SARLKFAIAE KYGMSSRDVQ AYVLGEHGDS SVSIISSAKI AGLPLKHFSK ASDIEKEFAE IDHFIRRRAY EIIERKGATF YGIGEATAEV AELILRDTKE VRVVASLING QYGAKDVMFG TPCVLGRNGV EKILEIELSA TEKAGLDKSI QVLKDNIKLA KL // ID LGT_MYCPN Reviewed; 389 AA. AC P75547; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Prolipoprotein diacylglyceryl transferase; DE EC=2.4.99.-; GN Name=lgt; OrderedLocusNames=MPN_224; ORFNames=MP607; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Transfers the N-acyl diglyceride group on what will CC become the N-terminal cysteine of membrane lipoproteins. CC {ECO:0000250}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis CC (diacylglyceryl transfer). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Lgt 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; U00089; AAB96255.1; -; Genomic_DNA. DR PIR; S73933; S73933. DR RefSeq; NP_109912.1; NC_000912.1. DR RefSeq; WP_010874581.1; NC_000912.1. DR EnsemblBacteria; AAB96255; AAB96255; MPN_224. DR GeneID; 877116; -. DR KEGG; mpn:MPN224; -. DR PATRIC; 20021773; VBIMycPne110_0243. DR KO; K13292; -. DR OMA; FEYFHPT; -. DR OrthoDB; EOG690MBD; -. DR BioCyc; MPNE272634:GJ6Z-231-MONOMER; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000000808; 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; 2. DR TIGRFAMs; TIGR00544; lgt; 1. DR PROSITE; PS01311; LGT; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 389 Prolipoprotein diacylglyceryl FT transferase. FT /FTId=PRO_0000172637. FT TRANSMEM 26 48 Helical. {ECO:0000255}. FT TRANSMEM 55 77 Helical. {ECO:0000255}. FT TRANSMEM 97 119 Helical. {ECO:0000255}. FT TRANSMEM 148 170 Helical. {ECO:0000255}. FT TRANSMEM 218 240 Helical. {ECO:0000255}. FT TRANSMEM 281 303 Helical. {ECO:0000255}. FT TRANSMEM 308 330 Helical. {ECO:0000255}. SQ SEQUENCE 389 AA; 44596 MW; FBFFB4AFF674FBBD CRC64; MNPSVSSRPP WSTAFYLGPG FPIQWYGIIV AIGIAFGILM FVLKLIYFYK IQDNSFYFFI FIAVLTMVLG ARAWYFLIEA VDGRSSGSNF FDFRNGGLAI QGGVLLTTLA GIIYFNVFLN MKTTKTKTTA KLLNNKNQIK TVYVERNISV FVMLDLIAPC VLIGQAIGRW GNFFNAEVYG AALVGSKNDT LSAANTTWGF LRILMPKVWD GMFINGSFRI PLFLIESFFN TIFFVFIYFV MDHIKGIRSG TIGFSYFLAT GIVRLILETQ RDEAFKYNTS IVFSALLILV GIVGIIYCQT LAIKLRGYFW TYFFLYGWYK VAAFFTTLFM KDRTQACSSK FAFYEKSLPE KERSFFQLKY YNDVLPPKIY RLYDHEMLMF DKLEAVPEA // ID LPLA_MYCPN Reviewed; 339 AA. AC P75394; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Probable lipoate-protein ligase A; DE Short=Lipoate--protein ligase; DE EC=6.3.1.20; GN Name=lplA; OrderedLocusNames=MPN_389; ORFNames=MP449; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of CC exogenously supplied lipoate to lipoyl-AMP and the transfer of the CC activated lipoyl onto the lipoyl domains of lipoate-dependent CC enzymes. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier CC protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine CC + AMP + diphosphate. CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260143, EBI-2260143; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group CC of lipoic 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:0000250}. CC -!- SIMILARITY: Belongs to the LplA 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; U00089; AAB96097.1; -; Genomic_DNA. DR PIR; S73775; S73775. DR RefSeq; NP_110077.1; NC_000912.1. DR RefSeq; WP_010874745.1; NC_000912.1. DR ProteinModelPortal; P75394; -. DR EnsemblBacteria; AAB96097; AAB96097; MPN_389. DR GeneID; 877079; -. DR KEGG; mpn:MPN389; -. DR PATRIC; 20022154; VBIMycPne110_0420. DR KO; K03800; -. DR OMA; WRNAETV; -. DR OrthoDB; EOG6038ZS; -. DR BioCyc; MPNE272634:GJ6Z-411-MONOMER; -. DR UniPathway; UPA00537; UER00594. DR UniPathway; UPA00537; UER00595. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR019491; Lipoate_protein_ligase_C. DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR Pfam; PF10437; Lip_prot_lig_C; 1. DR TIGRFAMs; TIGR00545; lipoyltrans; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 339 Probable lipoate-protein ligase A. FT /FTId=PRO_0000209568. FT DOMAIN 30 217 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT NP_BIND 77 80 ATP. {ECO:0000250}. FT BINDING 72 72 ATP. {ECO:0000250}. FT BINDING 135 135 ATP. {ECO:0000250}. FT BINDING 135 135 Lipoate. {ECO:0000250}. SQ SEQUENCE 339 AA; 39194 MW; DE2C78A4924E4FEA CRC64; MKTYILTSPK NIPYFNAALE EWLLTEFKKG EEIKVIYFWQ NANTIVVGRN QNTYAEVNLS EVEKDKVNLF RRFSGGGAVF HDMGNICFSI ILPKAKKEME NAYEETTRNV VKFLNSVGVP AQFHGRNDLE IEGKKFSGLA EYLSKDRVLV HGTLLFDTDF TKLAKYLNVD KTKMVSKGIE SVQKRVVNVK EYLPNLSTPT FLEKMVQFFT ETEHAETIHL DESSIKMVEK RAQEHFQSWD WNFGKTADYN FKNKKRFEGA GIFECNVQVD QGKVVDIKFY GDFLSVIDIT PVTQQLVGQK YDYQTFAKIL GNIDNFKEYF GTLTPQQMLE VIFDNKKDE // ID LON_MYCPN Reviewed; 795 AA. AC P78025; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973}; DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973}; DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=MPN_332; GN ORFNames=MP504; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_01973}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Contains 1 Lon N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU01123}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96152.1; -; Genomic_DNA. DR PIR; S73830; S73830. DR RefSeq; NP_110020.1; NC_000912.1. DR RefSeq; WP_010874688.1; NC_000912.1. DR ProteinModelPortal; P78025; -. DR MEROPS; S16.004; -. DR EnsemblBacteria; AAB96152; AAB96152; MPN_332. DR GeneID; 877195; -. DR KEGG; mpn:MPN332; -. DR PATRIC; 20022018; VBIMycPne110_0356. DR OMA; EGTFMPG; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; MPNE272634:GJ6Z-349-MONOMER; -. DR Proteomes; UP000000808; 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; PS51787; LON_N; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. DR PROSITE; PS01046; LON_SER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Reference proteome; Serine protease; KW Stress response. FT CHAIN 1 795 Lon protease. FT /FTId=PRO_0000076140. FT DOMAIN 7 211 Lon N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU01123}. FT DOMAIN 615 795 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT NP_BIND 379 386 ATP. {ECO:0000255|HAMAP-Rule:MF_01973}. FT COMPBIAS 304 308 Poly-Ser. FT ACT_SITE 702 702 {ECO:0000255|HAMAP-Rule:MF_01973}. FT ACT_SITE 745 745 {ECO:0000255|HAMAP-Rule:MF_01973}. SQ SEQUENCE 795 AA; 90204 MW; 7E7855082060C891 CRC64; MPAVKKPQIL VVRNQVIFPY NGFELDVGRE RSKKLIKALK NLKTKRLVLV TQKNSDQLNP EFDDIYHCGT LCDIDEIIEV PSEDGKTADY KIKGKGLQRV AITSFSDADL TKYDHHFLNS TLTENKALDK LLERIFPDKE DFAEILDSLN SFLELQELKK LSKVPKDIKR YDIITFKLAS LIFKDITLQQ AILEENDIEK RLQKIIGSGI EDLGHISEEA RAKQRESEFD KIDNRITRKV NEQLSRQQRD FYLREKLRVI REEIGMTSKK EDEVSNIRKK LEENPYPEHI KKRILSELDH FENSSSSSQE STLTKTYIDT LMNLPWWQES KDNADVKNLI KILNKNHSGL DKVKERVVEY LAVQLRTKKL KGPIMCLVGP PGVGKSSLAK SIAEALNKCF VKVSLGGVHD ESEIRGHRKT YLGSMPGRIL KGMVRAKVIN PLFLLDEIDK MTSSNQGYPS GALLEVLDPE LNNKFSDNYV EEDYDLSKVM FVATANYIED IPEALLDRME VIELTSYTEQ EKLQITKSHL VKRCLDDAEI KTDDLKFTDE GISYIIKFYT REAGVRQLER LIQQIVRKYI VNLQKTGEQQ VVVDVDLVKK YLKKEIFDYT VRDEDALPGI VNGMAYTPTG GDLLPIEVTH VAGKGDLILT GNLKQTMRES ASVALGYVKA NAQSFNINPN LFKKVDINIH VPGGGIPKDG PSAGAALVTA IISSLTGKKV DPKIAMTGEI TLRGKVMTIG GVKEKTISAY RGGVRTIFMP EKNERYLDEV PKDIVKDLEI ILVKEYKDIY NKIFN // ID LSPA_MYCPN Reviewed; 184 AA. AC P75484; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Lipoprotein signal peptidase; DE EC=3.4.23.36; DE AltName: Full=Prolipoprotein signal peptidase; DE AltName: Full=Signal peptidase II; DE Short=SPase II; GN Name=lspA; Synonyms=lsp; OrderedLocusNames=MPN_293; ORFNames=MP542; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000250}. 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. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). CC -!- INTERACTION: CC P75395:MPN_387; NbExp=1; IntAct=EBI-2258812, EBI-2258802; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase A8 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; U00089; AAB96190.1; -; Genomic_DNA. DR PIR; S73868; S73868. DR RefSeq; NP_109981.1; NC_000912.1. DR RefSeq; WP_010874650.1; NC_000912.1. DR IntAct; P75484; 1. DR EnsemblBacteria; AAB96190; AAB96190; MPN_293. DR GeneID; 877085; -. DR KEGG; mpn:MPN293; -. DR PATRIC; 20021921; VBIMycPne110_0317. DR KO; K03101; -. DR OMA; FINIYVI; -. DR OrthoDB; EOG647V1T; -. DR BioCyc; MPNE272634:GJ6Z-300-MONOMER; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000000808; 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 Pfam; PF01252; Peptidase_A8; 1. DR PRINTS; PR00781; LIPOSIGPTASE. DR TIGRFAMs; TIGR00077; lspA; 1. DR PROSITE; PS00855; SPASE_II; 1. PE 1: Evidence at protein level; KW Aspartyl protease; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 184 Lipoprotein signal peptidase. FT /FTId=PRO_0000178795. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT ACT_SITE 131 131 {ECO:0000250}. FT ACT_SITE 157 157 {ECO:0000250}. SQ SEQUENCE 184 AA; 20586 MW; C29480B17C7B98A3 CRC64; MAKAPTFFSK LLKQILFANR KPFLYYKLAL ILFVGFVILF QVFMLRAALN GEKGINGANG TDVARSSFIS IYVIGNKGVG FSLLADQPGL VYFLQGFLSF IALFFLVFST SYNYIFWITT LAFGSLGNFF DRLTSGSGEV LDYFVFSGGN SVFNLADCCI TFSFIGLFLS FLIQFFKEMK QTKS // ID MANB_MYCPN Reviewed; 554 AA. AC P75050; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; GN Name=manB; Synonyms=cpsG; OrderedLocusNames=MPN_066; ORFNames=MP088; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Alpha-D-mannose 1-phosphate = D-mannose 6- CC phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95736.1; -; Genomic_DNA. DR PIR; S73414; S73414. DR RefSeq; NP_109754.1; NC_000912.1. DR RefSeq; WP_010874423.1; NC_000912.1. DR ProteinModelPortal; P75050; -. DR IntAct; P75050; 3. DR EnsemblBacteria; AAB95736; AAB95736; MPN_066. DR GeneID; 876721; -. DR KEGG; mpn:MPN066; -. DR PATRIC; 20021411; VBIMycPne110_0067. DR KO; K01840; -. DR OMA; QAGSMGM; -. DR OrthoDB; EOG6103ZG; -. DR BioCyc; MetaCyc:MONOMER-621; -. DR BioCyc; MPNE272634:GJ6Z-68-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC. 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 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 SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 554 Phosphomannomutase. FT /FTId=PRO_0000147830. FT ACT_SITE 149 149 Phosphoserine intermediate. FT {ECO:0000250}. FT METAL 149 149 Magnesium; via phosphate group. FT {ECO:0000250}. FT METAL 301 301 Magnesium. {ECO:0000250}. FT METAL 303 303 Magnesium. {ECO:0000250}. FT METAL 305 305 Magnesium. {ECO:0000250}. SQ SEQUENCE 554 AA; 63215 MW; 9993A52B3D5E6C0B CRC64; MNSNAYLEAQ RWLSHPRVKP NLKEVITAMS AEEIEHFFSL KKPSFGTAGV RGKMAPGYHG MNVFSYAYLT QGYVNYIQSL NPTKKPLRFL VARDTRKHGA LFNGIVCDVI TSMGHVVYMF DNNEPTPTPL VSYVIKKYHF DGGVNVTASH NPKTDNGFKI YDGHGAQLLD FQTDQLIAML PPVVTMLDFE PRGNNELLHF LDNEVVYKNY FDDLKESLVV DNDSFKNLPV VFTGLHGTSV KLLPRFLTYL GYSNIISVQP QNVFDANFAN ADHLNPESKD TWELARQYAS NTKAKLMMAI DPDADRFAIA EWNPQTQDWH YFSGNESGVM VAYYKLKHKQ FKRQPYIVTT VVSTDLVDKI AKKYGAFVKR TNVGFKFIGQ AVNHFSKDNE LVVAFEEAIG MMASDGLNRE KDSFQAAAIM LEIARYCHNK GISLLEFYRG EIFGEFGDYY NWTVPHTIHG VNWKEKMEQV LHQLTTATIK EVVGHKITKI KNYVDINLVE YVLENGNWIK FRISGTEPKL KLYFNLSNGY LAALKHEAKK MHEFLVRLLN LDKA // ID MAP1_MYCPN Reviewed; 248 AA. AC Q11132; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974}; DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=MPN_186; GN ORFNames=MP645; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01974}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000255|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; U34795; AAC43695.1; -; Genomic_DNA. DR EMBL; U00089; AAB96293.1; -; Genomic_DNA. DR PIR; S62822; S62822. DR RefSeq; NP_109874.1; NC_000912.1. DR RefSeq; WP_010874543.1; NC_000912.1. DR ProteinModelPortal; Q11132; -. DR EnsemblBacteria; AAB96293; AAB96293; MPN_186. DR GeneID; 876883; -. DR KEGG; mpn:MPN186; -. DR PATRIC; 20021695; VBIMycPne110_0204. DR OMA; PNSGPKI; -. DR OrthoDB; EOG6MWNDS; -. DR BioCyc; MPNE272634:GJ6Z-193-MONOMER; -. DR Proteomes; UP000000808; 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; Complete proteome; Hydrolase; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1 248 Methionine aminopeptidase. FT /FTId=PRO_0000148947. FT METAL 94 94 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 105 105 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 105 105 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 169 169 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT METAL 202 202 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT BINDING 176 176 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. SQ SEQUENCE 248 AA; 27657 MW; D3F4B5F3F6048BF5 CRC64; MVYLKSAREV EQIRQACKIF QEAKAYFTIE RLLGKSLTAI DQALKQFIES KGATCAFHKY QNFPGFNCLS LNETVIHGIA DNRVFGVKDK LTLDIGINLN GYICDAAFTV LGPKAPEPMQ TLLEVTEACF TAVVEPQLRP NNPTGNVSHA IQTYFESKGY YLLKQFGGHG CGIKVHEEPL ILNYGKPDTG TKLEPGMVLC IEPMVMTDSD AMVMHNNSWN VLTPKSRYNC HVEQMYVITT SGFECLTN // ID METK_MYCPN Reviewed; 383 AA. AC P78003; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=S-adenosylmethionine synthase; DE Short=AdoMet synthase; DE EC=2.5.1.6; DE AltName: Full=MAT; DE AltName: Full=Methionine adenosyltransferase; GN Name=metK; Synonyms=metX; OrderedLocusNames=MPN_060; ORFNames=MP094; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 2 divalent ions per subunit. Magnesium or cobalt. CC {ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95742.1; -; Genomic_DNA. DR PIR; S73420; S73420. DR RefSeq; NP_109748.1; NC_000912.1. DR RefSeq; WP_010874417.1; NC_000912.1. DR ProteinModelPortal; P78003; -. DR IntAct; P78003; 2. DR EnsemblBacteria; AAB95742; AAB95742; MPN_060. DR GeneID; 876974; -. DR KEGG; mpn:MPN060; -. DR PATRIC; 20021397; VBIMycPne110_0060. DR KO; K00789; -. DR OMA; QDGFHWE; -. DR OrthoDB; EOG68WR6M; -. DR BioCyc; MPNE272634:GJ6Z-62-MONOMER; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000808; 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 1 383 S-adenosylmethionine synthase. FT /FTId=PRO_0000174553. FT NP_BIND 256 263 ATP. {ECO:0000255}. FT METAL 24 24 Magnesium. {ECO:0000250}. FT METAL 50 50 Potassium. {ECO:0000250}. FT METAL 260 260 Potassium. {ECO:0000250}. FT METAL 268 268 Magnesium. {ECO:0000250}. SQ SEQUENCE 383 AA; 42560 MW; 6E5817BAF4E65051 CRC64; MAKTIKHPRW GRYVAEAVGR GHPDKICDQI ADSILDECIK QSPTSHVACE VFASKNLIMV GGEILTTGYV DVVQTGWKVL NRLGYTENDF SFLSCINSQS SEINQAVQSN DEIGAGDQGI TVGYACSETE QLMPLGSIVA QALVQRAARI IDQYPFIKHD MKSQVVLNYT GNKVQCESVL MSVQHTQDVS LDQLRQTIIN QVILPVLTEY GLNDPKIKHL VNPGGSFVVG GPMADTGLTG RKIIVDTYGP YANHGGGSFS GKDPTKVDRT GAYFARFIAK HIVSLGWAEE CEVSISWVFS QPLPQSIQVK CFNINKEFSE QLINQVISQY FNWSVAKIIA KLKLLDQVEY FRYAVYGHFG HQTAPWEQLS ERDSLQCLIK NFQ // ID MGP3_MYCPN Reviewed; 1218 AA. AC Q50341; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Mgp-operon protein 3; DE Short=Mgp3; DE AltName: Full=ORF-3 protein; DE Flags: Precursor; GN OrderedLocusNames=MPN_142; ORFNames=MP012; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=2468577; DOI=10.1016/0378-1119(88)90323-X; RA Inamine J.M., Loechel S., Hu P.C.; RT "Analysis of the nucleotide sequence of the P1 operon of Mycoplasma RT pneumoniae."; RL Gene 73:175-183(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M21519; AAA88326.1; -; Genomic_DNA. DR EMBL; U00089; AAB95660.1; -; Genomic_DNA. DR PIR; JS0069; JS0069. DR RefSeq; NP_109830.1; NC_000912.1. DR RefSeq; WP_010874499.1; NC_000912.1. DR IntAct; Q50341; 2. DR EnsemblBacteria; AAB95660; AAB95660; MPN_142. DR GeneID; 877207; -. DR KEGG; mpn:MPN142; -. DR PATRIC; 20021599; VBIMycPne110_0156. DR OMA; GVVRLNF; -. DR OrthoDB; EOG6H7FQG; -. DR BioCyc; MPNE272634:GJ6Z-149-MONOMER; -. DR Proteomes; UP000000808; 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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR InterPro; IPR009896; Cytadhesin_P30. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF07271; Cytadhesin_P30; 1. DR Pfam; PF05220; MgpC; 1. PE 1: Evidence at protein level; KW Cell adhesion; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1218 Mgp-operon protein 3. FT /FTId=PRO_0000021721. FT TRANSMEM 1121 1141 Helical. {ECO:0000255}. SQ SEQUENCE 1218 AA; 130457 MW; 4DA29BCE41538311 CRC64; MKSKLKLKRY LLFLPLLPLG TLSLANTYLL QDHNTLTPYT PFTTPLNGGL DVVRAAHLHP SYELVDWKRV GDTKLVALVR SALVRVKFQD TTSSDQSNTN QNALSFDTQE SQKALNGSQS GSSDTSGSNS QDFASYVLIF KAAPRATWVF ERKIKLALPY VKQESQGSGD QGSNGKGSLY KTLQDLLVEQ PVTPYTPNAG LARVNGVAQD TVHFGSGQES SWNSQRSQKG LKNNPGPKAV TGFKLDKGRA YRKLNESWPV YEPLDSTKEG KGKDESSWKN SEKTTAENDA PLVGMVGSGA AGSASSLQGN GSNSSGLKSL LRSAPVSVPP SSTSNQTLSL SNPAPVGPQA VVSQPAGGAT AAVSVNRTAS DTATFSKYLN TAQALHQMGV IVPGLEKWGG NNGTGVVASR QDATSTNLPH AAGASQTGLG TGSPREPALT ATSQRAVTVV AGPLRAGNSS ETDALPNVIT QLYHTSTAQL AYLNGQIVVM GSDRVPSLWY WVVGEDQESG KATWWAKTEL NWGTDKQKQF VENQLGFKDD SNSDSKNSNL KAQGLTQPAY LIAGLDVVAD HLVFAAFKAG AVGYDMTTDS SASTYNQALA WSTTAGLDSD GGYKALVENT AGLNGPINGL FTLLDTFAYV TPVSGMKGGS QNNEEVQTTY PVKSDQKATA KIASLINASP LNSYGDDGVT VFDALGLNFN FKLNEERLPS RTDQLLVYGI VNESELKSAR ENAQSTSDDN SNTKVKWTNT ASHYLPVPYY YSANFPEAGN RRRAEQRNGV KISTLESQAT DGFANSLLNF GTGLKAGVDP APVARGHKPN YSAVLLVRGG VVRLNFNPDT DKLLDSTDKN SEPISFSYTP FGSAESAVDL TTLKDVTYIA ESGLWFYTFD NGEKPTYDGK QQQVKNRKGY AVITVSRTGI EFNEDANTTT LSQAPAALAV QNGIASSQDD LTGILPLSDE FSAVITKDQT WTGKVDIYKN TNGLFEKDDQ LSENVKRRDN GLVPIYNEGI VDIWGRVDFA ANSVLQARNL TDKTVDEVIN NPDILQSFFK FTPAFDNQRA MLVGEKTSDT TLTVKPKIEY LDGNFYGEDS KIAGIPLNID FPSRIFAGFA ALPSWVIPVS VGSSVGILLI LLILGLGIGI PMYKVRKLQD SSFVDVFKKV DTLTTAVGSV YKKIITQTSV IKKAPSALKA ANNAAPKAPV KPAAPTAPRP PVQPPKKA // ID MNMG_MYCPN Reviewed; 612 AA. AC P75221; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 97. 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=MPN_557; ORFNames=MP285; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95933.1; -; Genomic_DNA. DR PIR; S73611; S73611. DR RefSeq; NP_110246.1; NC_000912.1. DR RefSeq; WP_010874914.1; NC_000912.1. DR ProteinModelPortal; P75221; -. DR IntAct; P75221; 1. DR EnsemblBacteria; AAB95933; AAB95933; MPN_557. DR GeneID; 877193; -. DR KEGG; mpn:MPN557; -. DR PATRIC; 20022591; VBIMycPne110_0619. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR BioCyc; MPNE272634:GJ6Z-602-MONOMER; -. DR Proteomes; UP000000808; 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; -; 4. 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 1 612 tRNA uridine 5-carboxymethylaminomethyl FT modification enzyme MnmG. FT /FTId=PRO_0000117137. FT NP_BIND 9 14 FAD. {ECO:0000255|HAMAP-Rule:MF_00129}. FT NP_BIND 270 284 NAD. {ECO:0000255|HAMAP-Rule:MF_00129}. SQ SEQUENCE 612 AA; 68053 MW; 35DFF3A14395BC2C CRC64; MSFTLTVIGG GHAGLEAAFI ASKLGLKVNL LVLDPNHVGS CPCNPAIGGP AKGIVTREID VLGGMQGKAA DATALQYKLL NSSKGPAVQA IRAQIDKIAY QKWFRQQIDQ TPNIELIAGE AVDILESNGK VKGVVLADGS ELASDAVIVT TGTYLKAKTY CGSLSKEEGP DRAKRSEYLS TNLIKRGFKT LRLKTGTPPR ILRESLDFSQ MAVEANTTPH LAFSFTTKNY LPLEQQVICH LIHTNPQIHQ LILANLKQSA VFNGSIKANG PLYCPSIEDK VFRFQDKERH QIFVEPESLS LETVYLAGFS TSFPPEVQEH IVRLLPGFKN ARFQKYGYAI EYDAFSSIQL KSTLETKLIQ NLYFAGQING TSGYEEAAGQ GLIAGINAAL KLQRKPEFVL QRNEAYLGVM INDLVTKEIS DPYRLLTSRA EHRLWLRNDN LQERLIEKSR ALGLVEADVY ANYLEQQQKK KQLIDYLQTT TVGQIAALKL NFKNTAQTLF DFTKRAEIKL VDLVQLLPKR FDLDVQSLNQ IDIDIKYAGY IKKSEKYFKS LNNLSSVKIP LKLNYHKVPN LASEAIVKLS KIRPTDLSVA SQVAGINFND ILAIKHFLDN HE // ID MNMA_MYCPN Reviewed; 370 AA. AC P75365; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 16-MAR-2016, entry version 91. 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=MPN_422; ORFNames=MP419; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble CC position (U34) of tRNA, leading to the formation of s(2)U34. CC {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- CATALYTIC ACTIVITY: A [protein]-S-sulfanyl-L-cysteine + CC uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L- CC cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + CC acceptor. {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP- CC Rule:MF_00144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96067.1; -; Genomic_DNA. DR PIR; S73745; S73745. DR RefSeq; NP_110110.1; NC_000912.1. DR RefSeq; WP_010874778.1; NC_000912.1. DR ProteinModelPortal; P75365; -. DR EnsemblBacteria; AAB96067; AAB96067; MPN_422. DR GeneID; 877362; -. DR KEGG; mpn:MPN422; -. DR PATRIC; 20022240; VBIMycPne110_0457. DR KO; K00566; -. DR OMA; CYYLKIW; -. DR OrthoDB; EOG6RZB5H; -. DR BioCyc; MPNE272634:GJ6Z-451-MONOMER; -. DR Proteomes; UP000000808; 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 1 370 tRNA-specific 2-thiouridylase MnmA. FT /FTId=PRO_0000121654. FT NP_BIND 9 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 107 109 Interaction with target base in tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 159 161 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT ACT_SITE 112 112 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT ACT_SITE 209 209 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT BINDING 35 35 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT BINDING 137 137 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 138 138 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 348 348 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT DISULFID 112 209 Alternate. {ECO:0000255|HAMAP- FT Rule:MF_00144}. SQ SEQUENCE 370 AA; 41773 MW; 3C7D154F2CDCDC22 CRC64; MQNKTVFVGI SGGVDSAVSA LLLKQQYREV IGIFMECWDN TLNNDQLGHR AFNEHKSGCS SKEDFREAQA IAQLLGIKLI KQNLVEPYWK QVFLPTIDAF KNGLTPNPDM LCNRLIKFGL MRDYCKQLDP NSDFATGHYA ALSWDNNQPL LAIPKDKHKD QTYFLAHVKP AQLQDVVFPL AHLLKTEVRQ IALAHHFSVA TKKDSTGICF IGERHFSDFL KNYLPVKPGV IYDWKTQRQL GSHEGVWFYT TGQRSGLNLG GQAARNFVVE KDLKTNTLYV SSDPEDLQRR GITLSHFNWL YQPNPLTQTV LVRIRHAQPL VQGHITVQPN NVVQVQLDQP IDRVTNGQYG VLYTQNGICL GSGIITASQI // ID MNME_MYCPN Reviewed; 442 AA. AC P75104; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379}; DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379}; GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN Synonyms=thdF {ECO:0000255|HAMAP-Rule:MF_00379}, GN trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=MPN_008; GN ORFNames=MP146; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 -!- INTERACTION: CC P78012:groL; NbExp=3; IntAct=EBI-2259625, EBI-2258565; 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; U00089; AAB95794.1; -; Genomic_DNA. DR PIR; S73472; S73472. DR RefSeq; NP_109696.1; NC_000912.1. DR RefSeq; WP_010874365.1; NC_000912.1. DR ProteinModelPortal; P75104; -. DR IntAct; P75104; 2. DR EnsemblBacteria; AAB95794; AAB95794; MPN_008. DR GeneID; 877349; -. DR KEGG; mpn:MPN008; -. DR PATRIC; 20021289; VBIMycPne110_0008. DR KO; K03650; -. DR OMA; LIEISCH; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; MPNE272634:GJ6Z-8-MONOMER; -. DR Proteomes; UP000000808; 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; 1. DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51709; G_TRME; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome; KW tRNA processing. FT CHAIN 1 442 tRNA modification GTPase MnmE. FT /FTId=PRO_0000188892. FT DOMAIN 217 363 TrmE-type G. FT NP_BIND 227 232 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 246 252 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 271 274 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 331 334 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 227 227 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 231 231 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 246 246 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 248 248 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 251 251 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 252 252 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT BINDING 23 23 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 82 82 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 121 121 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 442 442 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. SQ SEQUENCE 442 AA; 49780 MW; FA8849BADBCB9AD5 CRC64; MDTKQTMFAL ATAPFNSAIH IIRLSGPDVY RIINQITNKE VKPLGMRIQR VWLIDHNQKK VDDVLLFKFV APNSYTGEDL IEISCHGSMV IVNEIIGLLL KHGAVQAQPG EFTQRGYLNG KMSLNQAASV NNLVLSPNTT LKDVALNALA GQVDARLEPL VEKLGQLVMQ MEVNLDYPEY TDEQRELVTM NQAVVQITQI LNQIVVGQDQ LQRLKDPFKI AIIGNTNVGK SSLLNALLDQ DKAIVSAIKG STRDIVEGDF ALNGHFVKIL DTAGIRQHQS ALEKAGIQKT FGAIKTANLV IYLLDARQPE PDPKIIARLK KLKKDFFLVH NKADLVQQSF QVSISAKQKQ IQPLVDLLTQ YLHQFYSVEQ NQLYLISDWQ TILLQKAIAE LEHFLIKQQN CLFFDILVVH LRAAHEYILQ VLGKNTNYDL INEIFKHFCL GK // ID MSRA_MYCPN Reviewed; 157 AA. AC P75188; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; GN Name=msrA; Synonyms=pmsR; OrderedLocusNames=MPN_607; ORFNames=MP235; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase 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; U00089; AAB95883.1; -; Genomic_DNA. DR PIR; S73561; S73561. DR RefSeq; NP_110296.1; NC_000912.1. DR RefSeq; WP_010874964.1; NC_000912.1. DR ProteinModelPortal; P75188; -. DR EnsemblBacteria; AAB95883; AAB95883; MPN_607. DR GeneID; 876738; -. DR KEGG; mpn:MPN607; -. DR PATRIC; 20022695; VBIMycPne110_0670. DR KO; K07304; -. DR OMA; TYEDICT; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; MPNE272634:GJ6Z-653-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-HAMAP. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 157 Peptide methionine sulfoxide reductase FT MsrA. FT /FTId=PRO_0000138558. FT ACT_SITE 10 10 {ECO:0000250}. SQ SEQUENCE 157 AA; 18379 MW; 02DCE014D5BD3DCB CRC64; MKQIYFGGGC FWGTQKYFDL IKGVQKTSVG YLNSNMKNPT YEQVCSGQTN AVEAVFVEYD ENKVSLNELI DAFFKVIDPT IRNRQGNDIG TQYRTGVYWV DPQDEQLITQ KFRELQANYP KPIVTENRAM ENYFLAEEYH QDYLKKNPHG YCHIKFD // ID MSRB_MYCPN Reviewed; 151 AA. AC P75129; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400}; DE EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400}; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400}; GN Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; GN OrderedLocusNames=MPN_662; ORFNames=K05_orf151, MP180; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01400}. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC {ECO:0000255|HAMAP-Rule:MF_01400}. CC -!- SIMILARITY: Contains 1 MsrB (methionine-R-sulfoxide reductase) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01126}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95828.1; -; Genomic_DNA. DR PIR; S73506; S73506. DR RefSeq; NP_110351.1; NC_000912.1. DR RefSeq; WP_010875019.1; NC_000912.1. DR ProteinModelPortal; P75129; -. DR SMR; P75129; 4-145. DR IntAct; P75129; 3. DR EnsemblBacteria; AAB95828; AAB95828; MPN_662. DR GeneID; 877011; -. DR KEGG; mpn:MPN662; -. DR PATRIC; 20022809; VBIMycPne110_0727. DR KO; K07305; -. DR OMA; RMQYEVT; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; MPNE272634:GJ6Z-708-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-HAMAP. 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 HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 151 Peptide methionine sulfoxide reductase FT MsrB. FT /FTId=PRO_0000140284. FT DOMAIN 9 132 MsrB. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT ACT_SITE 121 121 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. SQ SEQUENCE 151 AA; 17279 MW; 3E6D23F0AC857744 CRC64; MSKYQKKSDG ELKRTLTKLQ YDVTQNAHTE PPYTNEYNRH YEKGIYVDIT SGEPLFISTD KFKSGCGWPA FTKPISQDLI ANYRDESHGM IRTEVRAKNS NSHLGHVFRD GPEEHGGLRY CINSAALKFI PFAEMESAGY GEYLKLFKES N // ID MRAZ_MYCPN Reviewed; 141 AA. AC P75467; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Transcriptional regulator MraZ; GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; GN OrderedLocusNames=MPN_314; ORFNames=MP522; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND SUBUNIT. RX PubMed=15146477; DOI=10.1002/prot.10593; RA Chen S., Jancrick J., Yokota H., Kim R., Kim S.-H.; RT "Crystal structure of a protein associated with cell division from RT Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved RT sequence motif."; RL Proteins 55:785-791(2004). CC -!- SUBUNIT: Homooctamer. Forms a ring. {ECO:0000269|PubMed:15146477}. 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; U00089; AAB96170.1; -; Genomic_DNA. DR PIR; S73848; S73848. DR RefSeq; NP_110002.1; NC_000912.1. DR RefSeq; WP_010874670.1; NC_000912.1. DR PDB; 1N0E; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-141. DR PDB; 1N0F; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-141. DR PDB; 1N0G; X-ray; 2.80 A; A/B=1-141. DR PDBsum; 1N0E; -. DR PDBsum; 1N0F; -. DR PDBsum; 1N0G; -. DR ProteinModelPortal; P75467; -. DR SMR; P75467; 1-137. DR IntAct; P75467; 2. DR EnsemblBacteria; AAB96170; AAB96170; MPN_314. DR GeneID; 877153; -. DR KEGG; mpn:MPN314; -. DR PATRIC; 20021980; VBIMycPne110_0337. DR KO; K03925; -. DR OMA; TYECKAD; -. DR OrthoDB; EOG6G4W1C; -. DR BioCyc; MPNE272634:GJ6Z-331-MONOMER; -. DR EvolutionaryTrace; P75467; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1 141 Transcriptional regulator MraZ. FT /FTId=PRO_0000108508. FT DOMAIN 5 47 SpoVT-AbrB 1. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT DOMAIN 76 119 SpoVT-AbrB 2. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT STRAND 4 8 {ECO:0000244|PDB:1N0E}. FT STRAND 14 17 {ECO:0000244|PDB:1N0E}. FT HELIX 21 25 {ECO:0000244|PDB:1N0E}. FT STRAND 28 31 {ECO:0000244|PDB:1N0E}. FT STRAND 41 43 {ECO:0000244|PDB:1N0E}. FT HELIX 45 55 {ECO:0000244|PDB:1N0E}. FT STRAND 60 62 {ECO:0000244|PDB:1N0E}. FT HELIX 63 73 {ECO:0000244|PDB:1N0E}. FT STRAND 78 80 {ECO:0000244|PDB:1N0E}. FT STRAND 85 88 {ECO:0000244|PDB:1N0E}. FT HELIX 91 96 {ECO:0000244|PDB:1N0E}. FT STRAND 103 107 {ECO:0000244|PDB:1N0E}. FT STRAND 112 116 {ECO:0000244|PDB:1N0E}. FT HELIX 117 125 {ECO:0000244|PDB:1N0E}. FT HELIX 130 135 {ECO:0000244|PDB:1N0E}. SQ SEQUENCE 141 AA; 16335 MW; 1A8705F5486CA6BC CRC64; MLLGTFNITL DAKNRISLPA KLRAFFEGSI VINRGFENCL EVRKPQDFQK YFEQFNSFPS TQKDTRTLKR LIFANANFVD VDTAGRVLIP NNLINDAKLD KEIVLIGQFD HLEIWDKKLY EDYLANSESL ETVAERMKDV K // ID MTHFS_MYCPN Reviewed; 164 AA. AC P75430; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase; DE EC=6.3.3.2; DE AltName: Full=5,10-methenyl-tetrahydrofolate synthetase; DE Short=MTHFS; DE Short=Methenyl-THF synthetase; GN OrderedLocusNames=MPN_348; ORFNames=H91_orf164, MP488; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. RX PubMed=15281135; DOI=10.1002/prot.20214; RA Chen S., Shin D.-H., Pufan R., Kim R., Kim S.H.; RT "Crystal structure of methenyltetrahydrofolate synthetase from RT Mycoplasma pneumoniae (GI: 13508087) at 2.2 A resolution."; RL Proteins 56:839-843(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ADP RP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, COFACTOR, AND SUBUNIT. RX PubMed=16104022; DOI=10.1002/prot.20591; RA Chen S., Yakunin A.F., Proudfoot M., Kim R., Kim S.H.; RT "Structural and functional characterization of a 5,10- RT methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: RT 13508087)."; RL Proteins 61:433-443(2005). CC -!- FUNCTION: Involved in folate metabolism. Catalyzes the CC irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to CC yield 5,10-methenyltetrahydrofolate. CC {ECO:0000269|PubMed:16104022}. CC -!- CATALYTIC ACTIVITY: ATP + 5-formyltetrahydrofolate = ADP + CC phosphate + 5,10-methenyltetrahydrofolate. CC {ECO:0000269|PubMed:16104022}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:16104022}; CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000269|PubMed:16104022}; CC Note=Magnesium. It can also use divalent cations such as CC manganese, calcium, zinc, iron, cobalt and copper. CC {ECO:0000269|PubMed:16104022}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=165 uM for 5-FTHF (at pH 6 and 37 degrees Celsius) CC {ECO:0000269|PubMed:16104022}; CC KM=166 uM for ATP (at pH 6 and 37 degrees Celsius) CC {ECO:0000269|PubMed:16104022}; CC Vmax=2.70 umol/min/mg enzyme toward 5-FTHF (at pH 6 and 37 CC degrees Celsius) {ECO:0000269|PubMed:16104022}; CC Vmax=2.84 umol/min/mg enzyme toward ATP (at pH 6 and 37 degrees CC Celsius) {ECO:0000269|PubMed:16104022}; CC Note=Kcat is 0.94 sec(-1) for cyclo-ligase activity with 5-FTHF CC (at pH 6 and 37 degrees Celsius). Kcat is 0.99 sec(-1) for CC cyclo-ligase activity with ATP (at pH 6 and 37 degrees CC Celsius).; CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:15281135, CC ECO:0000269|PubMed:16104022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase 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; U00089; AAB96136.1; -; Genomic_DNA. DR PIR; S73814; S73814. DR RefSeq; NP_110036.1; NC_000912.1. DR RefSeq; WP_010874704.1; NC_000912.1. DR PDB; 1SBQ; X-ray; 2.20 A; A/B=1-164. DR PDB; 1U3F; X-ray; 2.50 A; A/B=1-164. DR PDB; 1U3G; X-ray; 2.50 A; A=1-164. DR PDBsum; 1SBQ; -. DR PDBsum; 1U3F; -. DR PDBsum; 1U3G; -. DR ProteinModelPortal; P75430; -. DR SMR; P75430; 1-164. DR EnsemblBacteria; AAB96136; AAB96136; MPN_348. DR GeneID; 876747; -. DR KEGG; mpn:MPN348; -. DR PATRIC; 20022056; VBIMycPne110_0375. DR KO; K01934; -. DR OMA; CVFTPLV; -. DR OrthoDB; EOG6RVG1P; -. DR BioCyc; MPNE272634:GJ6Z-365-MONOMER; -. DR BRENDA; 6.3.3.2; 3534. DR EvolutionaryTrace; P75430; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 164 5-formyltetrahydrofolate cyclo-ligase. FT /FTId=PRO_0000200288. FT NP_BIND 3 7 ATP. FT NP_BIND 115 123 ATP. {ECO:0000305}. FT METAL 124 124 Magnesium. {ECO:0000269|PubMed:16104022}. FT METAL 154 154 Magnesium. {ECO:0000269|PubMed:16104022}. FT BINDING 50 50 Substrate. {ECO:0000269|PubMed:16104022}. FT BINDING 55 55 Substrate. {ECO:0000269|PubMed:16104022}. FT BINDING 125 125 ATP. FT BINDING 153 153 ATP. FT HELIX 3 16 {ECO:0000244|PDB:1SBQ}. FT HELIX 19 37 {ECO:0000244|PDB:1SBQ}. FT STRAND 45 47 {ECO:0000244|PDB:1SBQ}. FT HELIX 60 68 {ECO:0000244|PDB:1SBQ}. FT STRAND 72 78 {ECO:0000244|PDB:1SBQ}. FT STRAND 80 82 {ECO:0000244|PDB:1SBQ}. FT STRAND 84 87 {ECO:0000244|PDB:1SBQ}. FT HELIX 96 98 {ECO:0000244|PDB:1SBQ}. FT STRAND 101 105 {ECO:0000244|PDB:1SBQ}. FT STRAND 107 109 {ECO:0000244|PDB:1SBQ}. FT STRAND 114 116 {ECO:0000244|PDB:1U3G}. FT STRAND 118 120 {ECO:0000244|PDB:1U3F}. FT HELIX 122 126 {ECO:0000244|PDB:1SBQ}. FT HELIX 127 129 {ECO:0000244|PDB:1SBQ}. FT STRAND 136 140 {ECO:0000244|PDB:1SBQ}. FT HELIX 142 144 {ECO:0000244|PDB:1SBQ}. FT STRAND 158 162 {ECO:0000244|PDB:1SBQ}. SQ SEQUENCE 164 AA; 19265 MW; D44365FDE62A9DDF CRC64; MDKNALRKQI LQKRMALSTI EKSHLDQKIN QKLVAFLTPK PCIKTIALYE PIKNEVTFVD FFFEFLKINQ IRAVYPKVIS DTEIIFIDQE TNTFEPNQID CFLIPLVGFN KDNYRLGFGK GYYDRYLMQL TRQQPKIGIA YSFQKGDFLA DPWDVQLDLI INDE // ID MTLD_MYCPN Reviewed; 364 AA. AC P78008; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase; DE EC=1.1.1.17; GN Name=mtlD; OrderedLocusNames=MPN_652; ORFNames=MP190; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD(+) = D-fructose CC 6-phosphate + NADH. CC -!- INTERACTION: CC P75082:MPN_032; NbExp=1; IntAct=EBI-2262576, EBI-2261859; CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase 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; U00089; AAB95838.1; -; Genomic_DNA. DR PIR; S73516; S73516. DR RefSeq; NP_110341.1; NC_000912.1. DR RefSeq; WP_010875009.1; NC_000912.1. DR ProteinModelPortal; P78008; -. DR IntAct; P78008; 1. DR EnsemblBacteria; AAB95838; AAB95838; MPN_652. DR GeneID; 877028; -. DR KEGG; mpn:MPN652; -. DR PATRIC; 20022787; VBIMycPne110_0716. DR KO; K00009; -. DR OMA; IIELMER; -. DR OrthoDB; EOG67MF00; -. DR BioCyc; MetaCyc:MONOMER-622; -. DR BioCyc; MPNE272634:GJ6Z-698-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00196; Mannitol_dehydrog; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR023028; Mannitol_1_phos_5_DH. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 364 Mannitol-1-phosphate 5-dehydrogenase. FT /FTId=PRO_0000170712. FT NP_BIND 6 17 NAD. {ECO:0000250}. SQ SEQUENCE 364 AA; 42271 MW; 199394BBF11E31B6 CRC64; MKRINVLHFG AGNIGRGVIL PIYQQNDFSI DLVELNQNTV NELQKQKQYQ VHYLDCDQSQ LVNDFNTWNL KDEAKIIELM ERADVISTSI GAKNLASLKT LFDKAKFHKR AIVLCFENGF RISSNFKNIL QLNNTQVNFV DVVIDTIAPN FEKKANFLDI YCEKYSEIYA ETFPLEIKGV NQKNSLDRFI IKKLLLVNAL HSVIGLLGFQ QKLKYVHETL QVKSNLTFVE KLAQQIIDAL CAEYPEFNKN NLLSYGKNNL VRFANPKIQD LNTRLIREPL RKLNQNERFY AIYKLFKKNK IALNNILQVY LMVLKTNITD DTESQQIAKL INEKAWTELA KLSSLEESEW NLIKQELSRE ITKK // ID NAOX_MYCPN Reviewed; 479 AA. AC P75389; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Probable NADH oxidase; DE Short=NOXase; DE EC=1.6.99.3; GN Name=nox; OrderedLocusNames=MPN_394; ORFNames=MP444; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular CC oxygen to water. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide CC oxidoreductase 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; U00089; AAB96092.1; -; Genomic_DNA. DR PIR; S73770; S73770. DR RefSeq; NP_110082.1; NC_000912.1. DR RefSeq; WP_010874750.1; NC_000912.1. DR ProteinModelPortal; P75389; -. DR IntAct; P75389; 2. DR EnsemblBacteria; AAB96092; AAB96092; MPN_394. DR GeneID; 877135; -. DR KEGG; mpn:MPN394; -. DR PATRIC; 20022164; VBIMycPne110_0425. DR OMA; LMHYPPE; -. DR OrthoDB; EOG6QVRCJ; -. DR BioCyc; MPNE272634:GJ6Z-417-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC. 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; 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; 1. DR SUPFAM; SSF55424; SSF55424; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; KW Redox-active center; Reference proteome. FT CHAIN 1 479 Probable NADH oxidase. FT /FTId=PRO_0000184703. FT NP_BIND 8 12 FAD. {ECO:0000250}. FT NP_BIND 111 114 FAD. {ECO:0000250}. FT NP_BIND 170 185 NAD. {ECO:0000250}. FT NP_BIND 295 305 FAD. {ECO:0000250}. FT ACT_SITE 11 11 Proton acceptor. {ECO:0000250}. FT ACT_SITE 43 43 Redox-active. FT BINDING 43 43 FAD. {ECO:0000250}. FT BINDING 197 197 NAD. {ECO:0000250}. FT BINDING 264 264 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 323 323 FAD; via amide nitrogen. {ECO:0000250}. FT MOD_RES 43 43 Cysteine sulfenic acid (-SOH). FT {ECO:0000250}. SQ SEQUENCE 479 AA; 52875 MW; 66B86EA3BA8E53F1 CRC64; MKKVIVIGVN HAGTSFIRTL LSKSKDFQVN AYDRNTNISF LGCGIALAVS GVVKNTEDLF YSTPEELKAM GANVFMAHDV VGLDLDKKQV IVKDLATGKE TVDHYDQLVV ASGAWPICMN VENEVTHTQL QFNHTDKYCG NIKNLISCKL YQHALTLIDS FRHDKSIKSV AIVGSGYIGL ELAEAAWQCG KQVTVIDMLD KPAGNNFDEE FTNELEKAMK KAGINLMMGS AVKGFIVDAD KNVVKGVETD KGRVDADLVI QSIGFRPNTQ FVPKDRQFEF NRNGSIKVNE YLQALNHENV YVIGGAAAIY DAASEQYENI DLATNAVKSG LVAAMHMIGS KAVKLESIVG TNALHVFGLN LAATGLTEKR AKMNGFDVGV SIVDDNDRPE FMGTFDKVRF KLIYDKKTLR LLGAQLLSWN TNHSEIIFYI ALAVQKKMLI SELGLVDVYF LPHYNKPFNF VLAAVLQALG FSYYTPKNK // ID NADE_MYCPN Reviewed; 248 AA. AC P75216; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable NH(3)-dependent NAD(+) synthetase; DE EC=6.3.1.5; GN Name=nadE; OrderedLocusNames=MPN_562; ORFNames=MP280; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC -!- SIMILARITY: Belongs to the NAD synthetase 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; U00089; AAB95928.1; -; Genomic_DNA. DR PIR; S73606; S73606. DR RefSeq; NP_110251.1; NC_000912.1. DR RefSeq; WP_010874919.1; NC_000912.1. DR ProteinModelPortal; P75216; -. DR IntAct; P75216; 2. DR EnsemblBacteria; AAB95928; AAB95928; MPN_562. DR GeneID; 876904; -. DR KEGG; mpn:MPN562; -. DR PATRIC; 20022603; VBIMycPne110_0624. DR KO; K01916; -. DR OMA; CARLRMA; -. DR OrthoDB; EOG64JFM7; -. DR BioCyc; MPNE272634:GJ6Z-608-MONOMER; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase 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_00193; NadE; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth. 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; Complete proteome; Ligase; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 248 Probable NH(3)-dependent NAD(+) FT synthetase. FT /FTId=PRO_0000152182. FT NP_BIND 31 38 ATP. {ECO:0000250}. FT ACT_SITE 33 33 {ECO:0000250}. SQ SEQUENCE 248 AA; 27892 MW; 68C5A04E86B93DE2 CRC64; MTKNLLNYLN ELEAWLTNYV NEAHAQGVVV GLSGGVDSAV VAAMTKKLFP QNHLTLVMHI NNSELDHKAT TALVEQLQLN NKQVDLEPPY RAMLQALTID PQKELMVAGN LKARLRMACL YTHAQKHNYL VLGTGNFIEY SLGYFTKWGD GACDVAPLAF LLKSDVYALS QHFNVPELVI ERAPTASLFA GQTDEAEMGL TYKELDQYFQ GHLQLSATKQ QRVDHLRQSS QHKRSLPKTF KPLYSFQI // ID NADK_MYCPN Reviewed; 259 AA. AC P75508; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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=MPN_267; ORFNames=MP566; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96214.1; -; Genomic_DNA. DR PIR; S73892; S73892. DR RefSeq; NP_109955.1; NC_000912.1. DR RefSeq; WP_010874624.1; NC_000912.1. DR ProteinModelPortal; P75508; -. DR IntAct; P75508; 1. DR EnsemblBacteria; AAB96214; AAB96214; MPN_267. DR GeneID; 877097; -. DR KEGG; mpn:MPN267; -. DR PATRIC; 20021859; VBIMycPne110_0286. DR KO; K00858; -. DR OMA; SGHFINE; -. DR OrthoDB; EOG6PZXDR; -. DR BioCyc; MPNE272634:GJ6Z-274-MONOMER; -. DR Proteomes; UP000000808; 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 1 259 NAD kinase. FT /FTId=PRO_0000120638. FT NP_BIND 43 44 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 111 112 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT ACT_SITE 43 43 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT BINDING 136 136 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. SQ SEQUENCE 259 AA; 29034 MW; AD381E3FB1F13805 CRC64; MKYKIFASTT PQTEPVLQKL KQVLKGCEAV EKGFDYLFVL GGDGFFVSTV ANYNCHNCRV VGINTGHLGF YTSFNEKDLD DNFLQKLQQC HFQRISLLEV SVNGQQHLVL NELAVYTNTA YPINIFIDGE AWEFYRGSGL LIGPRTGSTA LAKSAKGAVI FPGIDVLQII EMNPLLHPNQ VTIQSPIILP KETQVEFVVK KAFNPQQFPT FYCDGRKLEL PNADTTLALK LVQSTPMFNI SLKTQDFINK LKSTFIKQS // ID NRDI_MYCPN Reviewed; 153 AA. AC P75460; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 82. DE RecName: Full=Protein NrdI; GN Name=nrdI; OrderedLocusNames=MPN_323; ORFNames=MP513; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Probably involved in ribonucleotide reductase function. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NrdI 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; U00089; AAB96161.1; -; Genomic_DNA. DR PIR; S73839; S73839. DR RefSeq; NP_110011.1; NC_000912.1. DR RefSeq; WP_010874679.1; NC_000912.1. DR ProteinModelPortal; P75460; -. DR IntAct; P75460; 2. DR EnsemblBacteria; AAB96161; AAB96161; MPN_323. DR GeneID; 876949; -. DR KEGG; mpn:MPN323; -. DR PATRIC; 20022000; VBIMycPne110_0347. DR KO; K03647; -. DR OMA; NTHRFVG; -. DR OrthoDB; EOG6W19RD; -. DR BioCyc; MPNE272634:GJ6Z-340-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_00128; NrdI; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR020852; RNR_Ib_NrdI_bac. DR InterPro; IPR004465; RNR_NrdI. DR Pfam; PF07972; Flavodoxin_NdrI; 1. DR PIRSF; PIRSF005087; NrdI; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR TIGRFAMs; TIGR00333; nrdI; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 153 Protein NrdI. FT /FTId=PRO_0000164323. SQ SEQUENCE 153 AA; 17151 MW; 6580845DB93B9319 CRC64; MHKDIKIVDA SAIVKPTGTP YVVYFSSISN NTHRFIEKLE FEHTRIPVNL DEQIEVNQEY VLFCPTYSGG GEYTSGAVPK QVIHFLNNKH NRDLCRGVIS SGNTNFGNTF AIAGPILSKK LNVPLLYQFE LLGTKNDVEQ VQTIITNFFG KAK // ID NRNA_MYCPN Reviewed; 324 AA. AC P75144; Q50340; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Bifunctional oligoribonuclease and PAP phosphatase NrnA; DE EC=3.1.-.-; DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase; DE EC=3.1.3.7; DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase; DE Short=PAP phosphatase; DE AltName: Full=Mgp-operon protein 1; DE Short=Mgp1; DE AltName: Full=ORF-1 protein; DE AltName: Full=nanoRNase; GN Name=nrnA; OrderedLocusNames=MPN_140; ORFNames=MP014; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-324. RC STRAIN=ATCC 29342 / M129; RX PubMed=2468577; DOI=10.1016/0378-1119(88)90323-X; RA Inamine J.M., Loechel S., Hu P.C.; RT "Analysis of the nucleotide sequence of the P1 operon of Mycoplasma RT pneumoniae."; RL Gene 73:175-183(1988). RN [3] RP FUNCTION AS AN EXONUCLEASE, FUNCTION AS A PAP PHOSPHATASE, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 29342 / M129; RX PubMed=21087930; DOI=10.1074/jbc.M110.161596; RA Wakamatsu T., Kim K., Uemura Y., Nakagawa N., Kuramitsu S., Masui R.; RT "Role of RecJ-like protein with 5'-3' exonuclease activity in RT oligo(deoxy)nucleotide degradation."; RL J. Biol. Chem. 286:2807-2816(2011). RN [4] RP FUNCTION AS AN OLIGORIBONUCLEASE, FUNCTION AS A PAP PHOSPHATASE, RP COFACTOR, AND MUTAGENESIS OF 118-ASP--HIS-120. RC STRAIN=ATCC 29342 / M129; RX PubMed=22114320; DOI=10.1261/rna.029132.111; RA Postic G., Danchin A., Mechold U.; RT "Characterization of NrnA homologs from Mycobacterium tuberculosis and RT Mycoplasma pneumoniae."; RL RNA 18:155-165(2012). CC -!- FUNCTION: Bifunctional enzyme which has both oligoribonuclease and CC pAp-phosphatase activities. Degrades RNA and DNA oligonucleotides CC with a length of 5 nucleotides and shorter, with a preference for CC longer oligomers. Also degrades 11- and 24-mers, but less CC efficiently. Directionality is controversial; shown to degrade 5- CC mers and less in a 3' to 5' direction (PubMed:22114320), and 11- CC mers in a 5' to 3' direction (PubMed:21087930). Converts 3'(2')- CC phosphoadenosine 5'-phosphate (PAP) to AMP. CC {ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320}. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O = CC adenosine 5'-phosphate + phosphate. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:21087930, CC ECO:0000269|PubMed:22114320}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:21087930, CC ECO:0000269|PubMed:22114320}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:21087930, CC ECO:0000269|PubMed:22114320}; CC Note=Divalent metal cations; Co(2+), Mn(2+) or Mg(2+). CC {ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.75 uM for ssDNA 6-mers in the presence of Mg(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=1.5 uM for ssDNA 6-mers in the presence of Mn(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=0.32 uM for ssRNA 6-mers in the presence of Mg(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=0.96 uM for ssRNA 6-mers in the presence of Mn(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=3.5 uM for ssDNA 11-mers in the presence of Mn(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=2.9 uM for ssRNA 11-mers in the presence of Mn(2+) CC {ECO:0000269|PubMed:21087930}; CC KM=32 uM for PAP in the presence of Mn(2+) CC {ECO:0000269|PubMed:21087930}; CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:21087930}. CC -!- MISCELLANEOUS: In accordance with its dual activities, is able to CC complement both orn and cysQ mutants in E.coli. CC -!- SIMILARITY: Belongs to the NrnA oligoribonuclease family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA88324.1; 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; U00089; AAB95662.1; -; Genomic_DNA. DR EMBL; M21519; AAA88324.1; ALT_INIT; Genomic_DNA. DR PIR; S73340; S73340. DR RefSeq; NP_109828.1; NC_000912.1. DR RefSeq; WP_010874497.1; NC_000912.1. DR ProteinModelPortal; P75144; -. DR EnsemblBacteria; AAB95662; AAB95662; MPN_140. DR GeneID; 877340; -. DR KEGG; mpn:MPN140; -. DR PATRIC; 20021595; VBIMycPne110_0154. DR KO; K06881; -. DR OMA; RNVAIKW; -. DR OrthoDB; EOG6FBX0G; -. DR BioCyc; MPNE272634:GJ6Z-147-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. PE 1: Evidence at protein level; KW Complete proteome; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 324 Bifunctional oligoribonuclease and PAP FT phosphatase NrnA. FT /FTId=PRO_0000096466. FT MUTAGEN 118 120 DHH->AAA: Loss of activity on 5-mers, 15% FT activity on 24-mers, no longer FT complements E.coli orn mutant. FT {ECO:0000269|PubMed:22114320}. SQ SEQUENCE 324 AA; 37145 MW; F1BFDC4A4983A1F7 CRC64; MNSQVHRKGS IAEAVSAIQA HDKIVIFHHI RPDGDCLGAQ HGLARLIQTN FPHKQVFCVG DPKHNFPWLE MVFTPKEQIT PELMQQALAV IVDANYKERI ECRDLLDQNQ FKAVLRIDHH PNEDDLNTTH NFVDASYIAA AEQVVDLAVQ AKWKLSPPAA TALYLGIYTD SNRFLYSNTS WRTLYLGSML YRAQANIAKI HDELNHTSLK DIQFKQYVFK NFQTFQNVIY FVADKKFQKK LKVTPLECAR VNILANIEQF HIWLFFIEEG KNHYRVEFRS NGINVREVAL KYGGGGHIQA SGAVLKSKRD IIRVVQDCQK QIAV // ID NUSA_MYCPN Reviewed; 540 AA. AC P75591; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN OrderedLocusNames=MPN_154; ORFNames=MP677; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Participates in both transcription termination and CC antitermination. {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00945}. CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|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; U00089; AAB96325.1; -; Genomic_DNA. DR PIR; S74003; S74003. DR RefSeq; NP_109842.1; NC_000912.1. DR RefSeq; WP_010874511.1; NC_000912.1. DR ProteinModelPortal; P75591; -. DR EnsemblBacteria; AAB96325; AAB96325; MPN_154. DR GeneID; 877301; -. DR KEGG; mpn:MPN154; -. DR PATRIC; 20021629; VBIMycPne110_0171. DR KO; K02600; -. DR OMA; PANQIAN; -. DR OrthoDB; EOG6NSGHW; -. DR BioCyc; MPNE272634:GJ6Z-161-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO: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; 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; IPR010213; Tscrpt_termination_fac_NusA. DR Pfam; PF13184; KH_5; 1. DR Pfam; PF08529; NusA_N; 1. DR SMART; SM00322; KH; 2. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54814; SSF54814; 2. DR SUPFAM; SSF69705; SSF69705; 1. DR TIGRFAMs; TIGR01953; NusA; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Reference proteome; RNA-binding; KW Transcription; Transcription antitermination; KW Transcription regulation; Transcription termination. FT CHAIN 1 540 Transcription termination/antitermination FT protein NusA. FT /FTId=PRO_0000181972. FT DOMAIN 144 214 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_00945}. FT DOMAIN 319 386 KH. {ECO:0000255|HAMAP-Rule:MF_00945}. SQ SEQUENCE 540 AA; 60272 MW; 0A30E0AE6B998A7F CRC64; MNNQSNHFTN PLLQLIKNVA ETKNLAIDDV VLCLKTALAQ TYKKHLNYVN VEVNIDFNKG LMQIEQLFDV VDDNNEDYDD FLEMPLSEAK KLNPNLEVGG VLRKPVSLKD IKGDLISKMV LLFNQKINET AFKTVMSDFI NEVGQVIEAR VEDIDTNKDG GLKGYIVNLE TTKGYMPKRE LSKGEKLDIG KKYLFVIKEI QKQSSMWPIT LSRSDSRLLE FLLNSNTPEI ANGTIEIKKM ERSPGTKSKV AVISKDPVVD PIAAILGPKG ERIRGISEEF NGEIIDIVIW NEDKLKFLVN AVLPAEVVGY NILQDDERDT SIEIVVPANQ IANVFGFKGI NIRLISNLTG WSSVDVYTEK DAAEQGIEFT RVNFQPQGIF GIKKRRDKIS NNPRNNNQQL ASDKVFYTSK ANVVDDEIIV DLAKQAEAKR VKQIKQEATK PELQLQQELN LEATPKVAAP TPTPAPQPTP APTKVEPVPP PVSVTPKPIP KVNKPKPVVK PKSVFSITVE ADDSKTKPEK SSAKTNTPQT KQTFDNFDDL // ID ODPA_MYCPN Reviewed; 358 AA. AC P75390; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha; DE EC=1.2.4.1; GN Name=pdhA; OrderedLocusNames=MPN_393; ORFNames=MP445; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96093.1; -; Genomic_DNA. DR PIR; S73771; S73771. DR RefSeq; NP_110081.1; NC_000912.1. DR RefSeq; WP_010874749.1; NC_000912.1. DR ProteinModelPortal; P75390; -. DR IntAct; P75390; 3. DR EnsemblBacteria; AAB96093; AAB96093; MPN_393. DR GeneID; 877083; -. DR KEGG; mpn:MPN393; -. DR PATRIC; 20022162; VBIMycPne110_0424. DR KO; K00161; -. DR OMA; LILYWRA; -. DR OrthoDB; EOG6VMTKR; -. DR BioCyc; MetaCyc:MONOMER-586; -. DR BioCyc; MPNE272634:GJ6Z-416-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017596; PdhA/BkdA. DR InterPro; IPR029061; THDP-binding. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 358 Pyruvate dehydrogenase E1 component FT subunit alpha. FT /FTId=PRO_0000162201. SQ SEQUENCE 358 AA; 40594 MW; E6184A2026D7A143 CRC64; MAILIKNKVP TTLYQVYDNE GKLMDPNHKI TLSNEQLKHA FYLMNLSRIM DKKMLVWQRA GKMLNFAPNL GEEALQVGMG MGLNENDWFC PTFRSGALML YRGVKPEQLL LYWNGNENGS KIEAKYKTLP INITIGAQYS HAAGLGYMLH YKKLPNVAVT MIGDGGTAEG EFYEAMNIAS IHKWNSVFCI NNNQFAISTR TKLESAVSDL STKAIAVNIP RIRVDGNDLI ASYEAMHEAA NYARSGNGPV LIEFFSWRQG PHTTSDDPSI YRTKEEEAEA MKSDPVKRLR NFLFDRGILT PQQEEEMVAK IEQEVQAAYE VMVSKTPVTL DEVFDYNYEK LTPDLARQKA EAKKYFKD // ID OPPD_MYCPN Reviewed; 423 AA. AC P75552; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Oligopeptide transport ATP-binding protein OppD; GN Name=oppD; OrderedLocusNames=MPN_217; ORFNames=MP614; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96262.1; -; Genomic_DNA. DR PIR; S73940; S73940. DR RefSeq; NP_109905.1; NC_000912.1. DR RefSeq; WP_010874574.1; NC_000912.1. DR ProteinModelPortal; P75552; -. DR EnsemblBacteria; AAB96262; AAB96262; MPN_217. DR GeneID; 877077; -. DR KEGG; mpn:MPN217; -. DR PATRIC; 20021759; VBIMycPne110_0236. DR KO; K15583; -. DR OMA; EIEENHF; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-224-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 423 Oligopeptide transport ATP-binding FT protein OppD. FT /FTId=PRO_0000092657. FT DOMAIN 24 309 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 58 65 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 423 AA; 47407 MW; 727028A1627275ED CRC64; MALKATNFFT EPEYKLQDDL ILDIRDLHVS FKVKDGIMQA VRGVDLKVKK GSIVGIVGES GSGKSVCVKS IIGFNDGAKT TAKLMNFKNI DISKMKKHQW QYYRGTYVSY ISQDPLFSLN PTMTIGRQVK EAIYVSCKRR YYQTKSDLKY DLQTERIDLD TYKEKLAQAK ETYKAKTTKA AVHAKTLEIL NFIGIDQAEK RLKAFPSEFS GGMRQRIVIA IAVATEPDLI IADEPTTALD VTIQAKALNL IKQLRDLLNI TIIFISHNIS LIANFCDFVY VMYAGRLVEK GLVEEIFTNP VHPYTWALMA SIPEGTDKNA PLTSIPGYIP NMLSPPKGDA FAARNQFALA IDFEHQPPFF DVTETHKAAT WLLHPQAPKV EMPADVKEKI AITRKALAIK MPSQPVKQPK SNGNKKTKTK SAR // ID OBG_MYCPN Reviewed; 433 AA. AC P75215; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454}; DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454}; DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454}; GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=MPN_563; GN ORFNames=MP279; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly CC (p)ppGpp with moderate affinity, with high nucleotide exchange CC rates and a fairly low GTP hydrolysis rate. Plays a role in CC control of the cell cycle, stress response, ribosome biogenesis CC and in those bacteria that undergo differentiation, in CC morphogenesis control. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_01454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95927.1; -; Genomic_DNA. DR PIR; S73605; S73605. DR RefSeq; NP_110252.1; NC_000912.1. DR RefSeq; WP_010874920.1; NC_000912.1. DR ProteinModelPortal; P75215; -. DR IntAct; P75215; 4. DR EnsemblBacteria; AAB95927; AAB95927; MPN_563. DR GeneID; 876882; -. DR KEGG; mpn:MPN563; -. DR PATRIC; 20022605; VBIMycPne110_0625. DR KO; K03979; -. DR OMA; TAIYDAD; -. DR OrthoDB; EOG6H1Q1M; -. DR BioCyc; MPNE272634:GJ6Z-609-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.210.12; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01454; GTPase_Obg; 1. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR014100; GTP-bd_Obg/CgtA. DR InterPro; IPR015349; GTP-bd_prot_GTP1/OBG_C. 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; PF09269; DUF1967; 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; SSF102741; SSF102741; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF82051; SSF82051; 1. DR TIGRFAMs; TIGR02729; Obg_CgtA; 1. DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1. DR PROSITE; PS51710; G_OBG; 1. DR PROSITE; PS00905; GTP1_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 433 GTPase Obg. FT /FTId=PRO_0000205442. FT DOMAIN 160 329 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 212 215 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 282 285 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 310 312 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT METAL 173 173 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT METAL 193 193 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. SQ SEQUENCE 433 AA; 47951 MW; D0D8A4E044EDCECA CRC64; MGLTDYCECR FSAGNGGNGI IAWRREAHYD KGGPGGGNGG NGGNVVLQAD HNCDSLFFLK NKKHLFAESG GNGKPDLAHG KNGEDLVIKV PVGTTVRDLD TNQILMDFVH DQQSFILCYG GKGGKGNAAF KSPIMRAPNL YENGDKGQSL HVSLEIKYLA NVGIVGFPNT GKSTLISKLS NAKPKIANYR FTTLVPVLGV VKHNDQSLVF ADIPGLIENA SEGSGLGHYF LRHIERCEIL IHLISLDPVD HDDPCQAYEQ IMRELSKYSQ LLVKKKMLVV ANKTDVDLDG TRFQKLAQYL ENKGIPLFKI SALKQELGDL VAQVFALHQK TLAQFGANKF HLPMEMEKHY VFEQASETDH DPLNIERDAL GRWHVECKRL HYWFDKIPQT TLDNIRRLGN KIKEVGIEDQ LKVAGAKKGD VIVFAGQEFV IND // ID ODP2_MYCPN Reviewed; 402 AA. AC P75392; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; DE EC=2.3.1.12; DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; DE AltName: Full=E2; GN Name=pdhC; OrderedLocusNames=MPN_391; ORFNames=MP447; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine CC = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01066, 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; U00089; AAB96095.1; -; Genomic_DNA. DR PIR; S73773; S73773. DR RefSeq; NP_110079.1; NC_000912.1. DR RefSeq; WP_010874747.1; NC_000912.1. DR ProteinModelPortal; P75392; -. DR IntAct; P75392; 1. DR EnsemblBacteria; AAB96095; AAB96095; MPN_391. DR GeneID; 877106; -. DR KEGG; mpn:MPN391; -. DR PATRIC; 20022158; VBIMycPne110_0422. DR KO; K00627; -. DR OMA; PMMELRE; -. DR OrthoDB; EOG610413; -. DR BioCyc; MetaCyc:MONOMER-584; -. DR BioCyc; MPNE272634:GJ6Z-413-MONOMER; -. DR Proteomes; UP000000808; Chromosome. 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 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; IPR011053; Single_hybrid_motif. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Glycolysis; Lipoyl; KW Reference proteome; Transferase. FT CHAIN 1 402 Dihydrolipoyllysine-residue FT acetyltransferase component of pyruvate FT dehydrogenase complex. FT /FTId=PRO_0000162282. FT DOMAIN 2 77 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT ACT_SITE 374 374 {ECO:0000255}. FT MOD_RES 43 43 N6-lipoyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. SQ SEQUENCE 402 AA; 42397 MW; F09314A9E714A1D6 CRC64; MANEFKFTDV GEGLHEGKVT EILKKVGDTI KVDEALFVVE TDKVTTELPS PYAGVITAIT TNVGDVVHIG QVMAVIDDGA GAAAPAAPQP VSAPAPAPTP TFTPTPAPVT TEPVVEEAGA SVVGEIKVSN SVFPIFGVQP SAPQPTPAPV VQPTSAPTPT PAPASAAAPS GEETIAITTM RKAIAEAMVK SHENIPATIL TFYVNATKLK QYRESVNGLA LSKYNMKISF FAFFVKAIVN ALKKFPVFNG RYDKERNLIV LNKDVNVGIA VDTPDGLIVP NIKQAQTKSV VDIAKDIVDL ANRARSKQIK LPDLSKGTIS VTNFGSLGAA FGTPIIKHPE MCIVATGNME ERVVRAEGGV AVHTILPLTI AADHRWVDGA DVGRFGKEIA KQIEELIDLE VA // ID OPPC_MYCPN Reviewed; 376 AA. AC P75553; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Oligopeptide transport system permease protein OppC; GN Name=oppC; OrderedLocusNames=MPN_216; ORFNames=MP615; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides; probably responsible for the translocation of CC the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. OppBC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96263.1; -; Genomic_DNA. DR PIR; S73941; S73941. DR RefSeq; NP_109904.1; NC_000912.1. DR RefSeq; WP_010874573.1; NC_000912.1. DR ProteinModelPortal; P75553; -. DR IntAct; P75553; 1. DR EnsemblBacteria; AAB96263; AAB96263; MPN_216. DR GeneID; 876977; -. DR KEGG; mpn:MPN216; -. DR PATRIC; 20021757; VBIMycPne110_0235. DR KO; K15582; -. DR OMA; DRIVIDY; -. DR OrthoDB; EOG6HTNTX; -. DR BioCyc; MPNE272634:GJ6Z-223-MONOMER; -. DR Proteomes; UP000000808; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Peptide transport; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 376 Oligopeptide transport system permease FT protein OppC. FT /FTId=PRO_0000060142. FT TRANSMEM 46 66 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 149 169 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 173 193 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 209 229 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 242 262 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 297 317 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 341 361 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 169 362 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 376 AA; 41234 MW; FD3042160B7F9797 CRC64; MDKHQKFDQS LFQRVDINVL KRSDQLIGKP TTNFVEIMKR LFQNKWAILF FLLIVLIILL AIIVPLASPY SAVTPVSNNA LAQNLPPRYL WNGAGDIQVE KITARSIAEV AQSSGVLVGK LPEASSNPLA TNVKYNIAPY QLAELKNYYP LLGTNGLGVD IWTLLWASMA KSLWIAIVVA LVSMVFGTIY GAIAGSFVGR AADNIMSRII EIIDLVPSIL WIIVLGATFR FGGVKQFDDS VVIFTLIFVF WTWPAATTRI YILKNKDTEY IQAARTLGAK QIRIIFVHML PVVTGRLAVV FVSLIPAVIG YEASLVFLGL KPATEVGLGA LLNQVTSSGN IALITSSIVS FAILTVSTRV FANALNDAID PRVIRR // ID NUSG_MYCPN Reviewed; 320 AA. AC P75049; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN OrderedLocusNames=MPN_067; ORFNames=D09_orf320, MP087; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Participates in transcription elongation, termination CC and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}. CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95735.1; -; Genomic_DNA. DR PIR; S73413; S73413. DR RefSeq; NP_109755.1; NC_000912.1. DR RefSeq; WP_010874424.1; NC_000912.1. DR ProteinModelPortal; P75049; -. DR IntAct; P75049; 2. DR EnsemblBacteria; AAB95735; AAB95735; MPN_067. DR GeneID; 876828; -. DR KEGG; mpn:MPN067; -. DR PATRIC; 20021413; VBIMycPne110_0068. DR KO; K02601; -. DR OMA; SEDAWRI; -. DR OrthoDB; EOG6FFS95; -. DR BioCyc; MPNE272634:GJ6Z-69-MONOMER; -. DR Proteomes; UP000000808; 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; 3.30.70.940; -; 1. DR HAMAP; MF_00948; NusG; 1. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR001062; Transcrpt_antiterm_NusG. DR InterPro; IPR010216; Transcrpt_antiterm_NusG_myco. DR Pfam; PF02357; NusG; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF82679; SSF82679; 2. DR TIGRFAMs; TIGR01956; NusG_myco; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Transcription; Transcription antitermination; KW Transcription regulation; Transcription termination. FT CHAIN 1 320 Transcription termination/antitermination FT protein NusG. FT /FTId=PRO_0000113975. SQ SEQUENCE 320 AA; 36107 MW; ECE3C626C8EAE63F CRC64; MEQVELIPQW YVAPVSVKDE AVVRNLKAKV KALGFDNEIL DVRVLKEREV IEEVFSLKSG KLPRSLKNTA FTKWFVLDED RYLKVKISEK NLLGRYIYIK MIYSEDAWRI IRNFPGITGI VGSSGRGALP TPLDQADADN LEQMLKGISV NPKKRVLVTN TAIVEMDADK FDEKCQYILK HKQVKPEAIA QVNESGEIID TNQFAQALME ANKAEQDEWN EDVAIVKSEA NKVDPSVLIP YLGKYEIVEG DTKVDQLQQF SVGNLVEVHL TGAIHIQGQI KALYQGTINK AVVEVELTTK TQLINLPLEN LSFIEVEQSH // ID OTCC_MYCPN Reviewed; 346 AA. AC P75473; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2003, sequence version 2. DT 11-MAY-2016, entry version 108. DE RecName: Full=Ornithine carbamoyltransferase, catabolic {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=arcB {ECO:0000255|HAMAP-Rule:MF_01109}; GN OrderedLocusNames=MPN_306; ORFNames=MP530; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 degradation; L-arginine degradation via ADI CC pathway; carbamoyl phosphate from L-arginine: step 2/2. 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 -!- SEQUENCE CAUTION: CC Sequence=AAB96178.1; Type=Frameshift; Positions=32; 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; U00089; AAB96178.1; ALT_FRAME; Genomic_DNA. DR PIR; S73856; S73856. DR RefSeq; YP_009121719.1; NC_000912.1. DR ProteinModelPortal; P75473; -. DR IntAct; P75473; 2. DR EnsemblBacteria; AAB96178; AAB96178; MPN_306. DR GeneID; 876935; -. DR KEGG; mpn:MPN306; -. DR PATRIC; 20021964; VBIMycPne110_0330. DR OMA; DFRIFAP; -. DR OrthoDB; EOG690MGV; -. DR BioCyc; MetaCyc:MONOMER-533; -. DR BioCyc; MPNE272634:GJ6Z-322-MONOMER; -. DR UniPathway; UPA00254; UER00365. DR Proteomes; UP000000808; 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:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway. DR GO; GO:0019546; P:arginine deiminase pathway; 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 Arginine metabolism; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 346 Ornithine carbamoyltransferase, FT catabolic. FT /FTId=PRO_0000112954. FT REGION 58 62 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT REGION 136 139 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT REGION 243 244 Ornithine binding. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT REGION 279 282 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT BINDING 85 85 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 109 109 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 168 168 Ornithine. {ECO:0000250}. FT BINDING 239 239 Ornithine. {ECO:0000250}. FT BINDING 314 314 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 332 332 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT SITE 149 149 Important for structural integrity. FT {ECO:0000255|HAMAP-Rule:MF_01109}. SQ SEQUENCE 346 AA; 38149 MW; 51BC8925AF8888EF CRC64; MPINLKGRSL DSALNFTTAQ INYLIDLAID LNAVNTKLHI QNRPLAGKNI VLLFQKDSTR TRCAFEVAAF DLGMGCTYIG PSGSNFGKKE SIEDTAKVLG SMYDGIEFRG FKQSDVDALV KYSGVPVWNG LTDAEHPTQM LADYMTIKEL KGDLKGRKIV FAGDIKNNVA RSLMIGAAFV GMDIVLVGPK AQHELVQNGA GYKEVFEQCQ ALFQLNGGSV SFSTDKLQAA KNADVIYTDV WLSLGEDFSL FEERIQELGQ FQVDMAMIKA AKSDVIFLHC LPAFHDDHTS FSLEIKQKLG KKYPVVKTGA MEVTDTVFQS KHNMAFIQAE NRLHTIKAVI LATLGY // ID ODPB_MYCPN Reviewed; 327 AA. AC P75391; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta; DE EC=1.2.4.1; GN Name=pdhB; OrderedLocusNames=MPN_392; ORFNames=MP446; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96094.1; -; Genomic_DNA. DR PIR; S73772; S73772. DR RefSeq; NP_110080.1; NC_000912.1. DR RefSeq; WP_010874748.1; NC_000912.1. DR ProteinModelPortal; P75391; -. DR IntAct; P75391; 3. DR EnsemblBacteria; AAB96094; AAB96094; MPN_392. DR GeneID; 877125; -. DR KEGG; mpn:MPN392; -. DR PATRIC; 20022160; VBIMycPne110_0423. DR KO; K00162; -. DR OMA; LAWGAQM; -. DR OrthoDB; EOG6JQH4C; -. DR BioCyc; MetaCyc:MONOMER-587; -. DR BioCyc; MPNE272634:GJ6Z-415-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR PANTHER; PTHR11624; PTHR11624; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 327 Pyruvate dehydrogenase E1 component FT subunit beta. FT /FTId=PRO_0000162224. FT BINDING 63 63 Thiamine pyrophosphate. {ECO:0000250}. SQ SEQUENCE 327 AA; 35914 MW; 06513520FDAFED54 CRC64; MSKTIQANNI EALGNAMDLA LERDPNVVLY GQDAGFEGGV FRATKGLQKK YGEERVWDCP IAEAAMAGIG VGAAIGGLKP IVEIQFSGFS FPAMFQIFTH AARIRNRSRG VYTCPIIVRM PMGGGIKALE HHSETLEAIY GQIAGLKTVM PSNPYDTKGL FLAAVESPDP VVFFEPKKLY RAFRQEIPAD YYTVPIGQAN LISQGNNLTI VSYGPTMFDL INMVYGGELK DKGIELIDLR TISPWDKETV FNSVKKTGRL LVVTEAAKTF TTSGEIIASV TEELFSYLKA APQRVTGWDI VVPLARGEHY QFNLNARILE AVNQLLK // ID P29_MYCPN Reviewed; 244 AA. AC P75370; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Probable ABC transporter ATP-binding protein p29; GN Name=p29; OrderedLocusNames=MPN_416; ORFNames=MP424; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of a high-affinity transport system. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96072.1; -; Genomic_DNA. DR PIR; S73750; S73750. DR RefSeq; NP_110104.1; NC_000912.1. DR RefSeq; WP_010874772.1; NC_000912.1. DR ProteinModelPortal; P75370; -. DR IntAct; P75370; 3. DR EnsemblBacteria; AAB96072; AAB96072; MPN_416. DR GeneID; 877307; -. DR KEGG; mpn:MPN416; -. DR PATRIC; 20022228; VBIMycPne110_0451. DR KO; K02041; -. DR OMA; QTNDAMM; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; MPNE272634:GJ6Z-445-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 244 Probable ABC transporter ATP-binding FT protein p29. FT /FTId=PRO_0000092679. FT DOMAIN 6 241 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 244 AA; 28010 MW; FDE4A4F6FCF1067D CRC64; MVNPVLVFDQ VSLRYNGAPL LENINFTISP GEHICLLGKS GVGKTSLLNC ITNTKTISKG TIYFNGIASN NKDYKQLKKQ FSFLDQVPNL IDTDFVYDAI WREAKNNLKW WQRLFLVEPQ SLREQIIQIL EEVNLKEYVT YIIKDLSGGQ KQRVEVAKLF FANSQVLLVD EPTTGLDLIN AHKIMELIIQ FARQKAMTLI FVTHDVEFAL KYSDRIIALK NKALVLDQAT NKLTKQKLMQ IYHD // ID OHRL_MYCPN Reviewed; 140 AA. AC P75123; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Organic hydroperoxide resistance protein-like; GN OrderedLocusNames=MPN_668; ORFNames=K05_orf140, MP174; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the OsmC/Ohr 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; U00089; AAB95822.1; -; Genomic_DNA. DR PIR; S73500; S73500. DR RefSeq; NP_110357.1; NC_000912.1. DR RefSeq; WP_010875025.1; NC_000912.1. DR ProteinModelPortal; P75123; -. DR IntAct; P75123; 4. DR EnsemblBacteria; AAB95822; AAB95822; MPN_668. DR GeneID; 877018; -. DR KEGG; mpn:MPN668; -. DR PATRIC; 20022821; VBIMycPne110_0733. DR OMA; RLEHATN; -. DR OrthoDB; EOG6HQSVF; -. DR BioCyc; MPNE272634:GJ6Z-714-MONOMER; -. DR Proteomes; UP000000808; 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; IPR019953; OHR. DR InterPro; IPR003718; OsmC/Ohr_fam. DR Pfam; PF02566; OsmC; 1. DR SUPFAM; SSF82784; SSF82784; 1. DR TIGRFAMs; TIGR03561; organ_hyd_perox; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Organic hydroperoxide resistance protein- FT like. FT /FTId=PRO_0000172732. SQ SEQUENCE 140 AA; 14882 MW; 985660EEEC229265 CRC64; MAVIYKTTAH ASAGREGVVQ TVDGFTVSLA FPKPGATHQD KNNPEQLFAS AYAGCFSQAV RVVLQQHQLQ LATQPIVGVS VELHDQDGLF HIKAGVELAI TGVDQTTAQT VITAAHAMCP FSRLIKPENF LGLTLNGAKL // ID OPPB_MYCPN Reviewed; 389 AA. AC P75554; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Oligopeptide transport system permease protein OppB; GN Name=oppB; OrderedLocusNames=MPN_215; ORFNames=MP616; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides; probably responsible for the translocation of CC the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. OppBC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96264.1; -; Genomic_DNA. DR PIR; S73942; S73942. DR RefSeq; NP_109903.1; NC_000912.1. DR RefSeq; WP_010874572.1; NC_000912.1. DR ProteinModelPortal; P75554; -. DR EnsemblBacteria; AAB96264; AAB96264; MPN_215. DR GeneID; 877136; -. DR KEGG; mpn:MPN215; -. DR PATRIC; 20021755; VBIMycPne110_0234. DR KO; K15581; -. DR OMA; DSWKHYI; -. DR OrthoDB; EOG6JHRMD; -. DR BioCyc; MPNE272634:GJ6Z-222-MONOMER; -. DR Proteomes; UP000000808; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein 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 Cell membrane; Complete proteome; Membrane; Peptide transport; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 389 Oligopeptide transport system permease FT protein OppB. FT /FTId=PRO_0000060140. FT TRANSMEM 1 21 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 83 103 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 115 135 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 161 181 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 220 240 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 270 290 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 79 289 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 389 AA; 43538 MW; A2A7189BABFD9017 CRC64; MFIVMTIVFF LVNSTGQTPL SATSSKDLEA VKTQLDAFGF NDPLIVRYGR YWQTLFSGSL GTYYSSPNQT IDQIVFGRVP NTLYVVLISF FIGSLLGIIF GMISGLFRGK LIDAVINVLV VLFVSIPSFV VGLGLLKAAG LFRLPPRFIN FDDANFNFGN FLLASIIPIL SLVFYTSAAF TYRVRNEVVE VMNQDYIKTA RSKGLSTFAV ALYHIFRNSI IPSVPLFVFG ISGAFSGGFI IESLFGVQGV SRILIDSVQS NETNLVMFNI MFIQGIPLLA SVFIELIYVL VDPRIRIASA GGVSLWTKLK FVYLRQAWLR KWRRINHTNS HNVLFNSPQH RQLLELKAID YKHNTISLTE QQKTTLKIEP TANFVLLGTK CLKIITIHG // ID OPPF_MYCPN Reviewed; 851 AA. AC P75551; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Oligopeptide transport ATP-binding protein OppF; GN Name=oppF; OrderedLocusNames=MPN_218; ORFNames=MP613; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96261.1; -; Genomic_DNA. DR PIR; S73939; S73939. DR RefSeq; NP_109906.1; NC_000912.1. DR RefSeq; WP_010874575.1; NC_000912.1. DR ProteinModelPortal; P75551; -. DR IntAct; P75551; 1. DR PRIDE; P75551; -. DR EnsemblBacteria; AAB96261; AAB96261; MPN_218. DR GeneID; 876777; -. DR KEGG; mpn:MPN218; -. DR PATRIC; 20021761; VBIMycPne110_0237. DR KO; K10823; -. DR OMA; IMHLGKI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-225-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 851 Oligopeptide transport ATP-binding FT protein OppF. FT /FTId=PRO_0000092670. FT DOMAIN 14 788 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 48 55 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 851 AA; 98611 MW; 6D3A3EC76B27DCC2 CRC64; METKKQKQNP LVNVKALSML FKVRGSFFKA LDEIDFTVNE GDFFGVIGES GSGKSTTGKC LIRLNIPSGG KVEIANHLIS GKKLTRENDH WLKQNVQMVF QDPYSSLNPT KNVLTVISEP LVITKTVYGE VKEYLKTLAK LSFKTKKELL REDFELETQF YEKFFSKVLF HLETTINKFA LLQESNNNSS AELAQTILGH TDDLIEALRQ EFGLVYEFSS SQSEPLQKAL KDKQETLAQD TIDKLKQELY TTQQKAKVST QAFATWQKLQ QTKQNLKAYR AQMAEELQNK PRIYLNAWLL TTKNYIKDSR QNTQLTDDVF AFSYNDMVDK KRRLVLVLSE YYKALPYFYD NWIHQNADRF DELTNAVFFD LIDVVIALNR DFANVESDAK AELIRFVQFI RRLCDLRFAA LKKSFKKQTN YSFDFNRETE LLYANSCYDI KELPQVIQPY WEKLFSDANY DKIAKSVQEL NDIISTDIEK ASNIASEINT KISSFKTEIA ELKATFKTEK KAEDHSAQIT GLKTQIAEIQ TQIKQQKREV QSTEKAALKP VLKQYKSALH LYKRFKQLLR QFTKQLNLLV KKQQELEKIE EGLDLTIWER IQLLFYPVEG DLKSELKTRL KSFGVINFEY KRAVRESRVF RLVHFGHDVM KWGLFLPLTK IFMRNKVYEA LDSVGLKREH AYRYPHEFSG GQRQRIAIAR ALITKPKLII ADELISALDV SIQAQVINIL KDLAKKHNLT VLFIAHDLSM VQTVCNRLII MHRGKIVERG STDEIFAHPV HPYTRSLIKA SPKLSKINID LASFDEKFTY DSDYSLTNMP SFLKVPNTQE HELYCTQGQF DSWIKGASRI N // ID P37_MYCPN Reviewed; 380 AA. AC P75371; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=High affinity transport system protein p37; DE Flags: Precursor; GN Name=p37; OrderedLocusNames=MPN_415; ORFNames=MP425; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: P37 is part of a high-affinity transport system. CC -!- SUBCELLULAR LOCATION: Cell 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; U00089; AAB96073.1; -; Genomic_DNA. DR PIR; S73751; S73751. DR RefSeq; NP_110103.1; NC_000912.1. DR RefSeq; WP_010874771.1; NC_000912.1. DR IntAct; P75371; 1. DR EnsemblBacteria; AAB96073; AAB96073; MPN_415. DR GeneID; 877304; -. DR KEGG; mpn:MPN415; -. DR PATRIC; 20022226; VBIMycPne110_0450. DR KO; K02044; -. DR OMA; CARRESN; -. DR OrthoDB; EOG6HB9MH; -. DR BioCyc; MPNE272634:GJ6Z-444-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR010592; Mycoplasma_p37. DR Pfam; PF06646; Mycoplasma_p37; 1. DR PIRSF; PIRSF004523; Mycoplasma_p37; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal; Transport. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 380 High affinity transport system protein FT p37. FT /FTId=PRO_0000018096. FT LIPID 27 27 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 27 27 S-diacylglycerol cysteine. {ECO:0000305}. SQ SEQUENCE 380 AA; 43495 MW; B8EBDE2199CCC792 CRC64; MLKRKKLLQG FLKFLPLIIP ATIFVSCARR ESNHLIFNIS LDHDADASIS KFFELYSNNL SKKLDKKVTV SFNIIDDSFT KISNIQTAKA DFAFVNSQSI KDNGIEEFNL ILQTQTDAFK EDTNLDYYSD GQLKSKAEKM TTLFSKTPYK DWEDTAQQWT GSRYNFLYET NKLINFYRGM ILITGSEEEI KKIKEAWDQK KWSDFMNYGI GHGSSGSAGK FQLPDLLLRK HFGSSYPGLQ NAINQNPDKF ANVRGREIGR DNKIKIVFDD ANSFAWTHND KNATNHFYTP TENNGKGDSE KSNNKNNKVE ILTYTDPMLY DIGIVSDTLS DRYQKAIAEV FVELAKTKQD IYGPSYGYNG YNLITDPNKE ILDVIHKTYG // ID P65_MYCPN Reviewed; 405 AA. AC P0CJ81; P53663; P53664; Q6LAC2; Q6LAC3; DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE RecName: Full=Proline-rich P65 protein; GN Name=p65; OrderedLocusNames=MPN_309; ORFNames=MP527; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=7768845; RA Proft T., Hilbert H., Layh-Schmitt G., Herrmann R.; RT "The proline-rich P65 protein of Mycoplasma pneumoniae is a component RT of the Triton X-100-insoluble fraction and exhibits size polymorphism RT in the strains M129 and FH."; RL J. Bacteriol. 177:3370-3378(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-75 AND 83-95, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7768845, CC ECO:0000269|PubMed:7984111}; Peripheral membrane protein CC {ECO:0000269|PubMed:7768845, ECO:0000269|PubMed:7984111}. CC Note=Probably with epitopes exposed at the cell surface. CC -!- DOMAIN: The penta/hexapeptides repeats form a proline-rich acidic CC domain. In addition, a part of this region contains a perfect CC direct repeat. CC -!- PTM: The N-terminus is blocked. {ECO:0000305}. CC -!- CAUTION: The protein sequence for 83-95 might be that for residues CC 148-160; the 2 sequences are identical. CC {ECO:0000305|PubMed:7984111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z34977; CAA84429.1; -; Genomic_DNA. DR EMBL; U59896; AAB52526.1; -; Genomic_DNA. DR EMBL; U00089; AAB96175.1; -; Genomic_DNA. DR EMBL; Z32653; CAA83574.1; -; Genomic_DNA. DR EMBL; Z32655; CAA83576.1; -; Genomic_DNA. DR PIR; S73853; S73853. DR RefSeq; NP_109997.1; NC_000912.1. DR RefSeq; WP_010874665.1; NC_000912.1. DR EnsemblBacteria; AAB96175; AAB96175; MPN_309. DR GeneID; 876932; -. DR KEGG; mpn:MPN309; -. DR PATRIC; 20021970; VBIMycPne110_0333. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; MPNE272634:GJ6Z-325-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat. FT CHAIN 1 405 Proline-rich P65 protein. FT /FTId=PRO_0000058145. FT REPEAT 40 45 1. FT REPEAT 75 80 2. FT REPEAT 83 87 3. FT REPEAT 89 93 4. FT REPEAT 95 99 5. FT REPEAT 101 105 6. FT REPEAT 107 111 7. FT REPEAT 119 123 8. FT REPEAT 140 145 9. FT REPEAT 148 152 10. FT REPEAT 154 158 11. FT REPEAT 168 172 12. FT REGION 40 172 12 X 5 AA repeats of D-P-N-Q-A-Y. SQ SEQUENCE 405 AA; 47040 MW; 4805F2DAD0588232 CRC64; MDINKPGWNQ SDQQATAYDP NQQQYYGDGS TYYDPDQAVD PNQAYYPDPN TYPDAAAYYG YGQDGQAYPQ DYAQDPNQAY YADPNAYQDP NAYTDPNAYV DPNAYQDPNA YVDPNNYTDP NAYYGYGQDG QAYPQDYAQD PNQAYYADPN AYQDPNAYTD PYYVTSTDPN AYYGQVDNVP ALEASDLAYE VTPQEQAAEQ ELFSEPETKV IREIHEFPFE KIRSYFQTDF DSYNSRLTQL KDKLDNAIFS MRKAIDTVKE NSANLQIMKQ NFERQLKEQQ TQRLTSNTDA EKIGAKINQL EERMQRLSRT MESVEWTKKE PRQEQFDPRF VDPRNFNNYV NNTDTMMSMF EKVLMMNLLR STTPVQPPVQ YFTPQPLTAS PRPVYEEPIS ASFRRRGYRG DEFYE // ID PARC_MYCPN Reviewed; 789 AA. AC P75352; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00937}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00937}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00937}; GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00937}; GN OrderedLocusNames=MPN_123; ORFNames=MP031; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_00937}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00937}. CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00937}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00937}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00937}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00937}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95679.1; -; Genomic_DNA. DR PIR; S73357; S73357. DR RefSeq; NP_109811.1; NC_000912.1. DR RefSeq; WP_010874480.1; NC_000912.1. DR ProteinModelPortal; P75352; -. DR IntAct; P75352; 1. DR PRIDE; P75352; -. DR EnsemblBacteria; AAB95679; AAB95679; MPN_123. DR GeneID; 877177; -. DR KEGG; mpn:MPN123; -. DR PATRIC; 20021547; VBIMycPne110_0130. DR KO; K02621; -. DR OMA; GRYAKYI; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; MPNE272634:GJ6Z-130-MONOMER; -. DR Proteomes; UP000000808; 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_00937; ParC_type2; 1. DR InterPro; IPR024946; Arg_repress_C-like. 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; IPR005741; TopoIV_A_Gpos. DR Pfam; PF03989; DNA_gyraseA_C; 3. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01061; parC_Gpos; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; DNA-binding; Isomerase; Membrane; KW Reference proteome; Topoisomerase. FT CHAIN 1 789 DNA topoisomerase 4 subunit A. FT /FTId=PRO_0000145402. FT ACT_SITE 122 122 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00937}. FT SITE 42 42 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 78 78 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 80 80 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 91 91 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 97 97 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 121 121 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00937}. SQ SEQUENCE 789 AA; 88669 MW; EE3A7BF9A867BD19 CRC64; MEKNKQALLL QAIEDVFAFS FSKYAKYIIQ DRALPDLRDG LKPVQRRILY GMYQMGLKPT SPYKKSARAV GEIMGKYHPH GDASIYDAIV RMSQAWKNNL TTISIHGNNG SIDGDNAAAM RYTEARLSPY GFELLKDIEK QLVPFVNNFD DSEVEPSVLP TLLPNLFING TSGIAAGYAT NIAPHNVGEL LDGLSYRIEN PDCDLKAILK IVKGPDFPTG GLVYFEQELA NIYQTGKGKF VIQAKYETNT AFGQNQIVIT EIPYETVKAN IVKQIEELIS DNKLSALESV IDSSDRSGIR IIINHKDFLS ADKIMAFLFK HTQLQVNFNL NNTVIANRCP VRVGLLAYFD QFLAFAHELI INSAKYDLAL ANKRLEIIKG LIKAVSMIDE IIRLIRRATD KQDAKTKLID KYAFTLNQAE AIVSLRLYQL TNTDIKVLFA EQKELEQTIQ TAERLIAKPQ ARNQLLQAQF FQYKKQFNQP RRAQIVGLIE KQKVQDSDFI EHKEVGLLIS HDGIYFKFEP EQLAKHLVEF KSEQDQLIFG GVVQNSDYFF MVTSLGNIIT VPIYKTLSNT KTKMNELLAK KPILMEDEKL VLAGIVNPDK MEQQLLVLTS QCGMVKRVEL SKVINTKQIK SSCCMALRER DKLVNAFVQT KGEPKLVCLV SSSNSFATFL AEEIPIISNK GIGVKGIKLK AEEKVRFAMP LQDNDALVVI NSDGGVYNFE VVELAVASRM SVGKKLIPKT KTPVSCFAAN KHSEIIGHRG KNGSDLFTLN ELNRLPKSTV SQMRLFKWS // ID P200_MYCPN Reviewed; 1036 AA. AC P75211; Q50346; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Protein P200; GN Name=p200; OrderedLocusNames=MPN_567; ORFNames=MP275; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675035; DOI=10.1016/0378-1119(96)00014-5; RA Proft T., Hilbert H., Plagens H., Herrmann R.; RT "The P200 protein of Mycoplasma pneumoniae shows common features with RT the cytadherence-associated proteins HMW1 and HMW3."; RL Gene 171:79-82(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 641-678. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). RN [4] RP FUNCTION IN GLIDING MOTILITY, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 29342 / M129-B18; RX PubMed=17043103; DOI=10.1128/IAI.01344-06; RA Jordan J.L., Chang H.Y., Balish M.F., Holt L.S., Bose S.R., RA Hasselbring B.M., Waldo R.H. III, Krunkosky T.M., Krause D.C.; RT "Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption RT but not gliding motility or colonization of differentiated bronchial RT epithelium."; RL Infect. Immun. 75:518-522(2007). CC -!- FUNCTION: Protein cytoskeleton-associated which plays a role in CC gliding motility and perhaps also in mucociliary clearance. CC {ECO:0000269|PubMed:17043103}. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC {ECO:0000269|PubMed:17043103}. CC -!- DISRUPTION PHENOTYPE: Has impaired gliding motility, glides at a CC slower speed and with longer resting periods than wild-type. Binds CC equally well to erythrocytes and a human lung adenocarcinoma cell CC line, but colonizes mucin-producing cells less well than wild-type CC cells. {ECO:0000269|PubMed:17043103}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U25989; AAC99815.1; -; Genomic_DNA. DR EMBL; U00089; AAB95923.1; -; Genomic_DNA. DR EMBL; Z32646; CAA83569.1; -; Genomic_DNA. DR PIR; S73601; S73601. DR RefSeq; NP_110256.1; NC_000912.1. DR RefSeq; WP_010874924.1; NC_000912.1. DR ProteinModelPortal; P75211; -. DR IntAct; P75211; 3. DR EnsemblBacteria; AAB95923; AAB95923; MPN_567. DR GeneID; 876843; -. DR KEGG; mpn:MPN567; -. DR PATRIC; 20022613; VBIMycPne110_0629. DR OMA; QERESIF; -. DR OrthoDB; EOG6NGVSD; -. DR BioCyc; MPNE272634:GJ6Z-613-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033099; C:attachment organelle; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR InterPro; IPR022466; AGR_box. DR Pfam; PF16713; EAGR_box; 6. DR TIGRFAMs; TIGR03834; EAGR_box; 5. PE 1: Evidence at protein level; KW Cell projection; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 1036 Protein P200. FT /FTId=PRO_0000058128. FT REPEAT 718 723 1. FT REPEAT 738 743 2. FT REPEAT 776 781 3. FT REGION 718 781 3 X 6 AA repeats of E-P-E-P-N-F. FT COMPBIAS 277 280 Poly-Thr. FT COMPBIAS 300 845 Pro-rich. FT COMPBIAS 357 360 Poly-Thr. FT COMPBIAS 401 404 Poly-Ala. FT CONFLICT 641 641 A -> P (in Ref. 3; CAA83569). FT {ECO:0000305}. SQ SEQUENCE 1036 AA; 116915 MW; DE5AEBAB6DD95B29 CRC64; MPKTIKKQNP SNTTLQYKKY LEQSKEKTAK AKNKDVSIDD LLKKPFLEEI KTNVLKKNKT TRASTATRGT SKVKKQIVES SIDFFDEKKR GVFIVPPAGT SVINDDRDDN KAVEETVSKT AISQNQLAHY ANSELVETEQ FELKPVALEH NQVLTSTRHS QERESIFEKA QLFWQIFVGD VRFGFWKNHT WIWLGFFDQH QNWYYFEVVE TVELPQEHTA FIKRKQIDSC FWKPLVGNPN YGYIQNNIWV WKGFFDTKLN WIPDPVRFTL PMVEKATTTT PVVQIELPAP PTVTVVDQTS PPTAAVTVST SQPVIEEQTT VFNQTTQLEQ LSVSAPLLDQ SEVETEMVEV PFVAPSTTTT QPQVVTVQAQ PASSSIQFQE PIIKVEFVNE SFDFKKPSQT AAAASQAPSQ AINIALNEAD LIDELVAVGT TATTALPQSE LIQEVVVIDN GQPQQAGFHY VVDFLTSTAP LTVAEIELQE QELVNEFVTT TSRETTTFAS TPVFEPVVIP TVESEEQLLE NEFVESTVVS ATSNEPNVAS TPVVETVELT ETPVSLEPLE TVQLETAPVV TETVTVTEKA VEPEVLAVVE EAPLAVEPIV ETSTTLAAET VEEAQVEQES TAVAVEPAIE TESKATSEAQ AELDWEALIG NSEYGYFDAE QNWIWTGYFD EDNKWVSTAT AQTEANAEEV VLTADAETSE LNTESDPSFE PEVEIQPEPE PNFDLETIPE PESIETTEPE PNFEPEVELE PEIEPNFESE TEVQQELAQE SSFESEPEPN FETEVEVQPE SEIESKFEAE VQSEPKVSLN SDFETKPEAQ AEVTPETLEV EATSEAPELQ PETEATKVVD DVEEEQLDWE LLIGNSNYGH YEPSGEWVWA GYFDDNQIWT PDASVEWARE SDYTDLIGDE IYGRYNRKGE WIWYGYYDET GEWVLVDEHY QNHQPRISEA PRFWEQLIGN EDYGYYEDNE WKWYDGEFDS EGNWLVFHSS NAEDAKNIDI AKDIPVFESF DVDSIDADEW LDQFSDSDAK EVFGED // ID PARE_MYCPN Reviewed; 635 AA. AC P78016; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00939}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00939}; DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00939}; GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00939}; GN OrderedLocusNames=MPN_122; ORFNames=MP032; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_00939}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; 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:0000255|HAMAP-Rule:MF_00939}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type CC 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00939}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95680.1; -; Genomic_DNA. DR PIR; S73358; S73358. DR RefSeq; NP_109810.1; NC_000912.1. DR RefSeq; WP_010874479.1; NC_000912.1. DR ProteinModelPortal; P78016; -. DR IntAct; P78016; 2. DR EnsemblBacteria; AAB95680; AAB95680; MPN_122. DR GeneID; 877280; -. DR KEGG; mpn:MPN122; -. DR PATRIC; 20021545; VBIMycPne110_0129. DR KO; K02622; -. DR OMA; PVGMHKL; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; MPNE272634:GJ6Z-129-MONOMER; -. DR Proteomes; UP000000808; 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_00939; ParE_type2; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005740; ParE_type2. 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; 1. DR TIGRFAMs; TIGR01058; parE_Gpos; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 635 DNA topoisomerase 4 subunit B. FT /FTId=PRO_0000145433. FT DOMAIN 422 537 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT NP_BIND 113 119 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 428 428 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 502 502 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 502 502 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT METAL 504 504 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT BINDING 5 5 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 45 45 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 72 72 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 340 340 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT SITE 453 453 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 456 456 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 509 509 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 621 621 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. SQ SEQUENCE 635 AA; 72413 MW; DA907DB744F4E0D6 CRC64; MKNNYSEANI KILKGLDAVK KRPGMYIGST DSRGFHHLLW EILDNCVDEV LSGFANTIAV VLHAENQITV SDNGRGIPFE THSDSKISTI DTVFTYLHAG GKFDNDSYKI AGGLHGVGAS VVNALSDQLQ VTVKRQGKVY RSVYENGGKI KQKAHCIGNA KIDEHGTSVT FRPDPKVFKK IHFDSELIRA RLKELAFLFK KLQLTFVDET GSGEKEVFFT EAGISQYLDE LNADSKQIAQ KIFVSGTEDD IELEAVFQFI DGEDEKLLSF ANSIRTSEGG SHEASFRQSV GDVINNYCRK YNFLKERDKN FEASEIREGL NGIIKVNLPE KIIAFEGQTK SKLFSKEVKA VVQKLTQKHF FQFLERNSVD AKLIVEKLFY NRKLRQELKQ QRQIKKNLSN PKAERILFGK LAPAQSKKVA ERELFVVEGD SAGGTAKMGR DRFLQAILPL RGKVLNVEKI NNKKEAINNE ELLTLIFCIG TGIGNNFTIR DRKYDKIIIM TDADNDGAHI QILLLTFFYR YMKPLIEKGH IYLALPPLYK FEGRDKKARY LWTEQELEQY RAKHSHFNVQ RYKGLGEMNA DQLWETTMNP MTRKLIQVKL DNFIQAEKQI NVFMGDKTEL RKSWIEANIN FSSEN // ID P69_MYCPN Reviewed; 542 AA. AC P75369; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=ABC transport system permease protein p69; GN Name=p69; OrderedLocusNames=MPN_417; ORFNames=MP423; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Probably part of a high-affinity transport system. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- DOMAIN: Composed of two homologous domains. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96071.1; -; Genomic_DNA. DR PIR; S73749; S73749. DR RefSeq; NP_110105.1; NC_000912.1. DR RefSeq; WP_010874773.1; NC_000912.1. DR ProteinModelPortal; P75369; -. DR EnsemblBacteria; AAB96071; AAB96071; MPN_417. DR GeneID; 877314; -. DR KEGG; mpn:MPN417; -. DR PATRIC; 20022230; VBIMycPne110_0452. DR KO; K02042; -. DR OMA; FESNIRW; -. DR OrthoDB; EOG6TR09N; -. DR BioCyc; MPNE272634:GJ6Z-446-MONOMER; -. DR Proteomes; UP000000808; 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 SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 542 ABC transport system permease protein FT p69. FT /FTId=PRO_0000060170. FT TRANSMEM 23 43 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 77 97 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 114 134 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 140 160 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 212 232 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 236 256 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 287 307 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 350 370 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 386 406 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 412 432 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 481 501 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 509 529 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 349 526 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 542 AA; 62474 MW; A6EA5C03464E2EA0 CRC64; MTSLFFYQIS DKQKRWNWYW KLALAIIVLV VIIYSFIDNF SGFNVSGFRN FSRNFIRLFT PDTARDYFLG SYLLQTIFYV VSGSILGFVI ALWFSYLTAF KIQPLYIALP TRLFTIFLRS FPVLVFAFLF NNLFNKQLTA TLTITWFSWL WSTKYITAFF ENSALKQFFN QSSRYIHKFK AFWNTVVISQ AERLWLFLLY SLEANFRWTT VLSIAGITGI GELIATPLGG TVQLNLVLIP MLTLIGFLLF LEASVFLLTK FVLQKQSQAG DYFLQAKTLQ KRKWKKVMIY ILALVLAAFT LANLVQLDYT VKAPGFVADF FKQFFQTKTA FLISEDANIN PLLMLLKLTT QAISLITLVF VLALLFGFLA SKLFSTITSI SLKLLLLVIR VIPSVLLFRL FDPIIFRPET TIIFVLAIHS AASYGQLITI NFDNANEGVI NNMQNHGFSR FYILWNYLIP TTKPQLLNTL SDSFDNAIRD LVVFGIFGGS IIGGRINNFF ERAQYSELGT ITLPLMVYLM VFEVILMAVR LNKLKVWQRH LW // ID PBDGT_MYCPN Reviewed; 341 AA. AC P75302; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Processive diacylglycerol beta-glycosyltransferase; DE EC=2.4.1.-; DE AltName: Full=Beta-monoglycosyldiacylglycerol synthase; DE Short=Beta-MGS; DE Short=MGlyDAG synthase; DE AltName: Full=Diglycosyldiacylglycerol synthase; DE Short=Beta-DGS; DE Short=DGlyDAG synthase; DE AltName: Full=Glycosyl-beta-1,6-galactosyldiacylglycerol synthase; DE AltName: Full=UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase; DE AltName: Full=UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase; GN OrderedLocusNames=MPN_483; ORFNames=MP359, P01_orf341; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND SUBSTRATE RP SPECIFICITY. RC STRAIN=ATCC 29342 / M129; RX PubMed=17697098; DOI=10.1111/j.1365-2958.2007.05865.x; RA Klement M.L., Ojemyr L., Tagscherer K.E., Widmalm G., Wieslander A.; RT "A processive lipid glycosyltransferase in the small human pathogen RT Mycoplasma pneumoniae: involvement in host immune response."; RL Mol. Microbiol. 65:1444-1457(2007). CC -!- FUNCTION: Processive glycosyltransferase involved in the CC biosynthesis of both the non-bilayer-prone beta- CC monoglycosyldiacylglycerol and the bilayer-forming membrane lipid CC glucosyl-galactosyldiacylglycerol and digalactosyl-diacylglycerol. CC These components contribute to regulate the properties and CC stability of the membrane. Catalyzes sequentially the transfers of CC glucosyl or galactosyl residues from UDP-Glc or UDP-Gal to CC diacylglycerol (DAG) acceptor to form the corresponding beta- CC glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-diacyl-sn-glycerol). CC Then, only beta-galactosyl-DAG (3-O-(beta-D-galactopyranosyl)-1,2- CC diacyl-sn-glycerol) can act as acceptor to give the beta-glycosyl- CC beta-galactosyl-DAG product (3-O-(beta-D-glycopyranosyl-(1->6)-D- CC galactopyranosyl)-1,2-diacyl-sn-glycerol). It can also use alpha- CC Gal-beta-Gal-DAG, ceramide (Cer) and beta-Gal-Cer as sugar CC acceptors. The enzyme is supposed to be mainly a CC galactosyltransferase, with higher glycosyltransferase activity CC for the addition of the second glycosyl on beta-Gal-DAG as CC acceptor. The main glycolipid produced in vivo is beta-Glc-beta- CC Gal-DAG with a beta-1,6 linkage. {ECO:0000269|PubMed:17697098}. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + CC 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:17697098}. CC -!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + CC 1,2-diacyl-3-O-(beta-D-galactopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:17697098}. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-3-O-(beta-D- CC galactopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D- CC glucopyranosyl-(1->6)-O-beta-D-galactopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:17697098}. CC -!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-3-O-(beta-D- CC galactopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D- CC galactopyranosyl-(1->6)-O-beta-D-galactopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:17697098}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Activated by the negatively charged lipid CC phosphatidylglycerol (PG). {ECO:0000269|PubMed:17697098}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. CC -!- MISCELLANEOUS: The local lipid environment around the enzyme CC affects both the extent of head group elongation and total amounts CC of glycolipids produced. {ECO:0000305|PubMed:17697098}. CC -!- MISCELLANEOUS: Glycolipids such as beta-Gal-DAG, alpha-Gal-beta- CC Gal-DAG, beta-Glc-beta-Gal-DAG and beta-Gal-Cer are highly CC immunogenic and are reactive towards IgM antibodies. Glycolipids CC with a terminal beta-Gal are more reactive than the ones with a CC beta-Glc residue (PubMed:17697098). {ECO:0000305|PubMed:17697098}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; U00089; AAB96007.1; -; Genomic_DNA. DR PIR; S73685; S73685. DR RefSeq; NP_110171.1; NC_000912.1. DR RefSeq; WP_010874839.1; NC_000912.1. DR ProteinModelPortal; P75302; -. DR IntAct; P75302; 3. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB96007; AAB96007; MPN_483. DR GeneID; 876759; -. DR KEGG; mpn:MPN483; -. DR PATRIC; 20022390; VBIMycPne110_0522. DR KO; K19004; -. DR OMA; NVIKYFV; -. DR OrthoDB; EOG6WQD5X; -. DR BioCyc; MPNE272634:GJ6Z-524-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB. 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 1: Evidence at protein level; KW Carbohydrate metabolism; Cell membrane; Complete proteome; KW Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Membrane; Reference proteome; KW Transferase. FT CHAIN 1 341 Processive diacylglycerol beta- FT glycosyltransferase. FT /FTId=PRO_0000059246. SQ SEQUENCE 341 AA; 40415 MW; C209F50D714CB3D0 CRC64; MNKLISILVP CYQSQPFLDR FFKSLLKQDW NGVKVIFFND NKPDPTYEIL KQFQQAHPQL AIEVHCGEKN VGVGGSRDQL INYVDTPYFY FVDPDDEFSD PNCFKAIVET IQGENFDIAV LNSIVYLQML KNDFLIKHIP LKNIFQGKVK LNPDNTVNHL HYIQNNDQYI WNIVINTAFF KALDLQFVNR FIEDIAVWFP IMFKAQKVLW IDVNGVNYYL RPNSASTQKN SIKLLSFIEA YERLYFHLKK VGKLADFIDP NNKIESRFWR RQAFIWFSFI NVSWMKAEFE QTKSVLQKLF DFMEANGIYD RVFTNKHHGI YLLWVNRLKH FKKLVQAQPH L // ID P30_MYCPN Reviewed; 274 AA. AC P75330; P94960; Q50282; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=P30 adhesin; DE AltName: Full=30 kDa adhesin-related protein; DE AltName: Full=Cytadhesin P30; GN Name=p30; OrderedLocusNames=MPN_453; ORFNames=MP388; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=2123834; RA Dallo S.F., Chavoya A., Baseman J.B.; RT "Characterization of the gene for a 30-kilodalton adhesion-related RT protein of Mycoplasma pneumoniae."; RL Infect. Immun. 58:4163-4165(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 mutant M6; RX PubMed=7836325; RA Layh-Schmitt G., Hilbert H., Pirkl E.; RT "A spontaneous hemadsorption-negative mutant of Mycoplasma pneumoniae RT exhibits a truncated adhesin-related 30-kilodalton protein and lacks RT the cytadherence-accessory protein HMW1."; RL J. Bacteriol. 177:843-846(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 mutant M7; RA Layh-Schmitt G., Himmelreich R., Leibfried U.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adhesin necessary for successful cytadherence and CC virulence. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane; Multi-pass membrane protein. Note=Integral and surface CC exposed membrane protein that localizes to the membrane at the CC attachment organelle. CC -!- DOMAIN: 13 hexapeptides with consensus sequence were found at the CC carboxy end between AA 177 and 267 in a proline-rich domain. CC -!- MISCELLANEOUS: Spontaneous hemadsorption-negative mutants M6 and CC M7 exhibit a truncated P30 adhesin. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57245; AAB36603.1; -; Genomic_DNA. DR EMBL; U00089; AAB96036.1; -; Genomic_DNA. DR EMBL; Z46228; CAB56613.1; -; Genomic_DNA. DR EMBL; U30326; AAC45467.1; -; Genomic_DNA. DR PIR; A41461; A41461. DR RefSeq; NP_110141.1; NC_000912.1. DR RefSeq; WP_010874809.1; NC_000912.1. DR ProteinModelPortal; P75330; -. DR EnsemblBacteria; AAB96036; AAB96036; MPN_453. DR GeneID; 877126; -. DR KEGG; mpn:MPN453; -. DR PATRIC; 20022304; VBIMycPne110_0489. DR OMA; PNMQQRP; -. DR OrthoDB; EOG6X3WGQ; -. DR BioCyc; MPNE272634:GJ6Z-482-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. 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:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR009896; Cytadhesin_P30. DR Pfam; PF07271; Cytadhesin_P30; 1. PE 4: Predicted; KW Cell adhesion; Cell membrane; Cell projection; Complete proteome; KW Cytadherence; Lipoprotein; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Virulence. FT CHAIN 1 274 P30 adhesin. FT /FTId=PRO_0000058130. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT REPEAT 177 182 1-1. FT REPEAT 183 188 2-1. FT REPEAT 189 194 1-2. FT REPEAT 195 200 3-1. FT REPEAT 201 206 1-3. FT REPEAT 207 212 2-2. FT REPEAT 213 218 1-4. FT REPEAT 219 224 3-2. FT REPEAT 225 230 1-5. FT REPEAT 231 236 2-3. FT REPEAT 237 242 1-6. FT REPEAT 243 248 3-3. FT REPEAT 249 254 1-7. FT REPEAT 268 273 3-4. FT REGION 177 254 7 X 6 AA repeats of P-G-M-A-P-R. FT REGION 183 236 3 X 6 AA repeats of P-G-M-P-P-H. FT REGION 195 248 4 X 6 AA repeats of P-G-F-P-P-Q. FT VARIANT 186 257 Missing (in strain: mutant M7). FT VARIANT 210 257 Missing (in strain: mutant M6). FT CONFLICT 80 80 G -> V (in Ref. 1; AAB36603). FT {ECO:0000305}. SQ SEQUENCE 274 AA; 29741 MW; BFB047831A4C9D7D CRC64; MKLPPRRKLK LFLLAWMLVL FSALIVLATL ILVQHNNTEL TEVKSELSPL NVVLHAEEDT VQIQGKPITE QAWFIPTVAG CFGFSALAII LGLAIGLPIV KRKEKRLLEE KERQEQLAEQ LQRISAQQEE QQALEQQAAA EAHAEAEVEP APQPVPVPPQ PQVQINFGPR TGFPPQPGMA PRPGMPPHPG MAPRPGFPPQ PGMAPRPGMP PHPGMAPRPG FPPQPGMAPR PGMPPHPGMA PRPGFPPQPG MAPRPGMQPP RPGMPPQPGF PPKR // ID PEPF_MYCPN Reviewed; 611 AA. AC P54125; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Oligoendopeptidase F homolog; DE EC=3.4.24.-; GN Name=pepF; OrderedLocusNames=MPN_197; ORFNames=MP634; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M3B 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; U34795; AAC43684.1; -; Genomic_DNA. DR EMBL; U00089; AAB96282.1; -; Genomic_DNA. DR PIR; S62811; S62811. DR RefSeq; NP_109885.1; NC_000912.1. DR RefSeq; WP_010874554.1; NC_000912.1. DR ProteinModelPortal; P54125; -. DR MEROPS; M03.007; -. DR EnsemblBacteria; AAB96282; AAB96282; MPN_197. DR GeneID; 876899; -. DR KEGG; mpn:MPN197; -. DR PATRIC; 20021717; VBIMycPne110_0215. DR KO; K08602; -. DR OMA; KEKWDLT; -. DR OrthoDB; EOG6CCH1Q; -. DR BioCyc; MPNE272634:GJ6Z-204-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR InterPro; IPR013647; OligopepF_N_dom. DR InterPro; IPR001567; Pept_M3A_M3B. DR InterPro; IPR004438; Peptidase_M3B. DR Pfam; PF01432; Peptidase_M3; 1. DR Pfam; PF08439; Peptidase_M3_N; 1. DR TIGRFAMs; TIGR00181; pepF; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1 611 Oligoendopeptidase F homolog. FT /FTId=PRO_0000078168. FT ACT_SITE 385 385 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 384 384 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 388 388 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 391 391 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 611 AA; 70959 MW; 8DB896D570BB215D CRC64; MNNQYNWNLE VLLNGKSLAD NFTELKQLSE QEKALYDGGA CFQTKAKFTE FLQLQEKIEV LENRYSNFLS NKHAENSLDK TINDALFQYE MFKSEHALVF VDFEKNLFKH EKVIRAYLQD PALKQYQRDF ELVWRNKKHQ IDPASQKLLA QISPAWNQAD KIFNVLSTAD LNLQPVVYKG KTYVINAVSD YQSLLENKDR GLREAAYKVW LEIYWPTRNT LSVSLVENYI QLETFAKLKK HPNYIAKTAF DDEIDVAFID FVYEQVASFA PTFKAFQSLR KQIYKHVLKL DKAQPWDLSV PLFKASGDYT IEQAQTDALK ILAPMGSEYL EVVKEAFRER WISWLPDKNK YTGAYSISNV KGLDHYFILM NFDKTRASLN TLVHELGHSV HSWYASKYQT QNLDPTIFYA EIASICNELL LCYHDIINYE NRNPQQLIRS LMEQISHFFG ATTRQLMFSQ FEQDTLKLIQ QNQKPDFKTL VEIYGKTAIK YQAANADAIT KKLKQTKYQK SLAYITSIPH FYAGNFYVYK YAIGQVVGTL VGKKLSAGDS NMLAAYKRFL SSGSTLPPLE TIKLLGIDLT QPEPWQEAHA ELKRWIKLVQ TAFKQLQHKK R // ID PARA_MYCPN Reviewed; 270 AA. AC Q50314; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=ParA family protein MPN_688; GN OrderedLocusNames=MPN_688; ORFNames=MP154; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ParA 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; U34816; AAC43646.1; -; Genomic_DNA. DR EMBL; U00089; AAB95802.1; -; Genomic_DNA. DR PIR; S62837; S62837. DR RefSeq; NP_110377.1; NC_000912.1. DR RefSeq; WP_010875045.1; NC_000912.1. DR ProteinModelPortal; Q50314; -. DR EnsemblBacteria; AAB95802; AAB95802; MPN_688. DR GeneID; 877040; -. DR KEGG; mpn:MPN688; -. DR PATRIC; 20022865; VBIMycPne110_0755. DR KO; K03496; -. DR OMA; TFRERNE; -. DR OrthoDB; EOG6D8BCX; -. DR BioCyc; MPNE272634:GJ6Z-734-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025669; AAA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13614; AAA_31; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 270 ParA family protein MPN_688. FT /FTId=PRO_0000201987. SQ SEQUENCE 270 AA; 30081 MW; B7B3FA5C810F93F3 CRC64; MIISFVNNKG GVLKTTMATN VAGSLVKLCP EQRKVILDLD GQGNVSASFG QNPERLNNTL IDILLKVPKF NGANSSIEID DCLLPVYEGL DILPCNFELN FADIDIARKK YKASDIAEIV KQLTRRYDFV LLDTPPNMAT LVSTAMSLSD VIVIPFEPDQ YSMLGLMRIV ETIDTFKEKN PNLKTILVPT KVNMRTRLHN DVIELVKSKA HKNNVAFSEH FVSLTSKSSA AVGYEKLPIS LVSPTSNKKY QTEYLEITKE ILNLVNHGHQ // ID PIP_MYCPN Reviewed; 309 AA. AC P75092; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Putative proline iminopeptidase; DE Short=PIP; DE EC=3.4.11.5; DE AltName: Full=Prolyl aminopeptidase; DE Short=PAP; GN Name=pip; OrderedLocusNames=MPN_022; ORFNames=MP132; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline CC residues from peptides. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95780.1; -; Genomic_DNA. DR PIR; S73458; S73458. DR RefSeq; NP_109710.1; NC_000912.1. DR RefSeq; WP_010874379.1; NC_000912.1. DR ProteinModelPortal; P75092; -. DR IntAct; P75092; 4. DR ESTHER; mycpn-pip; Proline_iminopeptidase. DR MEROPS; S33.001; -. DR EnsemblBacteria; AAB95780; AAB95780; MPN_022. DR GeneID; 876978; -. DR KEGG; mpn:MPN022; -. DR PATRIC; 20021319; VBIMycPne110_0021. DR KO; K01259; -. DR OMA; VSEMFPD; -. DR OrthoDB; EOG6BPDDC; -. DR BioCyc; MPNE272634:GJ6Z-24-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR InterPro; IPR005944; Pro_iminopeptidase. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF006431; Pept_S33; 1. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 309 Putative proline iminopeptidase. FT /FTId=PRO_0000080840. FT ACT_SITE 105 105 Nucleophile. {ECO:0000250}. FT ACT_SITE 262 262 {ECO:0000250}. FT ACT_SITE 290 290 Proton donor. {ECO:0000250}. SQ SEQUENCE 309 AA; 34690 MW; 6E414919FC01E767 CRC64; MNTSPKQSGY LKVGNGHEVY FWTAGNPQGK SALYVHGGPG SGTDAGCLKY FDLDTTYVIL LDQRGCGQSK AVNPLLHNTT QDLVGDLEAL RQHLKLERWT LFGGSWGSTL ALVYAITHPQ VVEQVFLRAL FLGREQDWAE MLLGLGKLFY PYEHQTLLKA IPQACRTDFT KFTNYFYEVL QGNDSALKTQ LANAWVKWEN TLLSPISYVK DEKAEDANFT FKLALLECHY AKHHSFLKPN FILENVAVLK DKPVHLIHGR FDLVCPLSQA LELKRALPTL NLYVTNNAGH SGSDPNNLTT IKHLLKTQL // ID PGK_MYCPN Reviewed; 409 AA. AC P78018; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=MPN_429; ORFNames=MP412; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96060.1; -; Genomic_DNA. DR PIR; S73738; S73738. DR RefSeq; NP_110117.1; NC_000912.1. DR RefSeq; WP_010874785.1; NC_000912.1. DR ProteinModelPortal; P78018; -. DR IntAct; P78018; 2. DR EnsemblBacteria; AAB96060; AAB96060; MPN_429. DR GeneID; 876849; -. DR KEGG; mpn:MPN429; -. DR PATRIC; 20022254; VBIMycPne110_0464. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR OrthoDB; EOG64N9Z0; -. DR BioCyc; MetaCyc:MONOMER-549; -. DR BioCyc; MPNE272634:GJ6Z-458-MONOMER; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000808; 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 1 409 Phosphoglycerate kinase. FT /FTId=PRO_0000145971. FT NP_BIND 365 368 ATP. {ECO:0000250}. FT REGION 22 24 Substrate binding. {ECO:0000250}. FT REGION 60 63 Substrate binding. {ECO:0000250}. FT BINDING 37 37 Substrate. {ECO:0000250}. FT BINDING 122 122 Substrate. {ECO:0000250}. FT BINDING 164 164 Substrate. {ECO:0000250}. FT BINDING 215 215 ATP. {ECO:0000250}. FT BINDING 338 338 ATP. {ECO:0000250}. SQ SEQUENCE 409 AA; 44212 MW; 6AF230188D398731 CRC64; MVDFKTVQAF DFQGKTVVLR ADLNVPMKDG VITDNERILA SLDTIKYLLG HNCKIVLLSH LSRVKSLDDK KGKKSLQPVA SALQNLLKNT KVHFCPENTG DKVKVAVNQL PLGEILVLEN TRYCDVNEAG EVVKHESKNN AELAQFWASL GDIFVNDAFG TAHRRHASNA GIAKYIKNSC IGLLMERELI NLYRLINNPP KPFVVVLGGA KVSDKLQVVN NLFKIADHIL IGGGMVNTFL KALGNEVGTS LVEEDLVQTA KQILDSDKDK KIVLGVDQML HASFKDEPGV ECVVAPQWPA ELQGFMSLDV GSKTVALFSS YLAKAKTIFW NGPMGVFEFS NYAQGTLAIG KAIAQNQQAF SVIGGGDSAA AAKQLQIADQ FSFISTGGGA SLALIGGEEL VGISDIQKK // ID PGSA_MYCPN Reviewed; 227 AA. AC P75520; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; DE EC=2.7.8.5; DE AltName: Full=Phosphatidylglycerophosphate synthase; DE Short=PGP synthase; GN Name=pgsA; OrderedLocusNames=MPN_253; ORFNames=MP579; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: This protein catalyzes the committed step to the CC synthesis of the acidic phospholipids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CDP-diacylglycerol + sn-glycerol 3-phosphate = CC CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol CC biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step CC 1/2. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96227.1; -; Genomic_DNA. DR PIR; S73905; S73905. DR RefSeq; NP_109941.1; NC_000912.1. DR RefSeq; WP_010874610.1; NC_000912.1. DR IntAct; P75520; 1. DR EnsemblBacteria; AAB96227; AAB96227; MPN_253. DR GeneID; 876733; -. DR KEGG; mpn:MPN253; -. DR PATRIC; 20021831; VBIMycPne110_0272. DR KO; K00995; -. DR OMA; LWITILF; -. DR OrthoDB; EOG6WMJ3D; -. DR BioCyc; MPNE272634:GJ6Z-260-MONOMER; -. DR UniPathway; UPA00084; UER00503. DR Proteomes; UP000000808; 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:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. 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 Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 227 CDP-diacylglycerol--glycerol-3-phosphate FT 3-phosphatidyltransferase. FT /FTId=PRO_0000056778. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. SQ SEQUENCE 227 AA; 26050 MW; 76192D444013B6D4 CRC64; MRSPFPVPMV PLTIKTWQKK LPNWLTIYRI FIAVPTIIFL GLNHLLGSVA SFTVLGNVTI HLQVSLFIGG VLFITAVISD YLDGYWARKW RVVSNFGKLW DPLADKVIIN GVLIALVAYG YFHFSFLIVI VLRDLVLDGL RFYAQEKQLI IPANQWGKWK TTWQMIAILM SCFVFSFSLK ETNSANTKIF YWAIVHLPYY LATAFSLVSF GIYAQQIYKT IKVKVKL // ID PFKA_MYCPN Reviewed; 328 AA. AC P75476; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 102. DE RecName: Full=Probable ATP-dependent 6-phosphofructokinase; DE Short=ATP-PFK; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; Synonyms=pfk; OrderedLocusNames=MPN_302; ORFNames=MP534; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate CC to fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000250|UniProtKB:P0A796}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000250|UniProtKB:P0A796}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0A796}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) 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; U00089; AAB96182.1; -; Genomic_DNA. DR PIR; S73860; S73860. DR RefSeq; NP_109990.1; NC_000912.1. DR RefSeq; WP_010874659.1; NC_000912.1. DR ProteinModelPortal; P75476; -. DR IntAct; P75476; 2. DR EnsemblBacteria; AAB96182; AAB96182; MPN_302. DR GeneID; 877241; -. DR KEGG; mpn:MPN302; -. DR PATRIC; 20021939; VBIMycPne110_0326. DR KO; K00850; -. DR OMA; LAFRMGS; -. DR OrthoDB; EOG644ZRM; -. DR BioCyc; MetaCyc:MONOMER-545; -. DR BioCyc; MPNE272634:GJ6Z-309-MONOMER; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase 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 GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR000023; Phosphofructokinase_dom. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 328 Probable ATP-dependent 6- FT phosphofructokinase. FT /FTId=PRO_0000111965. FT NP_BIND 77 78 ATP. {ECO:0000250|UniProtKB:P0A796}. FT NP_BIND 107 110 ATP. {ECO:0000250|UniProtKB:P0A796}. FT REGION 130 132 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT REGION 174 176 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT REGION 258 261 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT ACT_SITE 132 132 Proton acceptor. FT {ECO:0000250|UniProtKB:P0A796}. FT METAL 108 108 Magnesium; catalytic. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 16 16 ATP; via amide nitrogen. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 167 167 Substrate; shared with dimeric partner. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 226 226 Substrate. FT {ECO:0000250|UniProtKB:P0A796}. SQ SEQUENCE 328 AA; 35989 MW; E29C9F0536766321 CRC64; MSPKTTKKIA ILTSGGDAPG MNATLVYLTR YATSSEIEVF FVKNGYYGLY HDELVPAHQL DLSNSLFSAG TVIGSKRFVE FKELKVREQA AQNLKKRQID YLVVIGGDGS YMGAKLLSEL GVNCYCLPGT IDNDINSSEF TIGFLTALES IKVNVQAVYH TTKSHERVAI VEVMGRHCGD LAIFGALATN ADFVVTPSNK MDLKQLESAV KKILQHQNHC VVIVSENIYG FDGYPSLTAI KQHFDANNMK CNLVSLGHTQ RGFAPTSLEL VQISLMAQHT INLIGQNKVN QVIGNKANVP VNYDFDQAFN MPPVDRSALI AVINKNII // ID PLSX_MYCPN Reviewed; 328 AA. AC P75232; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. 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=MPN_546; ORFNames=MP296; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95944.1; -; Genomic_DNA. DR PIR; S73622; S73622. DR RefSeq; NP_110235.1; NC_000912.1. DR RefSeq; WP_010874903.1; NC_000912.1. DR ProteinModelPortal; P75232; -. DR EnsemblBacteria; AAB95944; AAB95944; MPN_546. DR GeneID; 877252; -. DR KEGG; mpn:MPN546; -. DR PATRIC; 20022569; VBIMycPne110_0608. DR KO; K03621; -. DR OMA; VPSDVKN; -. DR OrthoDB; EOG68H88P; -. DR BioCyc; MPNE272634:GJ6Z-591-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000808; 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 1 328 Phosphate acyltransferase. FT /FTId=PRO_0000189909. SQ SEQUENCE 328 AA; 36664 MW; 2BACE0DD9ADE32E7 CRC64; MAFRLAVDCL GFENHPREAI DAVLEYWSYH QELEFILVGD EKTFDGLDYL PKNITKQLAS SCIDMTDTPL TARRKVNNSM QKAINLVRDG AADVVISAGS SAVYASLTYD GFGKIHKDVK SAFMSYVPTA NNDWFYFLDV GANKNFTGKE LYFLGLMADI FVKKTTNKIS PRIALLNIGT EIHKGFDYHQ EGYQLLNEDK HLNFTGFIEP RFLLDGVCDI LVADGYSGNL VLKSMEGTFK TIARLLKQGY KRNPLAGLFS LGILKRIAKR FDYKNNAGAV VIGLNKLALK THGSADKQQF LSTIRLAHTS LKSDLINAIK SSLDNYEK // ID PLSY_MYCPN Reviewed; 239 AA. AC P75428; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 97. 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=MPN_350; ORFNames=MP486; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 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; U00089; AAB96134.1; -; Genomic_DNA. DR PIR; S73812; S73812. DR RefSeq; NP_110038.1; NC_000912.1. DR RefSeq; WP_010874706.1; NC_000912.1. DR ProteinModelPortal; P75428; -. DR IntAct; P75428; 2. DR EnsemblBacteria; AAB96134; AAB96134; MPN_350. DR GeneID; 876931; -. DR KEGG; mpn:MPN350; -. DR PATRIC; 20022060; VBIMycPne110_0377. DR KO; K08591; -. DR OMA; HSQYPKI; -. DR OrthoDB; EOG6M6JSX; -. DR BioCyc; MPNE272634:GJ6Z-367-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000808; 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 membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 239 Glycerol-3-phosphate acyltransferase. FT /FTId=PRO_0000188406. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 99 119 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 135 155 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 239 AA; 27439 MW; 6D4110A8253C9EBB CRC64; MNAASAIALL IVFSLVIGYL MGSVMFADVF GKILNKDVRK LGSKNPGATN SIRVFGLKIG FLVGLCDALK GFLAFVFSFL IFSFWLQQYL NVNQYQKVYY LTYLSCFAAT IGHIFPLYFK FKGGKAIATT GGSLLAISLW WFVICLVLWL LVTLITKYVS LASLVTFFIL AIIILVPWLD YLYFFKPNPI NAISYQNDWY IILFFVLWYW PLTIAVFWLH RKNIHRLLNK TENKVTQLN // ID PKNS_MYCPN Reviewed; 389 AA. AC P75524; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Putative serine/threonine-protein kinase; DE EC=2.7.11.1; GN OrderedLocusNames=MPN_248; ORFNames=MP584; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96232.1; -; Genomic_DNA. DR PIR; S73910; S73910. DR RefSeq; NP_109936.1; NC_000912.1. DR RefSeq; WP_010874605.1; NC_000912.1. DR ProteinModelPortal; P75524; -. DR IntAct; P75524; 1. DR EnsemblBacteria; AAB96232; AAB96232; MPN_248. DR GeneID; 876966; -. DR KEGG; mpn:MPN248; -. DR PATRIC; 20021821; VBIMycPne110_0267. DR KO; K08884; -. DR OMA; PGRDVNE; -. DR OrthoDB; EOG62NX1C; -. DR BioCyc; MPNE272634:GJ6Z-255-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 389 Putative serine/threonine-protein kinase. FT /FTId=PRO_0000171202. FT DOMAIN 15 356 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 164 164 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. SQ SEQUENCE 389 AA; 44882 MW; 838E5CDB5AD49B15 CRC64; MALNLKIGDI VQNKYRIEKL INRGGMNSYL FLASNLHVQE FGPLQKRQFT RLVLKVVQRT DKINDNNWKK FLDGTITTTR VSHKNLVQTF DVVSPRLSVL SENQVIVLED TVMIVMEYVD GPSLREMLNQ KGYFSVQEVV YYFTKLVKVI NYLHSFEHQI IHRDLKPENI LFTSNLTDIK LLDFGIASAV IRNAEKTEVL TDENSLFGTV SYMTPEVLES TVNKEGKRIR KPPTVQYDIY SLGVILFEML VGRVPFNKSI DPKKERETIQ KARNFDVPLM GNLRSDVPVS LENIVFKCTA VKRENSKWMY SDTKQLLADL AQWQTEQTLI KPVHERILEG QNEMRELMVS NYLPWYLRKG VLIFFSVVLL ALLIAVVSFF IITGVVVHS // ID PLSC_MYCPN Reviewed; 266 AA. AC P75479; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase; DE Short=1-AGP acyltransferase; DE Short=1-AGPAT; DE EC=2.3.1.51; DE AltName: Full=Lysophosphatidic acid acyltransferase; DE Short=LPAAT; GN Name=plsC; OrderedLocusNames=MPN_299; ORFNames=MP537; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic CC acid by incorporating acyl moiety at the 2 position. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity CC and may constitute the binding site for the phosphate moiety of CC the glycerol-3-phosphate. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96185.1; -; Genomic_DNA. DR PIR; S73863; S73863. DR RefSeq; NP_109987.1; NC_000912.1. DR RefSeq; WP_010874656.1; NC_000912.1. DR ProteinModelPortal; P75479; -. DR EnsemblBacteria; AAB96185; AAB96185; MPN_299. DR GeneID; 877232; -. DR KEGG; mpn:MPN299; -. DR PATRIC; 20021933; VBIMycPne110_0323. DR KO; K00655; -. DR OMA; KVAYNAF; -. DR OrthoDB; EOG6ZWJDH; -. DR BioCyc; MPNE272634:GJ6Z-306-MONOMER; -. DR UniPathway; UPA00557; UER00613. DR Proteomes; UP000000808; 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:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR004552; AGP_acyltrans. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 266 Probable 1-acyl-sn-glycerol-3-phosphate FT acyltransferase. FT /FTId=PRO_0000208173. FT MOTIF 92 97 HXXXXD motif. SQ SEQUENCE 266 AA; 30414 MW; 79D933AD8203927F CRC64; MKKLTQAFLR FCLRFLQLLS LVLVLPVFVL MLISSLISAK NYESIPENYP PEIRFKKVYR LVSLFLYIKG VKVVIVNPEN VPKKAVLVVA NHKSNLDPLI LIKAFGKTEG VPPLTFIAKI ELQDTWLFKI MKLIDCVFID RKNLRQMAAS LEQQQQIIRQ GTALCVFPEG TRVLSRQIGE FKSGALKVAY NAFVPIVPLT IVGSMGHMES KKRLQKAQVE RDRGYKIQVI FNTPINPINF NQIDSQNVAN NVWREISQTY AQYCQD // ID POTA_MYCPN Reviewed; 560 AA. AC P75059; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726}; DE EC=3.6.3.31 {ECO:0000255|HAMAP-Rule:MF_01726}; GN Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; GN OrderedLocusNames=MPN_055; ORFNames=MP099; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_01726}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + polyamine(Out) = ADP + phosphate CC + polyamine(In). {ECO:0000255|HAMAP-Rule:MF_01726}. 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:0000255|HAMAP-Rule:MF_01726}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01726}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Spermidine/putrescine importer (TC 3.A.1.11.1) family. CC {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95747.1; -; Genomic_DNA. DR PIR; S73425; S73425. DR RefSeq; NP_109743.1; NC_000912.1. DR RefSeq; WP_010874412.1; NC_000912.1. DR ProteinModelPortal; P75059; -. DR SMR; P75059; 29-65. DR EnsemblBacteria; AAB95747; AAB95747; MPN_055. DR GeneID; 876902; -. DR KEGG; mpn:MPN055; -. DR PATRIC; 20021387; VBIMycPne110_0055. DR KO; K11072; -. DR OMA; RQKMQVL; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-57-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015594; F:putrescine-importing ATPase activity; IEA:InterPro. DR GO; GO:0015595; F:spermidine-importing ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR017879; ABC_Sperm/Put_ATP-bd_PotA. 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 Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51305; POTA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 560 Spermidine/putrescine import ATP-binding FT protein PotA. FT /FTId=PRO_0000092751. FT DOMAIN 7 449 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01726}. FT NP_BIND 40 47 ATP. {ECO:0000255|HAMAP-Rule:MF_01726}. FT REGION 108 318 Insert. SQ SEQUENCE 560 AA; 65131 MW; 8993CAE61A28723D CRC64; MNERFLIEIE GLNKTFDDGF VSVRDINLKI KKGEFITILG PSGCGKTTTL RLLAGFEDPT YGKIKVNGLD IKDLPIHKRP FATVFQDYAL FSHLTVYKNI AYGLKAMYTK LDPIDKLVEQ YHQSLLDKQH RLHKRIERLE KSNANPQLLE QLKQTVVVQQ KQFKQQTETF KQKENARRDA IQQRLVQLTK EWESLSKQKL QQLEAEKKLL DKKFEQTERK YQKDAWMATH SEMRLKQFKQ EVLALKQLIK TKFKQNEPVD KLQLKLQTLK QKYAAKRQID KEYDKLVLAY NKKDYWTSYW ETYSLQQQEA FEKRYLSRKL TKQEQHQKVC AVIELVGLKG NEDKLPEELS GGMKQRVALA RSLVIEPDIL LLDEPLSALD AKVRKNLQKE LQKIHQQSGL TFILVTHDQE EALVLSNRIV VMNEGNILQV GSPADIYDSP KTEWIANFIG QANIFKGTYL GDLKIKLHSG EVIKTDVDNN YVVGKEYKIL IRPEDFDIVP KNKGFFNVRV IDKTYKGLLW KITTKLVDDT IVDLESVNDI EVDKTFGVTF DPIDVHLMEV // ID PPH_MYCPN Reviewed; 259 AA. AC P75525; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Putative protein phosphatase; DE EC=3.1.3.16; GN OrderedLocusNames=MPN_247; ORFNames=MP585; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O CC = [a protein]-serine/threonine + phosphate. CC -!- SIMILARITY: Contains 1 PPM-type phosphatase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01082}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96233.1; -; Genomic_DNA. DR PIR; S73911; S73911. DR RefSeq; NP_109935.1; NC_000912.1. DR RefSeq; WP_010874604.1; NC_000912.1. DR ProteinModelPortal; P75525; -. DR IntAct; P75525; 3. DR EnsemblBacteria; AAB96233; AAB96233; MPN_247. DR GeneID; 876954; -. DR KEGG; mpn:MPN247; -. DR PATRIC; 20021819; VBIMycPne110_0266. DR KO; K01090; -. DR OMA; VREENQD; -. DR OrthoDB; EOG65N17S; -. DR BioCyc; MPNE272634:GJ6Z-254-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR Gene3D; 3.60.40.10; -; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR PANTHER; PTHR13832; PTHR13832; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; SSF81606; 1. DR PROSITE; PS51746; PPM_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protein phosphatase; Reference proteome. FT CHAIN 1 259 Putative protein phosphatase. FT /FTId=PRO_0000057796. FT DOMAIN 8 255 PPM-type phosphatase. FT {ECO:0000255|PROSITE-ProRule:PRU01082}. SQ SEQUENCE 259 AA; 29689 MW; 4EE599CD210A66D8 CRC64; MDSTNQNLFA SLSKKGPVRK ENQDFSVVTF NRFGQLMSLV CDGLGGYKGG KMASALVSEV FTKSFTVFDF HSQTERAVKQ WFEITLIEAR RTLEQYFQTI KRNQVQFARM ATTLVLSIIS KQNIWTFWVG DSRAYLINSY QSLQITEDHN LYNQLLQMHA TPDVIASYKD KLLALTATVS KDQERQLKYS FRCDVVNAWD FLLLCSDGLY NFLDPNCFYE VITSAPNLKK AVTQLAKLSL DNASNDNITL NLINLKQWH // ID POTB_MYCPN Reviewed; 286 AA. AC P75058; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Spermidine/putrescine transport system permease protein PotB homolog; GN Name=potB; OrderedLocusNames=MPN_056; ORFNames=MP098; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for the activity of the bacterial transport CC system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95746.1; -; Genomic_DNA. DR PIR; S73424; S73424. DR RefSeq; NP_109744.1; NC_000912.1. DR RefSeq; WP_010874413.1; NC_000912.1. DR ProteinModelPortal; P75058; -. DR EnsemblBacteria; AAB95746; AAB95746; MPN_056. DR GeneID; 877403; -. DR KEGG; mpn:MPN056; -. DR PATRIC; 20021389; VBIMycPne110_0056. DR KO; K11071; -. DR OMA; QNSEFIN; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MPNE272634:GJ6Z-58-MONOMER; -. DR Proteomes; UP000000808; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 286 Spermidine/putrescine transport system FT permease protein PotB homolog. FT /FTId=PRO_0000060180. FT TRANSMEM 10 30 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 62 82 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 94 114 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 193 213 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 248 268 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 58 264 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 286 AA; 31936 MW; 04313B3A07384CDB CRC64; MKLSKKYLLA VPFFVLMVIF FVVPMAWIIV SGLQNENGAS ITEKYQPLVG GYSFFQSFWT SLWTATVTVL VALLVAFPFC YFLSQSKNKV FRSFVIALAT APIWSSFLIK LIGLKTLLDL VLGLALNRVG DNNLTFGSGY TLIGMIYLFT PFMFLPLYNN FCILPKNLIL ASQDLGYNWI TSFIKVVIPF SKTAILSGIA LTFFPSLTSV AIAQFLDNSN QNNTLGNYVF TLGNNGYDSA IERGRASGAI IIAALITFAF YFVVIFAPRI VRLIQTKCLK YRRVNV // ID POTC_MYCPN Reviewed; 286 AA. AC P75057; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Spermidine/putrescine transport system permease protein PotC homolog; GN Name=potC; OrderedLocusNames=MPN_057; ORFNames=MP097; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for the activity of the bacterial transport CC system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95745.1; -; Genomic_DNA. DR PIR; S73423; S73423. DR RefSeq; NP_109745.1; NC_000912.1. DR RefSeq; WP_010874414.1; NC_000912.1. DR ProteinModelPortal; P75057; -. DR EnsemblBacteria; AAB95745; AAB95745; MPN_057. DR GeneID; 876934; -. DR KEGG; mpn:MPN057; -. DR PATRIC; 20021391; VBIMycPne110_0057. DR KO; K11070; -. DR OMA; LIERIWY; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MPNE272634:GJ6Z-59-MONOMER; -. DR Proteomes; UP000000808; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 286 Spermidine/putrescine transport system FT permease protein PotC homolog. FT /FTId=PRO_0000060186. FT TRANSMEM 15 35 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 78 98 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 113 133 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 145 165 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 191 211 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 244 264 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 74 264 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 286 AA; 31895 MW; 8994ED9ED535422C CRC64; MFKMKSCKLW LRGSFFVIVL VLIYLPLIIV VLVSFNGSST RGNIVLDFGN VLNPNPDAKS AYLRLGEADF AIPLLNSVII GLITVIVSIP IAIMTAFALL RSRQWLNKTV FGIANFSLAT PDIITGISLV LLFANTWLSF NQQLGFFTII SSHISFSVPY ALVLIYPKMQ KLNRNLILAS QDLGYSPIAT FFHITLPYLL PSILSAILVV FATSFDDYVI TSLVQGSVKT VASELYSFRK GIKAWAIAFG TILILVSILA VLLVTLHKYL RFKHKEMLRV KQWKNS // ID PTMA_MYCPN Reviewed; 143 AA. AC P75145; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component; DE EC=2.7.1.-; DE AltName: Full=EIIA-Mtl; DE AltName: Full=EIII-Mtl; DE AltName: Full=PTS system mannitol-specific EIIA component; GN Name=mtlF; OrderedLocusNames=MPN_653; ORFNames=MP189; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in mannitol transport (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine + CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L- CC histidine/cysteine. {ECO:0000255|PROSITE-ProRule:PRU00417}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95837.1; -; Genomic_DNA. DR PIR; S73515; S73515. DR RefSeq; NP_110342.1; NC_000912.1. DR RefSeq; WP_010875010.1; NC_000912.1. DR ProteinModelPortal; P75145; -. DR IntAct; P75145; 1. DR EnsemblBacteria; AAB95837; AAB95837; MPN_653. DR GeneID; 877014; -. DR KEGG; mpn:MPN653; -. DR PATRIC; 20022789; VBIMycPne110_0717. DR KO; K02798; -. DR OMA; IQIAGIS; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; MPNE272634:GJ6Z-699-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR Pfam; PF00359; PTS_EIIA_2; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Phosphotransferase system; KW Reference proteome; Sugar transport; Transferase; Transport. FT CHAIN 1 143 Mannitol-specific phosphotransferase FT enzyme IIA component. FT /FTId=PRO_0000186635. FT DOMAIN 1 142 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT ACT_SITE 61 61 Tele-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00417}. SQ SEQUENCE 143 AA; 16313 MW; AA672A4051E5E8CA CRC64; MKLLKNNIYI NVYLKNKQEI FEFVFKKFKE DGAVLDSFLP AIVERDKAAS VAIGNYLFLP HPVYDEIANI QKEKMVFIGL KDVINIDGQP IKFICGLALK GEHQMDALQS LAIAFSDPEE VEKLVKDKDL TQDKVLEFLA KHN // ID PSTA_MYCPN Reviewed; 651 AA. AC P75185; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Phosphate transport system permease protein PstA homolog; GN Name=pstA; OrderedLocusNames=MPN_610; ORFNames=MP232; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Could be part of a binding-protein-dependent transport CC system for phosphate; probably responsible for the translocation CC of the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95880.1; -; Genomic_DNA. DR PIR; S73558; S73558. DR RefSeq; NP_110299.1; NC_000912.1. DR RefSeq; WP_010874967.1; NC_000912.1. DR ProteinModelPortal; P75185; -. DR EnsemblBacteria; AAB95880; AAB95880; MPN_610. DR GeneID; 877113; -. DR KEGG; mpn:MPN610; -. DR PATRIC; 20022701; VBIMycPne110_0673. DR KO; K02037; -. DR KO; K02038; -. DR OMA; PYHLFIL; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MPNE272634:GJ6Z-656-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR005672; Phosphate_PstA. DR Pfam; PF00528; BPD_transp_1; 2. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF161098; SSF161098; 2. DR TIGRFAMs; TIGR00974; 3a0107s02c; 1. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 651 Phosphate transport system permease FT protein PstA homolog. FT /FTId=PRO_0000060205. FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 64 84 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 107 127 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 143 163 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 203 223 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 266 286 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 368 388 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 417 437 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 451 471 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 486 506 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 535 555 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 613 633 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 70 285 ABC transmembrane type-1 1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 413 623 ABC transmembrane type-1 2. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 651 AA; 72748 MW; 228E845DDE225387 CRC64; MKQKIKSRLK KDNWLRYLSQ TVAVCFLLLF ISFFIFLLIE AAKTGPDFTK SLLGLEFNLG AKKASIWFPL LVSFVVSIGS LIIASYIGVR TSIFLVYRCK PRIRKKLLLV IDILSGIPSV IFGLFATQIL SSIFRDVLHL PPLSLLNVIV MLSFMIIPIV ISLTTNALLH VESSLMTVAI SLGENKTSVI YKVIKKEIKA QLVVILVLAF GRAISETMAV NFILQSVNYQ EVIANDRFFT SDLKTLGSVI STFIFSENGD EQVSGVLYTF GIIIFVLISF LNFFAIWSTR PKTLERYPFL KKISNFIYQV VWFIPNNIGA LFTDLTARRQ QVKKITAANV EQRATFFKER MQTNHLNKVY TSWKILQEIF CAVLAFGFVL GILLFVFING SQAIQRSGST VFSFGVDTTG RALVNTLVII LVAIGITFPI ALLIAIWLNE YTKSRIAKNT FSFVIDSLSS MPSIIYGLFG LSFFLRTLQL SAGGANGTSL MAGILTISVV VLPFLIRTCQ EALNNVSWDL RVSAYALGVS KREVIWKIVL PGALKGLIIA LILTINRIIA ETAPFFITAG LASSNLFDLS LPGQTLTTRI YGQLFSTNST AVDVMLETAL VSIVFLMFLI FLSSYLIPYL FSFNKQKWLQ IKSKLQLWKK A // ID PSTB_MYCPN Reviewed; 329 AA. AC P75186; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702}; DE EC=3.6.3.27 {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702}; GN Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; GN OrderedLocusNames=MPN_609; ORFNames=MP233; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phosphate(Out) = ADP + phosphate CC + phosphate(In). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PstB), two transmembrane proteins (PstC and PstA) and a solute- CC binding protein (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95881.1; -; Genomic_DNA. DR PIR; S73559; S73559. DR RefSeq; NP_110298.1; NC_000912.1. DR RefSeq; WP_010874966.1; NC_000912.1. DR ProteinModelPortal; P75186; -. DR EnsemblBacteria; AAB95881; AAB95881; MPN_609. DR GeneID; 877047; -. DR KEGG; mpn:MPN609; -. DR PATRIC; 20022699; VBIMycPne110_0672. DR KO; K02036; -. DR OMA; FDVSMKI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-655-MONOMER; -. DR Proteomes; UP000000808; 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:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase 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; IPR015850; ABC_transpr_PstB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005670; Phosp_transpt1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00972; 3a0107s01c2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51238; PSTB; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Phosphate transport; Reference proteome; KW Transport. FT CHAIN 1 329 Phosphate import ATP-binding protein FT PstB. FT /FTId=PRO_0000092847. FT DOMAIN 83 325 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01702}. FT NP_BIND 116 123 ATP. {ECO:0000255|HAMAP-Rule:MF_01702}. SQ SEQUENCE 329 AA; 38064 MW; A30B64546BE662D7 CRC64; MKKGLKTIWH NFIQKREKVK QYRALYEKQI KQYQQKVAKL DPTTKAEEIA NLQSEIDVLQ RLIKIKNTKD DVVKQDFDKK NVFEIENLNF WYNKDKQVLF DINLKIKRNK ITALIGKSGC GKSTFIRCLN KLNDLNENVR WNGKIFFLGK NINSGIINDL TLRTRVGMVF QQLTPFNFSI FENIAYGLRA HGIHNKQAIH EIVEQALKST ALWDEVKDNL HRNANTLSGG QQQRLCIARA IALQPDVLLM DEPTSALDSI ATNSIELLIQ QLKEKYTIII VTHSMAQTIR ITDETIFFAN GRVVEQGTTK QIFTRPKQKE TNRYISGRN // ID PTF3A_MYCPN Reviewed; 694 AA. AC P75039; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=PTS system fructose-specific EIIABC component; DE AltName: Full=EIIABC-Fru; DE Includes: DE RecName: Full=Fructose-specific phosphotransferase enzyme IIA component; DE AltName: Full=EII-Fru; DE AltName: Full=PTS system fructose-specific EIIA component; DE Includes: DE RecName: Full=Fructose-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.202; DE AltName: Full=EIII-Fru; DE AltName: Full=PTS system fructose-specific EIIB component; DE Includes: DE RecName: Full=Fructose permease IIC component; DE AltName: Full=PTS system fructose-specific EIIC component; GN Name=fruA; OrderedLocusNames=MPN_078; ORFNames=MP077; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in fructose transport. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC fructose(Side 1) = [protein]-L-histidine + D-fructose 1- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00427}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel CC and contains the specific substrate-binding site. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00422}. CC -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95725.1; -; Genomic_DNA. DR PIR; S73403; S73403. DR RefSeq; NP_109766.1; NC_000912.1. DR RefSeq; WP_010874435.1; NC_000912.1. DR ProteinModelPortal; P75039; -. DR EnsemblBacteria; AAB95725; AAB95725; MPN_078. DR GeneID; 877051; -. DR KEGG; mpn:MPN078; -. DR PATRIC; 20021437; VBIMycPne110_0079. DR KO; K02768; -. DR KO; K02769; -. DR KO; K02770; -. DR OMA; IPFVSEP; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; MPNE272634:GJ6Z-81-MONOMER; -. DR Proteomes; UP000000808; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro. DR GO; GO:0005351; F:sugar:proton symporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR InterPro; IPR013011; PTS_EIIB_2. DR InterPro; IPR003501; PTS_EIIB_2/3. DR InterPro; IPR003352; PTS_EIIC. DR InterPro; IPR013014; PTS_EIIC_2. DR InterPro; IPR004715; PTS_IIA_fruc. DR InterPro; IPR003353; PTS_IIB_fruc. DR InterPro; IPR006327; PTS_IIC_fruc. DR Pfam; PF00359; PTS_EIIA_2; 1. DR Pfam; PF02378; PTS_EIIC; 1. DR Pfam; PF02302; PTS_IIB; 1. DR SUPFAM; SSF52794; SSF52794; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR TIGRFAMs; TIGR00829; FRU; 1. DR TIGRFAMs; TIGR00848; fruA; 1. DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1. DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Kinase; Membrane; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 694 PTS system fructose-specific EIIABC FT component. FT /FTId=PRO_0000186511. FT TRANSMEM 318 338 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 364 384 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 390 410 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 422 442 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 461 481 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 502 522 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 542 562 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 576 596 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 602 622 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 655 675 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT DOMAIN 4 149 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT DOMAIN 179 275 PTS EIIB type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00422}. FT DOMAIN 310 687 PTS EIIC type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT ACT_SITE 68 68 Tele-phosphohistidine intermediate; for FT EIIA activity. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT ACT_SITE 185 185 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000250}. SQ SEQUENCE 694 AA; 75164 MW; 919E12BFBCC5FF6A CRC64; MFKPLLSAEL FFNWTAKDFK DKTSFLKQAC RVLQDKNCIK EEQIALTALK EREAQITTGI MSKLALPHMQ SATVLKPFVA VFKVNNVDWQ SLDNQPVKLI FLIGVPKDQG NLHLEFISQF SKLMLQDEFA NKVPNIRSFN GLINLIDSFQ QTAVASQPVV NEAAAQTEEP KDTNTQYDFV AVTACPTGIA HTFMAKEALE KFARDHNLKV KVETQGTDGI QNQLTESDLN NTKGIILACD RLIDLTRFYG HANVVEVSTT KAIKTPQTVY DQVVKKEGKL LGNKSSDSAS QTELKETTEQ LSFKDFHKRI YRAILSGVSY MLPFVVFGGI LIAIAFLIDI NNAGNAGKQF GSKDPIANWF KTLGGLSFGL IVPILSAYIA FALVGRQGLL PGFIVGLISA GKFLLNIDIV TGKIDWATES KVSSGFFGAI FGGLLAAVLI IVQQRYIYRK LPQALQGIKN ILFIPLLGTL VTAALFWVIN IPLIYLNYGL SKFLQIMDKP YLAPLLGLVI GLMMCFDLGG PVNKAAYVFG VVSLESQNSG TVAMASAILS GMVPPLGIAI AATIRKQCFD KEELPAAYAC YVMGLSFISE GAIPFVAKRP KIMLAANLIG GAVCGVLTGA FALTIRAPHG GVFVFALLKT NLEGIAGNTL QIGAGVGLAL LALIVSSFIS AGIIIGHNLL VVRKKTKQLV NTNA // ID PTG3C_MYCPN Reviewed; 940 AA. AC P75569; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=PTS system glucose-specific EIICBA component; DE AltName: Full=EII-Glc/EIII-Glc; DE AltName: Full=EIICBA-Glc; DE Includes: DE RecName: Full=Glucose permease IIC component; DE AltName: Full=PTS system glucose-specific EIIC component; DE Includes: DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.199; DE AltName: Full=PTS system glucose-specific EIIB component; DE Includes: DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component; DE AltName: Full=PTS system glucose-specific EIIA component; GN Name=ptsG; OrderedLocusNames=MPN_207; ORFNames=MP624; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in glucose transport. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC glucose(Side 1) = [protein]-L-histidine + D-glucose 6- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00426}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00426}. CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel CC and contains the specific substrate-binding site. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- SIMILARITY: Contains 1 PTS EIIA type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00416}. CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00426}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96272.1; -; Genomic_DNA. DR PIR; S73950; S73950. DR RefSeq; NP_109895.1; NC_000912.1. DR RefSeq; WP_010874564.1; NC_000912.1. DR ProteinModelPortal; P75569; -. DR IntAct; P75569; 4. DR EnsemblBacteria; AAB96272; AAB96272; MPN_207. DR GeneID; 876972; -. DR KEGG; mpn:MPN207; -. DR PATRIC; 20021739; VBIMycPne110_0226. DR KO; K02777; -. DR KO; K02778; -. DR KO; K02779; -. DR OMA; IFGYIER; -. DR OrthoDB; EOG6FFS9V; -. DR BioCyc; MPNE272634:GJ6Z-214-MONOMER; -. DR Proteomes; UP000000808; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1360.60; -; 1. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018113; PTrfase_EIIB_Cys. DR InterPro; IPR001127; PTS_EIIA_1_perm. DR InterPro; IPR003352; PTS_EIIC. DR InterPro; IPR013013; PTS_EIIC_1. DR InterPro; IPR001996; PTS_IIB_1. DR Pfam; PF00358; PTS_EIIA_1; 1. DR Pfam; PF00367; PTS_EIIB; 1. DR Pfam; PF02378; PTS_EIIC; 2. DR SUPFAM; SSF51261; SSF51261; 1. DR SUPFAM; SSF55604; SSF55604; 1. DR TIGRFAMs; TIGR00826; EIIB_glc; 1. DR TIGRFAMs; TIGR00830; PTBA; 1. DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1. DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1. DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1. DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Kinase; Membrane; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 940 PTS system glucose-specific EIICBA FT component. FT /FTId=PRO_0000186560. FT TRANSMEM 43 63 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 83 103 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 112 132 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 175 195 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 209 229 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 487 507 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 515 535 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 537 557 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 564 584 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 598 618 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT DOMAIN 1 284 PTS EIIC type-1; first part. FT {ECO:0000255|PROSITE-ProRule:PRU00426}. FT DOMAIN 479 630 PTS EIIC type-1; second part. FT {ECO:0000255|PROSITE-ProRule:PRU00426}. FT DOMAIN 661 743 PTS EIIB type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. FT DOMAIN 794 907 PTS EIIA type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00416}. FT REGION 285 478 Unknown. FT ACT_SITE 683 683 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. FT ACT_SITE 847 847 Tele-phosphohistidine intermediate; for FT EIIA activity. {ECO:0000255|PROSITE- FT ProRule:PRU00416}. SQ SEQUENCE 940 AA; 101619 MW; 44B836307FDA36EF CRC64; MQIKAQDTGQ QKKSCLLSNI RNKWKNRNRG SFRQWVGKLS NGLMIPIAVL PIAGIFLGVG DAIAGNAGDL TGLRYFGLFI KNGGDVVFAN LPILFAIAIA ITFSQDAGVA GFSAFVFWAA MNGFMSSLIL PFDKAGKIIT DTSTPIAGFK VLYNKSVPVH AIATTLGLRT LSTSVFGGII VGALTSVLYK KFYAIRLPDV IGFFSGTRFV PIICFVVAIP VALILLMIWP AVSIGLNAIG TGLGFLGGKG YGANSLIFGY IERSLIPFGV HHAFYAPLWY TSAGGSLQEI VNQQVWIRPD FHLSDNYVAR VIGWVDPNNS SMYIIPGALN GQNGSSTGNT MSKDLNGALS AYMSKESTAF LTWKDLVDGL TFKGNFDKMA ENGLLDGSNK IWLGLNGSGI LGKKLLLSDG NVYTITFKTF ANTTPIAWSK GAQAVLPLNA SSTIVNNPTA LAAATQSNNN TNNIKLYPVN SFRVAVESLN PAQYSQGKFP FMLFGIPAAG VAMILAAPKD RRKEAASIVG SAAFTSFLTG ITEPFEFTFL FLAPWLFYGV HAVLAAVSFW LMNILGANVG QTFSGSFIDF ILYGALPDGR RWLANSYLVP IIGLFLAAIY FPTFYFLIKH FNLATPGRGG KLITKKEYLA SKAAAKAEGV SGVAENFTQT QIEAGILLQA YGGKENIVEL GACITKLRVT VKNPELVKEE PIKELGAAGV MRTTPTFFVA VFGTRAAVYK SAMQDIIQGK VNWEALQKVI NTDQLAVEPK ETTPPKEVMP VVQDEIVILS PVNGTLKSLN QVPDETFKQK LVGEGVAIVP SDGHFKAPGE AGVKTELAFP GGHAYIFDID GIKVMLHIGI DTVQINAKKQ PGEPLEVFDI KTKQGEYTKE KSESVVEVDL KKLSKKYNPI TPFVVMKESL ENFKLVPIRQ RGEIKVGQPI FKLVYKKSQA // ID PTH_MYCPN Reviewed; 188 AA. AC P78034; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. 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=MPN_221; GN ORFNames=MP610; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96258.1; -; Genomic_DNA. DR PIR; S73936; S73936. DR RefSeq; NP_109909.1; NC_000912.1. DR RefSeq; WP_010874578.1; NC_000912.1. DR ProteinModelPortal; P78034; -. DR IntAct; P78034; 4. DR EnsemblBacteria; AAB96258; AAB96258; MPN_221. DR GeneID; 877101; -. DR KEGG; mpn:MPN221; -. DR PATRIC; 20021767; VBIMycPne110_0240. DR KO; K01056; -. DR OMA; FMNRSGL; -. DR OrthoDB; EOG6C5RTR; -. DR BioCyc; MPNE272634:GJ6Z-228-MONOMER; -. DR Proteomes; UP000000808; 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 1 188 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000187777. SQ SEQUENCE 188 AA; 21417 MW; 3F1F8F1F18C53073 CRC64; MDKLRLVVGL GNLGKQYAET RHNAGFKVID RLLSLYHVQL EERNNLGEFI LLRKHKVVLA KPNTYMNHSG KFVKWACQNW NIKPDKVMVV YDELAFPLGT VRLKMQGSAN NHNGIKSVIA HLNTEHFNRL RFGIKSDNTS NILHEVVMSE FTPAERNLLE TALTKAIEAL KGYIDGVTML KLMEVFNA // ID PT1_MYCPN Reviewed; 572 AA. AC P75168; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 103. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase; DE EC=2.7.3.9; DE AltName: Full=Phosphotransferase system, enzyme I; GN Name=ptsI; OrderedLocusNames=MPN_627; ORFNames=MP215; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine = CC pyruvate + protein N(pi)-phospho-L-histidine. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the CC central domain the pyrophosphate/phosphate carrier histidine, and CC the C-terminal domain the pyruvate binding site. {ECO:0000250}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated CC by a phosphocarrier histidine residue located on the surface of CC the central domain. The two first partial reactions are catalyzed CC at an active site located on the N-terminal domain, and the third CC partial reaction is catalyzed at an active site located on the C- CC terminal domain. For catalytic turnover, the central domain CC swivels from the concave surface of the N-terminal domain to that CC of the C-terminal domain (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95863.1; -; Genomic_DNA. DR PIR; S73541; S73541. DR RefSeq; NP_110316.1; NC_000912.1. DR RefSeq; WP_010874984.1; NC_000912.1. DR ProteinModelPortal; P75168; -. DR IntAct; P75168; 1. DR EnsemblBacteria; AAB95863; AAB95863; MPN_627. DR GeneID; 876731; -. DR KEGG; mpn:MPN627; -. DR PATRIC; 20022737; VBIMycPne110_0691. DR KO; K08483; -. DR OMA; NIEIGIM; -. DR OrthoDB; EOG657JBQ; -. DR BioCyc; MPNE272634:GJ6Z-673-MONOMER; -. DR Proteomes; UP000000808; 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; IPR018274; PEP_util_AS. 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. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transport. FT CHAIN 1 572 Phosphoenolpyruvate-protein FT phosphotransferase. FT /FTId=PRO_0000147077. FT ACT_SITE 190 190 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 498 498 Proton donor. {ECO:0000250}. FT METAL 427 427 Magnesium. {ECO:0000250}. FT METAL 451 451 Magnesium. {ECO:0000250}. FT BINDING 297 297 Substrate. {ECO:0000250}. FT BINDING 333 333 Substrate. {ECO:0000250}. FT BINDING 427 427 Substrate. {ECO:0000250}. FT BINDING 448 448 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 449 449 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 450 450 Substrate. {ECO:0000250}. FT BINDING 451 451 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 572 AA; 63950 MW; 5B12EF54B0CB80CB CRC64; MKKLSGIGVS DGMALAKAFL VKTPEFAVNK YLKHQLTKAQ AKRLLDSAFK KAVKDLEEIK EITVNNINTE AGMIFDAHIQ MLNDPTITEQ LEQQLAQNVH PVIAVDTVFS QTATMFSQMQ DKYFQERAAD ILDLRQRLLA YLTGQKPHDL VKIKSDVIIV AHDLTPSQTA TLNKKYVKGF LTEIGGRTSH AAIMARSLEI PAVVGIKGIT TKVKDGQIVG VDGRKGIAGL DLNSKDTTEW KKQKALEEKY QQELKQYTNK ETVTLDGHAV VVAANIGNVK DMELACQYNT NGVGLFRTEF LYMNSQEWPD EETQYQAYKA VLEQAHGDLV IIRTLDIGGD KKLNYYEFPH EDNPFLGYRA LRLTLDKQDI FKTQLRALLR AADHGQLGIM FPMVATLDEL LQAKQLLNQV HQELGGNKQF KLGIMIEIPA AVLAANTLSH HVDFFSIGTN DLIQYSFAAD RMNKNVSYLY QPLNPALLKL IYLTIEGGKV NDIWTGMCGE MAGEPLAIPL LLGLGLKEFS MSASSMFKAR MIIAKLNYTE CQTLAQKALT LANAKEVEKL VEKFFKKKDI FI // ID PTAS_MYCPN Reviewed; 320 AA. AC P75359; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Phosphate acetyltransferase; DE EC=2.3.1.8; DE AltName: Full=Phosphotransacetylase; GN Name=pta; OrderedLocusNames=MPN_428; ORFNames=MP413; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + phosphate = CoA + acetyl CC phosphate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and CC butyryltransferase 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; U00089; AAB96061.1; -; Genomic_DNA. DR PIR; S73739; S73739. DR RefSeq; NP_110116.1; NC_000912.1. DR RefSeq; WP_010874784.1; NC_000912.1. DR ProteinModelPortal; P75359; -. DR IntAct; P75359; 2. DR PRIDE; P75359; -. DR EnsemblBacteria; AAB96061; AAB96061; MPN_428. DR GeneID; 876938; -. DR KEGG; mpn:MPN428; -. DR PATRIC; 20022252; VBIMycPne110_0463. DR KO; K00625; -. DR OMA; GVFIMAR; -. DR OrthoDB; EOG6BKJ5W; -. DR BioCyc; MetaCyc:MONOMER-602; -. DR BioCyc; MPNE272634:GJ6Z-457-MONOMER; -. DR UniPathway; UPA00340; UER00459. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012147; P_Ac_Bu_trans. DR InterPro; IPR004614; P_AcTrfase. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF01515; PTA_PTB; 1. DR PIRSF; PIRSF000428; P_Ac_trans; 1. DR TIGRFAMs; TIGR00651; pta; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 320 Phosphate acetyltransferase. FT /FTId=PRO_0000179134. SQ SEQUENCE 320 AA; 35219 MW; DD1E674A6E4E898F CRC64; MSVIDLLKQR VQSAGKKPVI IFPEGWSPTV MEAVNQLQQA GILTPPVIFR TRSEVPAGFN TAIKHYVIEE MDLTKYANFV YEKRKHKGME MREAQKFVRD ASSLAATLVA LNEVDGEVCG KEYATKDTLR PALQLLGTGN FVSSVFIMEK NEERLYFTDC AFAVYPSPQE LAVVAENTFK FAQSMGEPEL KMVFLSYSTL GSGKGEAVDK VVSATQIFLE KHPELKANVC GELQFDSAFV EKVRKQKAPN LTWNGSANIY VFPNLDAGNI GYKIAQRLGG YEAIGPIVLG LARPFNDLSR GASVSDVFNV GIITAAQTLK // ID PTHP_MYCPN Reviewed; 88 AA. AC P75061; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 108. DE RecName: Full=Phosphocarrier protein HPr; DE EC=2.7.11.-; DE AltName: Full=Histidine-containing protein; GN Name=ptsH; OrderedLocusNames=MPN_053; ORFNames=MP101; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). RN [3] RP PHOSPHORYLATION. RX PubMed=12368461; RA Steinhauer K., Jepp T., Hillen W., Stuelke J.; RT "A novel mode of control of Mycoplasma pneumoniae HPr RT kinase/phosphatase activity reflects its parasitic lifestyle."; RL Microbiology 148:3277-3284(2002). RN [4] RP PHOSPHORYLATION AT SER-47, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14730672; DOI=10.1002/pmic.200300511; RA Jaffe J.D., Berg H.C., Church G.M.; RT "Proteogenomic mapping as a complementary method to perform genome RT annotation."; RL Proteomics 4:59-77(2004). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (sugar PTS). This major carbohydrate active-transport system CC catalyzes the phosphorylation of incoming sugar substrates CC concomitantly with their translocation across the cell membrane. CC The phosphoryl group from phosphoenolpyruvate (PEP) is transferred CC to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr CC then transfers it to the permease (enzymes II/III). CC -!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein CC A (CcpA), forming a complex that binds to DNA at the catabolite CC response elements cre, operator sites preceding a large number of CC catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in CC carbon catabolite repression (CCR), a mechanism that allows CC bacteria to coordinate and optimize the utilization of available CC carbon sources. P-Ser-HPr also plays a role in inducer exclusion, CC in which it probably interacts with several non-PTS permeases and CC inhibits their transport activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein HPr N(pi)-phospho-L-histidine + CC protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L- CC histidine. CC -!- ENZYME REGULATION: Phosphorylation on Ser-47 inhibits the CC phosphoryl transfer from enzyme I to HPr. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HPr domain. {ECO:0000255|PROSITE- CC ProRule:PRU00681}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95749.1; -; Genomic_DNA. DR PIR; S73427; S73427. DR RefSeq; NP_109741.1; NC_000912.1. DR RefSeq; WP_010874410.1; NC_000912.1. DR ProteinModelPortal; P75061; -. DR iPTMnet; P75061; -. DR EnsemblBacteria; AAB95749; AAB95749; MPN_053. DR GeneID; 876864; -. DR KEGG; mpn:MPN053; -. DR PATRIC; 20021383; VBIMycPne110_0053. DR KO; K11189; -. DR OMA; EYTIQDP; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; MPNE272634:GJ6Z-55-MONOMER; -. DR Proteomes; UP000000808; 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 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; 3.30.1340.10; -; 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 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; KW Phosphoprotein; Phosphotransferase system; Reference proteome; KW Serine/threonine-protein kinase; Sugar transport; Transcription; KW Transcription regulation; Transferase; Transport. FT CHAIN 1 88 Phosphocarrier protein HPr. FT /FTId=PRO_0000107864. FT DOMAIN 1 88 HPr. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT ACT_SITE 15 15 Pros-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. FT MOD_RES 47 47 Phosphoserine; by HPrK/P. FT {ECO:0000255|PROSITE-ProRule:PRU00681, FT ECO:0000269|PubMed:14730672}. SQ SEQUENCE 88 AA; 9495 MW; 5609A9F8F9E2C1FE CRC64; MKKIQVVVKD PVGIHARPAS IIAGEANKFK SELKLVSPSG VEGNIKSIIN LMSLGIKQND HITIKAEGTD EEEALNAIKA VLEKHQVI // ID PTMCB_MYCPN Reviewed; 488 AA. AC P75146; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-MAY-2016, entry version 107. DE RecName: Full=PTS system mannitol-specific EIICB component; DE AltName: Full=EIICB-Mtl; DE Short=EII-Mtl; DE Includes: DE RecName: Full=Mannitol permease IIC component; DE AltName: Full=PTS system mannitol-specific EIIC component; DE Includes: DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.197; DE AltName: Full=PTS system mannitol-specific EIIB component; GN Name=mtlA; OrderedLocusNames=MPN_651; ORFNames=MP191; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in mannitol transport. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC mannitol(Side 1) = [protein]-L-histidine + D-mannitol 1- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00427}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel CC and contains the specific substrate-binding site. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00422}. CC -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95839.1; Type=Frameshift; Positions=55, 68; 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; U00089; AAB95839.1; ALT_FRAME; Genomic_DNA. DR PIR; S73517; S73517. DR RefSeq; NP_110340.1; NC_000912.1. DR ProteinModelPortal; P75146; -. DR EnsemblBacteria; AAB95839; AAB95839; MPN_651. DR GeneID; 877002; -. DR KEGG; mpn:MPN651; -. DR PATRIC; 20022785; VBIMycPne110_0715. DR KO; K02799; -. DR KO; K02800; -. DR OMA; MLVNNFY; -. DR OrthoDB; EOG6FBWWQ; -. DR BioCyc; MPNE272634:GJ6Z-697-MONOMER; -. DR Proteomes; UP000000808; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10370; -; 1. DR InterPro; IPR013011; PTS_EIIB_2. DR InterPro; IPR003501; PTS_EIIB_2/3. DR InterPro; IPR029503; PTS_EIIB_mannitol. DR InterPro; IPR013014; PTS_EIIC_2. DR Pfam; PF02302; PTS_IIB; 1. DR SUPFAM; SSF52794; SSF52794; 1. DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1. DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Kinase; Membrane; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 488 PTS system mannitol-specific EIICB FT component. FT /FTId=PRO_0000186619. FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 51 71 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 80 100 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 103 123 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 151 171 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 187 207 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 227 247 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 277 297 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 299 319 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 335 355 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT DOMAIN 15 362 PTS EIIC type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT DOMAIN 397 488 PTS EIIB type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00422}. FT ACT_SITE 403 403 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000250}. SQ SEQUENCE 488 AA; 53440 MW; E4CDE1411110C9C4 CRC64; MRKKLAKVKV HIQSLDSLLS SMTMPIIGIF IAWGLLASFF IPSGWTPDKN LALMVGIGIQ YVIPTIIXFF GGKKIYEIRG GVIAVIIAIA VIAAGQTEAF TKIVGQKSVM FLGVMIFGPI AALILKHTEK FWIHRIKSGF EMLVNNFYLG FLGFALIFPS FYLSIYLIGY IQLGLKLLVE IMQQYKLYPI AAIVIEPAKV LFLNNAINHG VLTPLGLQQV RDSGKSILFL LESNPGPGLG LLVAFLIFFF KRDKKLSSNA ASSSPIHLFG GIHEVYFPFV LLKPVLILAT IAVGVVGNGI LQIFNAGTIA PVSPGSVIAG FLQINKTPLD VAGYALALVL SAVTSLLISL LLLSLTRKKQ LKTLQEAQAQ VAEMKQTPAK KPRQKDTPAI ATKIDFSQVT FVCDAGMGSS TMGAAIFRKE LKNQNIEDIT VINKAIVDLK DEKVIITISQ LYDRVKAKRA DATIYTINQF LDKQGYLTII EKIKNEKN // ID PYRH_MYCPN Reviewed; 235 AA. AC P75165; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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}; Synonyms=smbA; GN OrderedLocusNames=MPN_632; ORFNames=MP210; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95858.1; -; Genomic_DNA. DR PIR; S73536; S73536. DR RefSeq; NP_110321.1; NC_000912.1. DR RefSeq; WP_010874989.1; NC_000912.1. DR ProteinModelPortal; P75165; -. DR EnsemblBacteria; AAB95858; AAB95858; MPN_632. DR GeneID; 877000; -. DR KEGG; mpn:MPN632; -. DR PATRIC; 20022747; VBIMycPne110_0696. DR KO; K09903; -. DR OMA; ADNIGML; -. DR OrthoDB; EOG6M0T8S; -. DR BioCyc; MPNE272634:GJ6Z-678-MONOMER; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_B; PyrH_B; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR015963; Uridylate_kinase_bac. DR PANTHER; PTHR21499:SF23; PTHR21499:SF23; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02075; pyrH_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 235 Uridylate kinase. FT /FTId=PRO_0000143860. FT NP_BIND 8 11 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 131 138 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 49 49 UMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 50 50 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 54 54 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 159 159 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 165 165 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 168 168 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 235 AA; 25420 MW; 92A537B4468C2990 CRC64; MRLKILIKLS GAGMSADSSE PFSNQFLETV IAQLKQLVPN YQIGIVIGGG NIMRGKSCSD YNITEIAGHH LGIMATVING AFLKAKFDSH KLNSTLLSAV SCPSLATHIV SQTTIDDAFK NHDIVIFAGG TGNPYFSTDT AVALRATQMQ ADIILIGKNG VDGVYTADPK KDKHAKFLAS LTYAEAIKND LQIMDITAFT MCKENNLKVI IFNINAEHAI IKALSKQGKY TLIEK // ID RBFA_MYCPN Reviewed; 116 AA. AC P75589; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; GN OrderedLocusNames=MPN_156; ORFNames=MP675; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96323.1; -; Genomic_DNA. DR PIR; S74001; S74001. DR RefSeq; NP_109844.1; NC_000912.1. DR RefSeq; WP_010874513.1; NC_000912.1. DR PDB; 1PA4; NMR; -; A=1-116. DR PDBsum; 1PA4; -. DR ProteinModelPortal; P75589; -. DR SMR; P75589; 6-101. DR IntAct; P75589; 2. DR EnsemblBacteria; AAB96323; AAB96323; MPN_156. DR GeneID; 877289; -. DR KEGG; mpn:MPN156; -. DR PATRIC; 20021635; VBIMycPne110_0174. DR KO; K02834; -. DR OMA; NRTIINE; -. DR OrthoDB; EOG6XQ3TJ; -. DR BioCyc; MPNE272634:GJ6Z-163-MONOMER; -. DR EvolutionaryTrace; P75589; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW rRNA processing. FT CHAIN 1 116 Ribosome-binding factor A. FT /FTId=PRO_0000102695. FT HELIX 8 21 {ECO:0000244|PDB:1PA4}. FT STRAND 25 28 {ECO:0000244|PDB:1PA4}. FT HELIX 30 33 {ECO:0000244|PDB:1PA4}. FT STRAND 39 41 {ECO:0000244|PDB:1PA4}. FT TURN 42 44 {ECO:0000244|PDB:1PA4}. FT STRAND 47 49 {ECO:0000244|PDB:1PA4}. FT STRAND 54 58 {ECO:0000244|PDB:1PA4}. FT HELIX 59 68 {ECO:0000244|PDB:1PA4}. FT HELIX 70 78 {ECO:0000244|PDB:1PA4}. FT HELIX 84 86 {ECO:0000244|PDB:1PA4}. FT STRAND 93 95 {ECO:0000244|PDB:1PA4}. SQ SEQUENCE 116 AA; 13389 MW; EBF11E251DE30720 CRC64; MASYKKERLE NDIIRLINRT VIHEIYNETV KTGHVTHVKL SDDLLHVTVY LDCYNREQID RVVGAFNQAK GVFSRVLAHN LYLAKAVQIH FVKDKAIDNA MRIESIINSL KKSKPN // ID RF1_MYCPN Reviewed; 359 AA. AC P75420; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Peptide chain release factor 1; DE Short=RF-1; GN Name=prfA; OrderedLocusNames=MPN_361; ORFNames=MP475; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000250}. CC -!- INTERACTION: CC P75368:alaS; NbExp=1; IntAct=EBI-2259108, EBI-2259873; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF1 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor 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; U00089; AAB96123.1; -; Genomic_DNA. DR PIR; S73801; S73801. DR RefSeq; NP_110049.1; NC_000912.1. DR RefSeq; WP_010874717.1; NC_000912.1. DR ProteinModelPortal; P75420; -. DR IntAct; P75420; 3. DR EnsemblBacteria; AAB96123; AAB96123; MPN_361. DR GeneID; 877356; -. DR KEGG; mpn:MPN361; -. DR PATRIC; 20022088; VBIMycPne110_0388. DR KO; K02835; -. DR OMA; VAMQNEK; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; MPNE272634:GJ6Z-381-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 359 Peptide chain release factor 1. FT /FTId=PRO_0000177709. FT MOD_RES 236 236 N5-methylglutamine. {ECO:0000250}. SQ SEQUENCE 359 AA; 40812 MW; DAA730666E97A6A5 CRC64; MEFDKQFFSS VEKIVELAEQ LEKDLNKPDL TFEQIKAINK ELKHKQPLVV KFKEFKRLID QALEAEAILE NNELKELHDE AKKELERVRS VVPEYEEALK LLLLPIDENN QKNVIVELRP AAGGDESCIF LADLFNMYRN FCSNKGWKLQ INEMIPSSVG LNFVSFEVNG VDVFAKLKFE SGVHRVQRVP ATESKGRVHT STVTVAVLPQ LEAVEVHINP ADLRVDTYRA SGAGGQHVNR TESAVRITHL PTGIVVSCQE GKSQFTNRDT AMKMLRAKLW EKAQNEQLST QAGLRKSQVG SGDRAEKIRT YNYPQNRVTD HRIKLTVNKL NTIILGDLDE IIEALQADEK KQQLENFFS // ID RBGA_MYCPN Reviewed; 271 AA. AC P75135; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Probable ribosome biogenesis GTPase A; GN Name=rbgA; OrderedLocusNames=MPN_656; ORFNames=K05_orf271, MP186; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for a late step of 50S ribosomal subunit CC assembly. Has GTPase activity. Binds to the 23S rRNA (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC P75429:MPN_349; NbExp=1; IntAct=EBI-2259776, EBI-2260743; CC P75401:MPN_381; NbExp=1; IntAct=EBI-2259776, EBI-2260760; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC MTG1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC -!- SIMILARITY: Contains 1 CP-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95834.1; -; Genomic_DNA. DR PIR; S73512; S73512. DR RefSeq; NP_110345.1; NC_000912.1. DR RefSeq; WP_010875013.1; NC_000912.1. DR ProteinModelPortal; P75135; -. DR IntAct; P75135; 10. DR EnsemblBacteria; AAB95834; AAB95834; MPN_656. DR GeneID; 877013; -. DR KEGG; mpn:MPN656; -. DR PATRIC; 20022797; VBIMycPne110_0721. DR KO; K14540; -. DR OMA; ARCPISS; -. DR OrthoDB; EOG6G4VXH; -. DR BioCyc; MPNE272634:GJ6Z-702-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.10.1580.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR030378; G_CP_dom. 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. DR PROSITE; PS51721; G_CP; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; KW Nucleotide-binding; Reference proteome; Ribosome biogenesis. FT CHAIN 1 271 Probable ribosome biogenesis GTPase A. FT /FTId=PRO_0000210615. FT DOMAIN 21 175 CP-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01058}. FT NP_BIND 127 132 GTP. {ECO:0000250}. FT BINDING 171 171 GTP; via amide nitrogen. {ECO:0000250}. SQ SEQUENCE 271 AA; 30514 MW; A15D4842DBFB6A29 CRC64; MDTFTSAVKI NWFPGHMKKT HDQLKKLASS LDGVIEVVDA RAPTLTQNPE ITAYFTNKPK LTLALKADLA QTVANSNILW GTLKQGLQLK RLVIKKLQTL FQAKKNQLKA KGLLVHQFRL AVIGMPNVGK SSLINLLLNK NHLQVANRAG VTKSMSWNQI SSEFYLSDTP GVFFKRIDEM AVGYKLVLTN VIKREVVPLE DVGAFAFCYL SKHYPQLLPY EGTDFTEFLH KFAISRKLLQ KSNQLNINLA CELFVSELIN GKYGKLSFEL D // ID RIBF_MYCPN Reviewed; 269 AA. AC P75587; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative riboflavin biosynthesis protein RibF; DE Includes: DE RecName: Full=Riboflavin kinase; DE EC=2.7.1.26; DE AltName: Full=Flavokinase; DE Includes: DE RecName: Full=FMN adenylyltransferase; DE EC=2.7.7.2; DE AltName: Full=FAD pyrophosphorylase; DE AltName: Full=FAD synthase; GN Name=ribF; OrderedLocusNames=MPN_158; ORFNames=MP673; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN. CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD. CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: CC step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from CC riboflavin (ATP route): step 1/1. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260090, EBI-2260090; CC -!- SIMILARITY: Belongs to the RibF 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; U00089; AAB96321.1; -; Genomic_DNA. DR PIR; S73999; S73999. DR RefSeq; NP_109846.1; NC_000912.1. DR RefSeq; WP_010874515.1; NC_000912.1. DR ProteinModelPortal; P75587; -. DR IntAct; P75587; 1. DR EnsemblBacteria; AAB96321; AAB96321; MPN_158. DR GeneID; 877209; -. DR KEGG; mpn:MPN158; -. DR PATRIC; 20021639; VBIMycPne110_0176. DR KO; K11753; -. DR OMA; QRKIYKS; -. DR OrthoDB; EOG6QP0ZV; -. DR BioCyc; MPNE272634:GJ6Z-165-MONOMER; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW ATP-binding; Complete proteome; FAD; Flavoprotein; FMN; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 269 Putative riboflavin biosynthesis protein FT RibF. FT /FTId=PRO_0000194146. SQ SEQUENCE 269 AA; 30435 MW; 2E63D7BC7A8FA12D CRC64; MQQTLIIGAF DGLHKGHQLL AQAASGPVVA LLIANIPSLQ SDWLYEPKQR QVQLQQHFQS VVHSYDVIEH NISAQAFFDQ IISPLRCQQL VVGADFCFGK DNQNADFLRR LFPNTTIIPK DSQTLSSSTI RQWLKQGQIE QANAVLLEPY FREGVVIRGN QQARFLGWPT ANITLKPYMV PLRCGSYVIT VTYHQTNYPG VGFISYKNDQ LVCETHLIGF SGDLYGKQLR FTFNQFIRPQ QKFSGVQALQ KAISGDLKQA QKWFAQSTN // ID RECA_MYCPN Reviewed; 336 AA. AC P78014; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. 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=MPN_490; ORFNames=MP352; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of CC single-stranded DNA, the ATP-dependent uptake of single-stranded CC DNA by duplex DNA, and the ATP-dependent hybridization of CC homologous single-stranded DNAs. It interacts with LexA causing CC its activation and leading to its autocatalytic cleavage. CC {ECO:0000255|HAMAP-Rule:MF_00268}. CC -!- INTERACTION: CC P75080:polC; NbExp=3; IntAct=EBI-2258718, EBI-2258713; 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; U00089; AAB96000.1; -; Genomic_DNA. DR PIR; S73678; S73678. DR RefSeq; NP_110178.1; NC_000912.1. DR RefSeq; WP_010874846.1; NC_000912.1. DR ProteinModelPortal; P78014; -. DR IntAct; P78014; 2. DR EnsemblBacteria; AAB96000; AAB96000; MPN_490. DR GeneID; 877213; -. DR KEGG; mpn:MPN490; -. DR PATRIC; 20022406; VBIMycPne110_0530. DR KO; K03553; -. DR OMA; TRKGAWY; -. DR OrthoDB; EOG6ZKXNZ; -. DR BioCyc; MPNE272634:GJ6Z-531-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 336 Protein RecA. FT /FTId=PRO_0000122765. FT NP_BIND 66 73 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. SQ SEQUENCE 336 AA; 36918 MW; EA580D4A7657EB4D CRC64; MVQKEMINKK ISQDNSFIQN NNLADFDFLD AKKNSEIKTV STGSLHLDEA LGTGGLPLGR IVELYGNESS GKTTVALHAV ASFQKAGKVA CYIDAEGALD LSYAKAIGID LGKLLVAHPK HGENAFALME SLIKTNKVAL IVVDSVAALI PKQELEGNMD DQTIGLHARM MSKGLRRVQS LLPESDTCLL FINQLREKPG VMFGNGEVTT GGRALKFYAS MRMEAKRSEL LKDRFGNYVG IKSKLTVSKN KVARPFGVAF LEIMFNRGIV YEHEVIELAL KHNVVVRSDN AYSFKSQNIA IGKEKLFSVL AEKPELFEQI KQLTIKQIHS PPPPAS // ID RIR2_MYCPN Reviewed; 339 AA. AC P75461; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=nrdF; OrderedLocusNames=MPN_322; ORFNames=MP514; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC small chain family. {ECO:0000305}. CC -!- CAUTION: Seems to lack two of the iron-binding residues. 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; U00089; AAB96162.1; -; Genomic_DNA. DR PIR; S73840; S73840. DR RefSeq; NP_110010.1; NC_000912.1. DR RefSeq; WP_010874678.1; NC_000912.1. DR ProteinModelPortal; P75461; -. DR SMR; P75461; 24-307. DR IntAct; P75461; 4. DR EnsemblBacteria; AAB96162; AAB96162; MPN_322. DR GeneID; 876942; -. DR KEGG; mpn:MPN322; -. DR PATRIC; 20021998; VBIMycPne110_0346. DR KO; K00526; -. DR OMA; YYQADEP; -. DR OrthoDB; EOG68DD19; -. DR BioCyc; MPNE272634:GJ6Z-339-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR026494; RNR_NrdF. DR InterPro; IPR000358; RNR_small. DR PANTHER; PTHR23409; PTHR23409; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 339 Ribonucleoside-diphosphate reductase FT subunit beta. FT /FTId=PRO_0000190484. FT ACT_SITE 125 125 {ECO:0000250}. FT METAL 87 87 Iron 1. {ECO:0000250}. FT METAL 121 121 Iron 1. {ECO:0000250}. FT METAL 215 215 Iron 2. SQ SEQUENCE 339 AA; 39413 MW; AE2FA78C2B745176 CRC64; MANTKKYFLE SVSPLEYAQK KFQGNLRSVN WNLVDDEKDL EVWNRITQNF WLPEKIPVSN DIPSWKQLSK EWQDLITKTF TGLTLLDTIQ ATIGDIKQID YALTDHEQVI YANFAFMVGV HARSYGTIFS TLCTSEQITE AHEWVVKTES LQKRAKALIP YYTGKDPLKS KVAAALMPGF LLYGGFYLPF YLSSRKQLPN TSDIIRLILR DKVIHNYYSG YKFQRKVEKM SKEKQAEMKR FVFDLMYELI ELEKAYLKEL YEGFGIVEDA IKFSIYNAGK FLQNLGYDSP FTEEETRIKP EIFAQLSARA DENHDFFSGN GSSYVMGISE ETEDKDWDF // ID RL10_MYCPN Reviewed; 161 AA. AC P75240; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=50S ribosomal protein L10; GN Name=rplJ; OrderedLocusNames=MPN_538; ORFNames=MP304; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central CC role in the interaction of the ribosome with GTP-bound translation CC factors. {ECO:0000250}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC The N-terminus interacts with L11 and the large rRNA to form the CC base of the stalk. The C-terminus forms an elongated spine to CC which L12 dimers bind in a sequential fashion forming a multimeric CC L10(L12)X complex (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95952.1; -; Genomic_DNA. DR PIR; S73630; S73630. DR RefSeq; NP_110227.1; NC_000912.1. DR RefSeq; WP_010874895.1; NC_000912.1. DR ProteinModelPortal; P75240; -. DR IntAct; P75240; 1. DR EnsemblBacteria; AAB95952; AAB95952; MPN_538. DR GeneID; 877400; -. DR KEGG; mpn:MPN538; -. DR PATRIC; 20022553; VBIMycPne110_0600. DR KO; K02864; -. DR OMA; VWGTEDE; -. DR OrthoDB; EOG6DNTDR; -. DR BioCyc; MPNE272634:GJ6Z-583-MONOMER; -. DR Proteomes; UP000000808; 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 1 161 50S ribosomal protein L10. FT /FTId=PRO_0000154672. SQ SEQUENCE 161 AA; 17618 MW; 4A7C387BBA49D446 CRC64; MEAKKDKAQQ VADVSHLLST SAGFVIFDYT SMSAIEATSI RKKLFKNGSK IKVIKNNILR RALKAGKFEG IDETAIKGKL AVAVGVNEIV ETLKAVDGVV KAKEAMNFVC GYFDNRAFNS ADLEKIAKLP GRNELYGMFL SVLQAPLRKF LYALEAVKAA K // ID RL17_MYCPN Reviewed; 124 AA. AC Q59547; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; GN OrderedLocusNames=MPN_192; ORFNames=MP639; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43689.1; -; Genomic_DNA. DR EMBL; U00089; AAB96287.1; -; Genomic_DNA. DR PIR; S62816; S62816. DR RefSeq; NP_109880.1; NC_000912.1. DR RefSeq; WP_010874549.1; NC_000912.1. DR ProteinModelPortal; Q59547; -. DR IntAct; Q59547; 2. DR EnsemblBacteria; AAB96287; AAB96287; MPN_192. DR GeneID; 877223; -. DR KEGG; mpn:MPN192; -. DR PATRIC; 20021707; VBIMycPne110_0210. DR KO; K02879; -. DR OMA; KTVQRRG; -. DR OrthoDB; EOG6GR3GR; -. DR BioCyc; MPNE272634:GJ6Z-199-MONOMER; -. DR Proteomes; UP000000808; 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 1 124 50S ribosomal protein L17. FT /FTId=PRO_0000175534. SQ SEQUENCE 124 AA; 14245 MW; 3A627DB7EBF8C62E CRC64; MSYINKPGKT SAWRVMTVRQ QVSAVLAYGK IETTLKKAKN TQKRLDKLIT LAKVDNFNNR RQVKKWLLNT NLFDVDQLMD HLFSKVAPKY EKTPGGYSRV LKLGPRRGDA TEMAILQLTD AKYK // ID RL18_MYCPN Reviewed; 116 AA. AC Q50302; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=MPN_181; ORFNames=MP650; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43700.1; -; Genomic_DNA. DR EMBL; U00089; AAB96298.1; -; Genomic_DNA. DR PIR; S62826; S62826. DR RefSeq; NP_109869.1; NC_000912.1. DR RefSeq; WP_010874538.1; NC_000912.1. DR ProteinModelPortal; Q50302; -. DR EnsemblBacteria; AAB96298; AAB96298; MPN_181. DR GeneID; 876739; -. DR KEGG; mpn:MPN181; -. DR PATRIC; 20021685; VBIMycPne110_0199. DR KO; K02881; -. DR OMA; NEFIFDR; -. DR OrthoDB; EOG64NB48; -. DR BioCyc; MPNE272634:GJ6Z-188-MONOMER; -. DR Proteomes; UP000000808; 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 1 116 50S ribosomal protein L18. FT /FTId=PRO_0000131303. SQ SEQUENCE 116 AA; 13046 MW; B2D5D17D9934109A CRC64; MKTRTEQRRL RHKRIVKKIR ATNHDNRVVL MVIKSLNHIS VQAWDFSQNI VLASSSSLAL KLKNGNKDNA KLVGQDIADK LVKLKLTNVV FDTGGSKYHG RIAALAEAAR ERGLNF // ID RL20_MYCPN Reviewed; 127 AA. AC P78023; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=50S ribosomal protein L20; GN Name=rplT; OrderedLocusNames=MPN_117; ORFNames=MP037; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 subunit CC (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P75133:rplS; NbExp=1; IntAct=EBI-2259250, EBI-2259323; CC -!- SIMILARITY: Belongs to the ribosomal protein L20P 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; U00089; AAG34734.1; -; Genomic_DNA. DR PIR; S73363; S73363. DR RefSeq; NP_109805.1; NC_000912.1. DR RefSeq; WP_010874474.1; NC_000912.1. DR ProteinModelPortal; P78023; -. DR SMR; P78023; 2-114. DR IntAct; P78023; 1. DR EnsemblBacteria; AAG34734; AAG34734; MPN_117. DR GeneID; 877370; -. DR KEGG; mpn:MPN117; -. DR PATRIC; 20021533; VBIMycPne110_0124. DR KO; K02887; -. DR OMA; RKAKEQM; -. DR OrthoDB; EOG6CGCMB; -. DR BioCyc; MPNE272634:GJ6Z-123-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 127 50S ribosomal protein L20. FT /FTId=PRO_0000177187. SQ SEQUENCE 127 AA; 14708 MW; E11715E87AB1A4E2 CRC64; MRIKGGKQTR VRRKKWLKQA SGSFGTRHAS YKVAKQTVIQ AAKYAYRDRR NKKRDFRSLW ILRLNAALRE QGMTYSVFIN LLKKHNIEIN RKVLSELAIK EPSKFNLIVQ KVKSEQPKAA KPAALGN // ID RIR1_MYCPN Reviewed; 721 AA. AC P78027; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdE; OrderedLocusNames=MPN_324; ORFNames=MP512; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- ENZYME REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding. The type of CC nucleotide bound at the specificity site determines substrate CC preference. It seems probable that ATP makes the enzyme reduce CDP CC and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction CC (By similarity). {ECO:0000250}. CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC large chain 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; U00089; AAB96160.1; -; Genomic_DNA. DR PIR; S73838; S73838. DR RefSeq; NP_110012.1; NC_000912.1. DR RefSeq; WP_010874680.1; NC_000912.1. DR ProteinModelPortal; P78027; -. DR SMR; P78027; 18-700. DR IntAct; P78027; 7. DR EnsemblBacteria; AAB96160; AAB96160; MPN_324. DR GeneID; 876946; -. DR KEGG; mpn:MPN324; -. DR PATRIC; 20022002; VBIMycPne110_0348. DR KO; K00525; -. DR OMA; DNMESIA; -. DR OrthoDB; EOG6J48HC; -. DR BioCyc; MPNE272634:GJ6Z-341-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000808; 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; IPR013346; NrdE_NrdA. DR InterPro; IPR026459; RNR_1b_NrdE. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR013554; RNR_N. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR Pfam; PF08343; RNR_N; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR TIGRFAMs; TIGR04170; RNR_1b_NrdE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Disulfide bond; KW DNA replication; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 721 Ribonucleoside-diphosphate reductase FT subunit alpha. FT /FTId=PRO_0000187218. FT REGION 175 176 Substrate binding. {ECO:0000250}. FT REGION 384 388 Substrate binding. {ECO:0000250}. FT REGION 589 593 Substrate binding. {ECO:0000250}. FT ACT_SITE 384 384 Proton acceptor. {ECO:0000250}. FT ACT_SITE 386 386 Cysteine radical intermediate. FT {ECO:0000250}. FT ACT_SITE 388 388 Proton acceptor. {ECO:0000250}. FT BINDING 159 159 Substrate. {ECO:0000250}. FT BINDING 204 204 Substrate; via amide nitrogen. FT {ECO:0000250}. FT SITE 176 176 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 183 183 Allosteric effector binding. FT {ECO:0000250}. FT SITE 213 213 Allosteric effector binding. FT {ECO:0000250}. FT SITE 413 413 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 694 694 Important for electron transfer. FT {ECO:0000250}. FT SITE 695 695 Important for electron transfer. FT {ECO:0000250}. FT SITE 716 716 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT SITE 719 719 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT DISULFID 176 413 Redox-active. {ECO:0000250}. SQ SEQUENCE 721 AA; 82375 MW; 93CAEA95A2A9E647 CRC64; MSVKEKIPAF NTQEDLESYI SLNAYTKVYG DFKMDLHAVE AYIQEHVKPK TKVFHSTKER LDFLVKNDYY DENIINMYSF EQFEEITRKA YAYRFRYANF MGAFKFYNAY ALKTFDGKWY LENYEDRVVM NVLFLANGNY NKALKLLKQI ITNRFQPATP TFLNAGRKKR GEFVSCYLLR IEDNMESIGR AITTTLQLSK RDGGVALLLT NIRESGAPIK KIENQSSGII PIMKLLEDSF SYANQLGQRQ GAGAVYLHAH HPDVMQFLDT KRENADEKIR IKSLSLGLVI PDITFTLAKN NEEMALFSPY DVYEEYGKPL SDISVTEMYY ELLANQRIKK TFINARKFFQ TVAELHFESG YPYILFDDTV NRRNAHPNRI VMSNLCSEIV QPSTPSEFHH DLAFKKVGND ISCNLGSLNI AKAMESGPEF SELVKLAIES LDLVSRVSNL ETAPSIQKGN SENHALGLGA MNLHGFLATN QIYYNSPEAI DFTNIFFYTV AYHAFKASSE LALEKGKFKN FENTKFADGS YFDKYIKVEP DFWTPKTERV KALFQKYQVE IPTRENWKEL ALNIQKNGLA NSHLLAIAPT GSISYLSSCT PSLQPVVSPV EVRKEGRLGR IYVPAYQLNK DSYPFYKDGA YELGPEPIIN IAAAAQQHVD QAISLTLFMT DKATTRDLNK AYIYAFKKGC SSIYYVRVRQ EVLEDSEDHT IQMQQCEACV I // ID RL14_MYCPN Reviewed; 122 AA. AC Q50308; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=MPN_175; ORFNames=MP656; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43706.1; -; Genomic_DNA. DR EMBL; U00089; AAB96304.1; -; Genomic_DNA. DR PIR; S62831; S62831. DR RefSeq; NP_109863.1; NC_000912.1. DR RefSeq; WP_010874532.1; NC_000912.1. DR ProteinModelPortal; Q50308; -. DR SMR; Q50308; 1-122. DR EnsemblBacteria; AAB96304; AAB96304; MPN_175. DR GeneID; 876969; -. DR KEGG; mpn:MPN175; -. DR PATRIC; 20021673; VBIMycPne110_0193. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR BioCyc; MPNE272634:GJ6Z-182-MONOMER; -. DR Proteomes; UP000000808; 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_0000128553. SQ SEQUENCE 122 AA; 13454 MW; 4A41228FAA03AC37 CRC64; MVSFMTRLNV ADNTGAKQVG IIKVLGSTRK RYAFLGDVVV VSVKDAIPSG MVKKGQVLRA VIVRTKKGQQ RKDGTHLKFD DNACVLIKED KSPRGTRIFG PVARELRERG YNKILSLAVE VV // ID RL1_MYCPN Reviewed; 226 AA. AC P78035; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; GN OrderedLocusNames=MPN_220; ORFNames=MP611; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96259.1; -; Genomic_DNA. DR PIR; S73937; S73937. DR RefSeq; NP_109908.1; NC_000912.1. DR RefSeq; WP_010874577.1; NC_000912.1. DR ProteinModelPortal; P78035; -. DR IntAct; P78035; 10. DR EnsemblBacteria; AAB96259; AAB96259; MPN_220. DR GeneID; 877074; -. DR KEGG; mpn:MPN220; -. DR PATRIC; 20021765; VBIMycPne110_0239. DR KO; K02863; -. DR OMA; INAVQDY; -. DR OrthoDB; EOG6FBX2G; -. DR BioCyc; MPNE272634:GJ6Z-227-MONOMER; -. DR Proteomes; UP000000808; 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 1 226 50S ribosomal protein L1. FT /FTId=PRO_0000125693. SQ SEQUENCE 226 AA; 24355 MW; 668C165F9E483807 CRC64; MAKLSKKMKI AVGLVDKTKL YPLQEAVDLV KKTSITKFNG SVDIAVSLNL DTTKAEQQLR GAIAFPHSVG KPIRILAITD DEKAALEAGA DFVGGIDKIN DIKNGWLDFD LIITSPKFMA ALGKLGKLLG TKGLMPNPKT ETVTDDVPAA VRAYKKGKKE YRADSFGNIH MSLGRVDSAS NHLVENALAL LDLIKSRKPA TVKGIYIKNI ALTTTMGPSL KVKLPD // ID RL21_MYCPN Reviewed; 100 AA. AC P78026; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; GN OrderedLocusNames=MPN_325; ORFNames=MP511; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96159.1; -; Genomic_DNA. DR PIR; S73837; S73837. DR RefSeq; NP_110013.1; NC_000912.1. DR RefSeq; WP_010874681.1; NC_000912.1. DR ProteinModelPortal; P78026; -. DR EnsemblBacteria; AAB96159; AAB96159; MPN_325. DR GeneID; 876945; -. DR KEGG; mpn:MPN325; -. DR PATRIC; 20022004; VBIMycPne110_0349. DR KO; K02888; -. DR OMA; KIIDICC; -. DR OrthoDB; EOG6TJ84X; -. DR BioCyc; MPNE272634:GJ6Z-342-MONOMER; -. DR Proteomes; UP000000808; 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 1 100 50S ribosomal protein L21. FT /FTId=PRO_0000181007. SQ SEQUENCE 100 AA; 11639 MW; DB31C2887884D086 CRC64; MHAIVVCGSK QYLVHENDTF FVEKLEAPVG KEIQLDKVLM LDEKIGAPYL EKARVVCVVE KHGLQRKVNV IKHISQKHHL KKYGHRQPYT KLKVVRFVHD // ID RL22_MYCPN Reviewed; 159 AA. AC P75575; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 83. DE RecName: Full=50S ribosomal protein L22; GN Name=rplV; OrderedLocusNames=MPN_170; ORFNames=MP661; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP ANTIBIOTIC RESISTANT VARIANTS. RC STRAIN=ATCC 29342 / M129; RX PubMed=14742195; DOI=10.1128/AAC.48.2.460-465.2004; RA Pereyre S., Guyot C., Renaudin H., Charron A., Bebear C., Bebear C.M.; RT "In vitro selection and characterization of resistance to macrolides RT and related antibiotics in Mycoplasma pneumoniae."; RL Antimicrob. Agents Chemother. 48:460-465(2004). 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). {ECO:0000250}. 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:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family. CC {ECO:0000305}. CC -!- CAUTION: The antibiotic resistant variants could harbor other CC changes as the whole genes were not sequenced. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96309.1; 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; U00089; AAB96309.1; ALT_INIT; Genomic_DNA. DR PIR; S73987; S73987. DR RefSeq; NP_109858.1; NC_000912.1. DR RefSeq; WP_010874527.1; NC_000912.1. DR ProteinModelPortal; P75575; -. DR PRIDE; P75575; -. DR EnsemblBacteria; AAB96309; AAB96309; MPN_170. DR GeneID; 877319; -. DR KEGG; mpn:MPN170; -. DR PATRIC; 20021663; VBIMycPne110_0188. DR KO; K02890; -. DR OMA; KSPENTQ; -. DR OrthoDB; EOG6V4GKB; -. DR BioCyc; MPNE272634:GJ6Z-177-MONOMER; -. DR Proteomes; UP000000808; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 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 Antibiotic resistance; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 159 50S ribosomal protein L22. FT /FTId=PRO_0000125184. FT VARIANT 111 114 Missing (after 48 telithromycin passages; FT confers resistance to various antibiotics FT in combination with a 23S rRNA mutation FT and protein L4 H70L). FT VARIANT 112 112 N -> R (requires 2 nucleotide FT substitutions, after 37 telithromycin FT passages; confers resistance to various FT antibiotics in combination with R114T, a FT 23S rRNA mutation and protein L4 H70L). FT VARIANT 114 114 R -> T (after 20 and 32 telithromycin FT passages; confers resistance to various FT antibiotics in combination with a 23S FT rRNA mutation with and without protein L4 FT H70L). SQ SEQUENCE 159 AA; 17324 MW; 6E5C6B8F96BFCD02 CRC64; MIAFAKQFRV RISPQKARLV CQLIVGKKTA DAQNILSNTP KKAATLIAKL LNSAIANATN NHGMNGDALY VFECVANQGP SMKRTIPRAK GSSNMITKRS SNLVVKLSDN PNERQELIKQ QKALVKKRVE GQQKAKMARQ KAVTSVVKAP SKTQGGVQK // ID RL11_MYCPN Reviewed; 137 AA. AC P75550; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 93. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=MPN_219; ORFNames=MP612; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96260.1; -; Genomic_DNA. DR PIR; S73938; S73938. DR RefSeq; NP_109907.1; NC_000912.1. DR RefSeq; WP_010874576.1; NC_000912.1. DR ProteinModelPortal; P75550; -. DR IntAct; P75550; 5. DR EnsemblBacteria; AAB96260; AAB96260; MPN_219. DR GeneID; 877075; -. DR KEGG; mpn:MPN219; -. DR PATRIC; 20021763; VBIMycPne110_0238. DR KO; K02867; -. DR OMA; TANANYK; -. DR OrthoDB; EOG69PQ9D; -. DR BioCyc; MPNE272634:GJ6Z-226-MONOMER; -. DR Proteomes; UP000000808; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 137 50S ribosomal protein L11. FT /FTId=PRO_0000104323. SQ SEQUENCE 137 AA; 14782 MW; 04788E7F8A6C5924 CRC64; MAKKTITRIA KINLLGGQAK PGPALASVGI NMGEFTKQFN EKTKDKQGEM IPCVITAYND KSFDFILKTT PVSILLKQAA KLEKGAKNAK TIVGKITMAK AKEIAQYKLV DLNANTVEAA LKMVLGTAKQ MGIEVIE // ID RL13_MYCPN Reviewed; 146 AA. AC P75178; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=MPN_617; ORFNames=MP225; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95873.1; -; Genomic_DNA. DR PIR; S73551; S73551. DR RefSeq; NP_110306.1; NC_000912.1. DR RefSeq; WP_010874974.1; NC_000912.1. DR ProteinModelPortal; P75178; -. DR EnsemblBacteria; AAB95873; AAB95873; MPN_617. DR GeneID; 877335; -. DR KEGG; mpn:MPN617; -. DR PATRIC; 20022717; VBIMycPne110_0681. DR KO; K02871; -. DR OMA; YTPHMDC; -. DR OrthoDB; EOG628FBD; -. DR BioCyc; MPNE272634:GJ6Z-663-MONOMER; -. DR Proteomes; UP000000808; 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; IPR023563; Ribosomal_L13_CS. 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. DR PROSITE; PS00783; RIBOSOMAL_L13; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 146 50S ribosomal protein L13. FT /FTId=PRO_0000133743. SQ SEQUENCE 146 AA; 16791 MW; 869294BCEB2B5B90 CRC64; MQKTSMLTKE QANKRRQWYI VDAAGLVLGK LAVKAADLIR GKNKVDFTPN QDCGDYLIII NSDQVVLTGN KKENEFWYHH SQYIGGIKKV SGRDMLKKQS DKLVYNAVKG MLPDNRLSRR WITKVHVFKG DKHNMEAQKP TTLNWS // ID RL16_MYCPN Reviewed; 139 AA. AC P41204; P75573; Q50311; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 90. DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; GN OrderedLocusNames=MPN_172; ORFNames=MP659; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75. RC STRAIN=ATCC 29342 / M129; RX PubMed=1429453; RA Wenzel R., Pirkl E., Herrmann R.; RT "Construction of an EcoRI restriction map of Mycoplasma pneumoniae and RT localization of selected genes."; RL J. Bacteriol. 174:7289-7296(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-139. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). 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; U00089; AAB96307.1; -; Genomic_DNA. DR EMBL; X67651; CAA47893.1; -; Genomic_DNA. DR EMBL; U34795; AAC43709.1; -; Genomic_DNA. DR PIR; S73985; S73985. DR RefSeq; NP_109860.1; NC_000912.1. DR RefSeq; WP_010874529.1; NC_000912.1. DR ProteinModelPortal; P41204; -. DR IntAct; P41204; 5. DR EnsemblBacteria; AAB96307; AAB96307; MPN_172. DR GeneID; 876881; -. DR KEGG; mpn:MPN172; -. DR PATRIC; 20021667; VBIMycPne110_0190. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR BioCyc; MPNE272634:GJ6Z-179-MONOMER; -. DR Proteomes; UP000000808; 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. DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 139 50S ribosomal protein L16. FT /FTId=PRO_0000062148. SQ SEQUENCE 139 AA; 15617 MW; 5A034726D09C3F0C CRC64; MLQPKRTKYR KPHNVSYEGK AKGNSYVAFG EYGLVATKGN WIDARAIESA RIAISKCLGK TGKMWIRIFP HMSKTKKPLE VRMGSGKGNP EFWVAVVKQG TVMFEVANIP ESQMIKALTR AGHKLPVTWK ILKREEVSA // ID RL19_MYCPN Reviewed; 119 AA. AC P75133; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=50S ribosomal protein L19; GN Name=rplS; OrderedLocusNames=MPN_658; ORFNames=MP184; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000250}. CC -!- INTERACTION: CC P75580:rplC; NbExp=1; IntAct=EBI-2259323, EBI-2259216; CC Q50303:rplF; NbExp=1; IntAct=EBI-2259323, EBI-2259177; CC P78023:rplT; NbExp=1; IntAct=EBI-2259323, EBI-2259250; CC -!- SIMILARITY: Belongs to the ribosomal protein L19P 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; U00089; AAB95832.1; -; Genomic_DNA. DR PIR; S73510; S73510. DR RefSeq; NP_110347.1; NC_000912.1. DR RefSeq; WP_010875015.1; NC_000912.1. DR ProteinModelPortal; P75133; -. DR IntAct; P75133; 11. DR EnsemblBacteria; AAB95832; AAB95832; MPN_658. DR GeneID; 877010; -. DR KEGG; mpn:MPN658; -. DR PATRIC; 20022801; VBIMycPne110_0723. DR KO; K02884; -. DR OMA; TFTIRKM; -. DR OrthoDB; EOG6DZF5W; -. DR BioCyc; MPNE272634:GJ6Z-704-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00402; Ribosomal_L19; 1. DR InterPro; IPR001857; Ribosomal_L19. DR InterPro; IPR018257; Ribosomal_L19_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR15680; PTHR15680; 1. DR Pfam; PF01245; Ribosomal_L19; 1. DR PIRSF; PIRSF002191; Ribosomal_L19; 1. DR PRINTS; PR00061; RIBOSOMALL19. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01024; rplS_bact; 1. DR PROSITE; PS01015; RIBOSOMAL_L19; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 119 50S ribosomal protein L19. FT /FTId=PRO_0000163492. SQ SEQUENCE 119 AA; 13839 MW; 4A1A3F3D642D5D9D CRC64; MKKINKQALI DLVEQKQLKA YVPEFSAGDE VNVAIKLKEK EKVRIQNFTG TVLRRRGKGI SETFIVRKTT DGIPIEKNFQ IHNPNISIEL KRRGKVRRAY ISYMRERSGK AAKIKERKQ // ID RL24_MYCPN Reviewed; 111 AA. AC Q50307; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=MPN_176; ORFNames=MP655; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43705.1; -; Genomic_DNA. DR EMBL; U00089; AAB96303.1; -; Genomic_DNA. DR PIR; S62830; S62830. DR RefSeq; NP_109864.1; NC_000912.1. DR RefSeq; WP_010874533.1; NC_000912.1. DR ProteinModelPortal; Q50307; -. DR IntAct; Q50307; 6. DR EnsemblBacteria; AAB96303; AAB96303; MPN_176. DR GeneID; 876929; -. DR KEGG; mpn:MPN176; -. DR PATRIC; 20021675; VBIMycPne110_0194. DR KO; K02895; -. DR OMA; HIRATNE; -. DR OrthoDB; EOG6FFSDM; -. DR BioCyc; MPNE272634:GJ6Z-183-MONOMER; -. DR Proteomes; UP000000808; 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 1 111 50S ribosomal protein L24. FT /FTId=PRO_0000130682. SQ SEQUENCE 111 AA; 12433 MW; BA46C7ADD8B73F27 CRC64; MQRIKKGDKV VVITGKNKGG SGIVLKIMPA RQQAIVEGLN KVTRHKKKDQ TTKRAAKQST GKVQQEAPIF LSKLALFDQK AKQQTIGKIK YVMDPKTNKK TRVFKKSNNT L // ID RL15_MYCPN Reviewed; 151 AA. AC Q50300; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; GN OrderedLocusNames=MPN_183; ORFNames=MP648; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43698.1; -; Genomic_DNA. DR EMBL; U00089; AAB96296.1; -; Genomic_DNA. DR PIR; S62825; S62825. DR RefSeq; NP_109871.1; NC_000912.1. DR RefSeq; WP_010874540.1; NC_000912.1. DR ProteinModelPortal; Q50300; -. DR EnsemblBacteria; AAB96296; AAB96296; MPN_183. DR GeneID; 876773; -. DR KEGG; mpn:MPN183; -. DR PATRIC; 20021689; VBIMycPne110_0201. DR KO; K02876; -. DR OMA; NITANKF; -. DR OrthoDB; EOG6CGCM5; -. DR BioCyc; MPNE272634:GJ6Z-190-MONOMER; -. DR Proteomes; UP000000808; 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; 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. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 151 50S ribosomal protein L15. FT /FTId=PRO_0000104765. SQ SEQUENCE 151 AA; 16730 MW; 8464B05655943E8D CRC64; MELNQLKSVP KARNHKTKTL GRGHGSGLGK TSGRGQKGQK ARKSGLTRPG FEGGQTPLYR RLPKFGNARK GFLKQEWVVL NLNKIAKLKL DKINRASLIE KQVISAKSQL PIKLIGHTKL EKPLHFEVHK VSKQALKAVE NANGSVKLLE K // ID RL34_MYCPN Reviewed; 48 AA. AC P78006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=50S ribosomal protein L34; GN Name=rpmH; OrderedLocusNames=MPN_682; ORFNames=MP160; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L34P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95808.1; -; Genomic_DNA. DR PIR; S73486; S73486. DR RefSeq; NP_110371.1; NC_000912.1. DR RefSeq; WP_010875039.1; NC_000912.1. DR ProteinModelPortal; P78006; -. DR SMR; P78006; 1-48. DR EnsemblBacteria; AAB95808; AAB95808; MPN_682. DR GeneID; 877034; -. DR KEGG; mpn:MPN682; -. DR PATRIC; 20022853; VBIMycPne110_0749. DR KO; K02914; -. DR OrthoDB; EOG6DZF71; -. DR BioCyc; MPNE272634:GJ6Z-728-MONOMER; -. DR Proteomes; UP000000808; 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 48 50S ribosomal protein L34. FT /FTId=PRO_0000187416. SQ SEQUENCE 48 AA; 5600 MW; 6398EB40913C6FB1 CRC64; MKRTYQPSKL KRAKTHGFLA RMATASGRKV LKLRRKKQRA QLTVSSER // ID RL23_MYCPN Reviewed; 237 AA. AC P75578; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=50S ribosomal protein L23; GN Name=rplW; OrderedLocusNames=MPN_167; ORFNames=MP664; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, CC and trigger factor when it is bound to the ribosome (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P 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; U00089; AAB96312.1; -; Genomic_DNA. DR PIR; S73990; S73990. DR RefSeq; NP_109855.1; NC_000912.1. DR RefSeq; WP_010874524.1; NC_000912.1. DR ProteinModelPortal; P75578; -. DR IntAct; P75578; 9. DR EnsemblBacteria; AAB96312; AAB96312; MPN_167. DR GeneID; 877178; -. DR KEGG; mpn:MPN167; -. DR PATRIC; 20021657; VBIMycPne110_0185. DR KO; K02892; -. DR OMA; CRIRNGA; -. DR OrthoDB; EOG6HTP4P; -. DR BioCyc; MPNE272634:GJ6Z-174-MONOMER; -. DR Proteomes; UP000000808; 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-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. 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 1 237 50S ribosomal protein L23. FT /FTId=PRO_0000129420. FT REGION 1 100 50S ribosomal protein L23. FT REGION 101 237 Unknown. SQ SEQUENCE 237 AA; 25839 MW; 6B98B63153E97AEE CRC64; MDVTNVLLKP VLTEKVYFNQ MGETKKYVFV VNPKASKTRV KLAFELVYGI KPLKVNTLIR KPTTIRGGSR FPGLSKLEKL AVITLPKGIA ISVTGEAPEK TDKPADKTTL KESTVKEIKD TKNSPEAVVK TAVEALQIKP TAAPVTTAPL QTVAVKVAKE VKEVKVEKPV KVEKPTKPAK VAKEAKTTKV AKETKAEKSV QTTKVAKETK TEKSAKTTKT TATKTTKTKT TKKEVKK // ID RL28_MYCPN Reviewed; 65 AA. AC P75171; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=50S ribosomal protein L28 {ECO:0000255|HAMAP-Rule:MF_00373}; GN Name=rpmB {ECO:0000255|HAMAP-Rule:MF_00373}; GN OrderedLocusNames=MPN_624; ORFNames=MP218; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95866.1; -; Genomic_DNA. DR PIR; S73544; S73544. DR RefSeq; NP_110313.1; NC_000912.1. DR RefSeq; WP_010874981.1; NC_000912.1. DR ProteinModelPortal; P75171; -. DR EnsemblBacteria; AAB95866; AAB95866; MPN_624. DR GeneID; 877270; -. DR KEGG; mpn:MPN624; -. DR PATRIC; 20022731; VBIMycPne110_0688. DR KO; K02902; -. DR OMA; GGSMRIK; -. DR OrthoDB; EOG6W727M; -. DR BioCyc; MPNE272634:GJ6Z-670-MONOMER; -. DR Proteomes; UP000000808; 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 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 65 50S ribosomal protein L28. FT /FTId=PRO_0000178510. SQ SEQUENCE 65 AA; 7531 MW; 92D0C073B34E8E52 CRC64; MAKKDQLTLR GPLYGNNRSH SKTITRRKWN VNLQPCKVKT ADGKTTRILV STRTLRTLKK HNRLS // ID RL3_MYCPN Reviewed; 287 AA. AC P75580; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=MPN_165; ORFNames=MP666; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 -!- 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; U00089; AAB96314.1; -; Genomic_DNA. DR PIR; S73992; S73992. DR RefSeq; NP_109853.1; NC_000912.1. DR RefSeq; WP_010874522.1; NC_000912.1. DR ProteinModelPortal; P75580; -. DR IntAct; P75580; 12. DR EnsemblBacteria; AAB96314; AAB96314; MPN_165. DR GeneID; 877186; -. DR KEGG; mpn:MPN165; -. DR PATRIC; 20021653; VBIMycPne110_0183. DR KO; K02906; -. DR OMA; QVWDENN; -. DR OrthoDB; EOG6WDSMH; -. DR BioCyc; MPNE272634:GJ6Z-172-MONOMER; -. DR Proteomes; UP000000808; 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 287 50S ribosomal protein L3. FT /FTId=PRO_0000077123. SQ SEQUENCE 287 AA; 31247 MW; 2B6EC905363AF259 CRC64; MEIRGIFGVK VGMSQVFTTN NERLPITVIY CEPNQVAGVK TEAKDKYSAT LLSFDTVENK KLNKPQQGFF EKNNLKPTKH LQEIRNMTGF EMGQQITPQN LFQVGEYVDV SAISKGRGFT GAIKRWNFKI GPLGHGAGYP HRFQGSVQAG RGGASAQRVF KGKKMSGHYG HEKVTVQNLR IVGFDEANML VLVSGAIAGP EGGVVLIRTA KKKPGVVKPI ELAVQTEKAP EAKPAKLSKK KQAKELAKAQ AANQQTVEAK VDTPVVEPKP TEVKKAAPVV EKKGEDK // ID RL4_MYCPN Reviewed; 212 AA. AC P75579; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=MPN_166; ORFNames=MP665; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP ANTIBIOTIC RESISTANT VARIANTS. RC STRAIN=ATCC 29342 / M129; RX PubMed=14742195; DOI=10.1128/AAC.48.2.460-465.2004; RA Pereyre S., Guyot C., Renaudin H., Charron A., Bebear C., Bebear C.M.; RT "In vitro selection and characterization of resistance to macrolides RT and related antibiotics in Mycoplasma pneumoniae."; RL Antimicrob. Agents Chemother. 48:460-465(2004). 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 -!- CAUTION: The antibiotic variants could harbor other changes as CC whole genes were not sequenced. {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; U00089; AAB96313.1; -; Genomic_DNA. DR PIR; S73991; S73991. DR RefSeq; NP_109854.1; NC_000912.1. DR RefSeq; WP_010874523.1; NC_000912.1. DR ProteinModelPortal; P75579; -. DR IntAct; P75579; 4. DR EnsemblBacteria; AAB96313; AAB96313; MPN_166. DR GeneID; 877182; -. DR KEGG; mpn:MPN166; -. DR PATRIC; 20021655; VBIMycPne110_0184. DR KO; K02926; -. DR OMA; THSILTK; -. DR OrthoDB; EOG6M0T9G; -. DR BioCyc; MPNE272634:GJ6Z-173-MONOMER; -. DR Proteomes; UP000000808; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1370.10; -; 1. DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1. DR InterPro; IPR002136; Ribosomal_L4/L1e. DR InterPro; IPR023574; Ribosomal_L4_dom. DR InterPro; IPR013005; Ribosomal_uL4/L1e. DR PANTHER; PTHR10746; PTHR10746; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03953; rplD_bact; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 212 50S ribosomal protein L4. FT /FTId=PRO_0000129244. FT VARIANT 60 60 G -> GG (after 20 antibiotic passages; FT confers resistance to various FT antibiotics). FT VARIANT 60 60 G -> GGG (also to GGGG, after 47 FT antibiotic passages; confers greater FT resistance than the above variant). FT VARIANT 70 70 H -> L (after 32, 37 and 48 antibiotic FT passages; confers resistance to various FT antibiotics in combination with a 23S FT rRNA mutation and up to 3 mutations in FT protein L22). FT VARIANT 70 70 H -> R (after 30 clindamycin passages; FT confers resistance to clindamycin and FT josamycin). SQ SEQUENCE 212 AA; 23590 MW; 58421C03A2754D0B CRC64; MAKLKLIKID GSFETEPVKL SPGLIAKELK QQPVFDAVLV EQASWRQGTH SILTKGEVRG GGKKPYKQKH TGKARQGSTR NPHFVGGGIV FGPKPNRNYS LKLNKKAHTA ALHTVWSEKL ASDNTHLVDQ NLFNKTEGKT KVMMQFLKSA KLLDKNVLFV VNTLNTNLEQ STSNIKNVQV KHLDKVSVRD LMLANALLVE KEVLKALEGK FK // ID RL7_MYCPN Reviewed; 122 AA. AC P75239; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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=MPN_539; ORFNames=MP303; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95951.1; -; Genomic_DNA. DR PIR; S73629; S73629. DR RefSeq; NP_110228.1; NC_000912.1. DR RefSeq; WP_010874896.1; NC_000912.1. DR ProteinModelPortal; P75239; -. DR IntAct; P75239; 5. DR EnsemblBacteria; AAB95951; AAB95951; MPN_539. DR GeneID; 877373; -. DR KEGG; mpn:MPN539; -. DR PATRIC; 20022555; VBIMycPne110_0601. DR KO; K02935; -. DR OMA; CVVKQDI; -. DR OrthoDB; EOG6WMJ69; -. DR BioCyc; MPNE272634:GJ6Z-584-MONOMER; -. DR Proteomes; UP000000808; 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 1 122 50S ribosomal protein L7/L12. FT /FTId=PRO_0000157553. SQ SEQUENCE 122 AA; 13106 MW; 47F048CCC1AD7C2D CRC64; MAKLDKNQLI ESLKEMTIME IDEIIKAVEE AFGVSATPVV AAGAVGGTQE AASEVTVKVT GYTDNAKLAV LKLYREIAGV GLMEAKTAVE KLPCVVKQDI KPEEAEELKK RFVEVGATVE IK // ID RL29_MYCPN Reviewed; 111 AA. AC Q50310; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=50S ribosomal protein L29; GN Name=rpmC; OrderedLocusNames=MPN_173; ORFNames=MP658; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L29P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43708.1; -; Genomic_DNA. DR EMBL; U00089; AAB96306.1; -; Genomic_DNA. DR PIR; S62803; S62803. DR RefSeq; NP_109861.1; NC_000912.1. DR RefSeq; WP_010874530.1; NC_000912.1. DR ProteinModelPortal; Q50310; -. DR IntAct; Q50310; 1. DR EnsemblBacteria; AAB96306; AAB96306; MPN_173. DR GeneID; 876851; -. DR KEGG; mpn:MPN173; -. DR PATRIC; 20021669; VBIMycPne110_0191. DR KO; K02904; -. DR OrthoDB; EOG6VTK8Z; -. DR BioCyc; MPNE272634:GJ6Z-180-MONOMER; -. DR Proteomes; UP000000808; 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 1 111 50S ribosomal protein L29. FT /FTId=PRO_0000130422. FT REGION 1 77 50S ribosomal protein L29. FT REGION 78 111 Unknown. SQ SEQUENCE 111 AA; 12974 MW; 4A9BDAC971D4FC85 CRC64; MTVAKELRQK SSEELVKLVI KLKGELLEYR FKLAHGELDK PHLINQTRRL LATILTILTE RKLNWQEEQA KYKLLTKKTN EAAVNAWKQH LEANKAKLLK SRAKREDASK K // ID RL31_MYCPN Reviewed; 97 AA. AC P78020; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; GN OrderedLocusNames=MPN_360; ORFNames=MP476; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-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; U00089; AAB96124.1; -; Genomic_DNA. DR PIR; S73802; S73802. DR RefSeq; NP_110048.1; NC_000912.1. DR RefSeq; WP_010874716.1; NC_000912.1. DR ProteinModelPortal; P78020; -. DR IntAct; P78020; 2. DR EnsemblBacteria; AAB96124; AAB96124; MPN_360. DR GeneID; 876727; -. DR KEGG; mpn:MPN360; -. DR PATRIC; 20022086; VBIMycPne110_0387. DR KO; K02909; -. DR OMA; EMITANC; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; MPNE272634:GJ6Z-380-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005840; C:ribosome; 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 97 50S ribosomal protein L31. FT /FTId=PRO_0000173128. SQ SEQUENCE 97 AA; 10959 MW; 7EC51609B3519DF2 CRC64; MKKDFHFPSQ SVSFKCASCS NSFTIESTLK QKEITIDICG KCHPFYIGEL TKQTVHGRAE KLSGKFNAGK AFLENKTPKK AKGKTEEYTK HRSLNEL // ID RL6_MYCPN Reviewed; 184 AA. AC Q50303; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; GN OrderedLocusNames=MPN_180; ORFNames=MP651; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43701.1; -; Genomic_DNA. DR EMBL; U00089; AAB96299.1; -; Genomic_DNA. DR PIR; S62827; S62827. DR RefSeq; NP_109868.1; NC_000912.1. DR RefSeq; WP_010874537.1; NC_000912.1. DR ProteinModelPortal; Q50303; -. DR IntAct; Q50303; 1. DR EnsemblBacteria; AAB96299; AAB96299; MPN_180. DR GeneID; 876780; -. DR KEGG; mpn:MPN180; -. DR PATRIC; 20021683; VBIMycPne110_0198. DR KO; K02933; -. DR OMA; LIANMVE; -. DR OrthoDB; EOG67DPRD; -. DR BioCyc; MPNE272634:GJ6Z-187-MONOMER; -. DR Proteomes; UP000000808; 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 1 184 50S ribosomal protein L6. FT /FTId=PRO_0000131061. SQ SEQUENCE 184 AA; 20589 MW; C92DC101E99C2651 CRC64; MSKIGNRTIT LDPAKVNLNF QKDHIAVKGP LGQIELKLPP NLPLKFELKD NNLQITRNNE LKQSKIFHGT YNALITNAII GVTQGFEKKL RLVGVGYRAN VEGETLNLQL GYSHPIKEKI PKGLTVKVEK NTEITISGIS KELVGQFATE VRKWRKPEPY KGKGVLYFDE VIVRKAGKTA EGKK // ID RL9_MYCPN Reviewed; 149 AA. AC P75540; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=MPN_231; ORFNames=MP600; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96248.1; -; Genomic_DNA. DR PIR; S73926; S73926. DR RefSeq; NP_109919.1; NC_000912.1. DR RefSeq; WP_010874588.1; NC_000912.1. DR ProteinModelPortal; P75540; -. DR IntAct; P75540; 2. DR EnsemblBacteria; AAB96248; AAB96248; MPN_231. DR GeneID; 877076; -. DR KEGG; mpn:MPN231; -. DR PATRIC; 20021787; VBIMycPne110_0250. DR KO; K02939; -. DR OMA; CKDGKAN; -. DR OrthoDB; EOG6D8BH0; -. DR BioCyc; MPNE272634:GJ6Z-238-MONOMER; -. DR Proteomes; UP000000808; 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 1 149 50S ribosomal protein L9. FT /FTId=PRO_0000176653. SQ SEQUENCE 149 AA; 17152 MW; EED94AD27A4F08DF CRC64; MKVILKQDVS NLGKRFDVVD VKDGYAIHFL FPKKLAAPLT KKSLQDRDLF LKKQQEHYEI NKALSHKLKE VIEQTELHFS LKEHNGRPYG SIITKQIINQ AHTKGMALQK FMFKDNVRLG FGDHEITLHI FEDTTAVLKV KVTPDNGVK // ID RL27_MYCPN Reviewed; 104 AA. AC P75458; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=50S ribosomal protein L27 {ECO:0000255|HAMAP-Rule:MF_00539}; GN Name=rpmA {ECO:0000255|HAMAP-Rule:MF_00539}; GN OrderedLocusNames=MPN_327; ORFNames=MP509; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96157.1; -; Genomic_DNA. DR PIR; S73835; S73835. DR RefSeq; NP_110015.1; NC_000912.1. DR RefSeq; WP_010874683.1; NC_000912.1. DR ProteinModelPortal; P75458; -. DR SMR; P75458; 16-87. DR IntAct; P75458; 5. DR EnsemblBacteria; AAB96157; AAB96157; MPN_327. DR GeneID; 876951; -. DR KEGG; mpn:MPN327; -. DR PATRIC; 20022008; VBIMycPne110_0351. DR KO; K02899; -. DR OMA; LIMNLQL; -. DR OrthoDB; EOG6N94H6; -. DR BioCyc; MPNE272634:GJ6Z-344-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00539; Ribosomal_L27; 1. DR InterPro; IPR001684; Ribosomal_L27. DR InterPro; IPR018261; Ribosomal_L27_CS. DR PANTHER; PTHR15893; PTHR15893; 1. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR TIGRFAMs; TIGR00062; L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 104 50S ribosomal protein L27. FT /FTId=PRO_0000181128. SQ SEQUENCE 104 AA; 11504 MW; 7C1C8587544940D4 CRC64; MNNKYFLTKI DLQFFASKKG VGSTKNGRDS HAKRLGAKKA DGQMIRTGQI IYRQRGTRVY PGVNVGLGSD DTLFALSDGL VKYQKFGPKQ GKTRVSVVKH KLDA // ID RL331_MYCPN Reviewed; 53 AA. AC P78015; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=50S ribosomal protein L33 1; GN Name=rpmG1; Synonyms=rpmG; OrderedLocusNames=MPN_471; ORFNames=MP370; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75321:MPN_462; NbExp=1; IntAct=EBI-2260200, EBI-2260204; CC -!- SIMILARITY: Belongs to the ribosomal protein L33P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96018.1; -; Genomic_DNA. DR PIR; S73696; S73696. DR RefSeq; NP_110159.1; NC_000912.1. DR RefSeq; WP_010874827.1; NC_000912.1. DR ProteinModelPortal; P78015; -. DR IntAct; P78015; 1. DR EnsemblBacteria; AAB96018; AAB96018; MPN_471. DR GeneID; 877381; -. DR KEGG; mpn:MPN471; -. DR PATRIC; 20022364; VBIMycPne110_0509. DR KO; K02913; -. DR OMA; STRLGCN; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; MPNE272634:GJ6Z-512-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 53 50S ribosomal protein L33 1. FT /FTId=PRO_0000170190. SQ SEQUENCE 53 AA; 6282 MW; 461A08C51CBAF66A CRC64; MAVKRSTRLG CNDCREINYL TFKNVKKNPE KLALNKFCSR CRKVVVHKEV KRK // ID RL35_MYCPN Reviewed; 59 AA. AC P75447; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=50S ribosomal protein L35; GN Name=rpmI; OrderedLocusNames=MPN_116; ORFNames=MP038; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L35P 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; U00089; AAG34733.1; -; Genomic_DNA. DR PIR; S73364; S73364. DR RefSeq; NP_109804.1; NC_000912.1. DR RefSeq; WP_010874473.1; NC_000912.1. DR ProteinModelPortal; P75447; -. DR IntAct; P75447; 1. DR EnsemblBacteria; AAG34733; AAG34733; MPN_116. DR GeneID; 877369; -. DR KEGG; mpn:MPN116; -. DR PATRIC; 20021531; VBIMycPne110_0123. DR KO; K02916; -. DR OMA; VIKKKSH; -. DR OrthoDB; EOG651T3B; -. DR BioCyc; MPNE272634:GJ6Z-122-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 59 50S ribosomal protein L35. FT /FTId=PRO_0000177384. SQ SEQUENCE 59 AA; 6771 MW; 316D0F1672843AEE CRC64; MKVKSAAKKR FKLTKSGQIK RKHAYTSHLA PHKTTKQKRH LRKQGTVSAS DFKRIGNLI // ID RL2_MYCPN Reviewed; 287 AA. AC P75577; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; GN OrderedLocusNames=MPN_168; ORFNames=MP663; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96311.1; -; Genomic_DNA. DR PIR; S73989; S73989. DR RefSeq; NP_109856.1; NC_000912.1. DR RefSeq; WP_010874525.1; NC_000912.1. DR ProteinModelPortal; P75577; -. DR SMR; P75577; 65-203. DR IntAct; P75577; 2. DR EnsemblBacteria; AAB96311; AAB96311; MPN_168. DR GeneID; 876824; -. DR KEGG; mpn:MPN168; -. DR PATRIC; 20021659; VBIMycPne110_0186. DR KO; K02886; -. DR OMA; HNRGVTM; -. DR OrthoDB; EOG6TR0J1; -. DR BioCyc; MPNE272634:GJ6Z-175-MONOMER; -. DR Proteomes; UP000000808; 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 PANTHER; PTHR13691:SF5; PTHR13691:SF5; 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 1 287 50S ribosomal protein L2. FT /FTId=PRO_0000129585. SQ SEQUENCE 287 AA; 31902 MW; 9F16759C40725535 CRC64; MPIKKIISRS NSGIHHSTVI DYKKLLTTNK NKPEKSLLVT LKKHGGRNNQ GKITVRHQGG RNKRKYRIID FKRTHYDNIE ATVKSIEYDP NRSCFVSLIT YANGAKSYII SPDGIKVGDK ILASEHPIDI KPGFSMPLAF IPEGTQVHNI ELHPKGGGQI ARSAGSYARI LGQDETGKYV ILQLLSGETR KFLKECRATV GVVSNLDHNL VVIGKAGRNR HRGIRPTVRG SAMNPNDHPH GGGEGRSPVG RDAPRTPWGK RHMGVKTRNM KKASTNLIIR NRKGEQY // ID RL32_MYCPN Reviewed; 57 AA. AC P75238; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 78. DE RecName: Full=50S ribosomal protein L32; GN Name=rpmF; OrderedLocusNames=MPN_540; ORFNames=MP302; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L32P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95950.1; -; Genomic_DNA. DR PIR; S73628; S73628. DR RefSeq; NP_110229.1; NC_000912.1. DR RefSeq; WP_010874897.1; NC_000912.1. DR ProteinModelPortal; P75238; -. DR IntAct; P75238; 2. DR EnsemblBacteria; AAB95950; AAB95950; MPN_540. DR GeneID; 877240; -. DR KEGG; mpn:MPN540; -. DR PATRIC; 20022557; VBIMycPne110_0602. DR KO; K02911; -. DR OMA; CSCGMYG; -. DR OrthoDB; EOG6VMTT4; -. DR BioCyc; MPNE272634:GJ6Z-585-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00340; Ribosomal_L32; 1. DR InterPro; IPR002677; Ribosomal_L32p. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01783; Ribosomal_L32p; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01031; rpmF_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 57 50S ribosomal protein L32. FT /FTId=PRO_0000172370. SQ SEQUENCE 57 AA; 6623 MW; 60D0E826E5C42868 CRC64; MAVQQRRSSK HRRDKRRSHD ALTAQALSVC QKCGKKKLFH RVCSCGMYGD LRVKKAY // ID RL332_MYCPN Reviewed; 48 AA. AC P56850; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=50S ribosomal protein L33 2; GN Name=rpmG2; OrderedLocusNames=MPN_069; ORFNames=MP085.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L33P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34736.1; -; Genomic_DNA. DR RefSeq; NP_109757.1; NC_000912.1. DR RefSeq; WP_010874426.1; NC_000912.1. DR ProteinModelPortal; P56850; -. DR EnsemblBacteria; AAG34736; AAG34736; MPN_069. DR GeneID; 877273; -. DR KEGG; mpn:MPN069; -. DR PATRIC; 20021417; VBIMycPne110_0070. DR KO; K02913; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; MPNE272634:GJ6Z-71-MONOMER; -. DR Proteomes; UP000000808; 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; IPR011332; Ribosomal_zn-bd. DR Pfam; PF00471; Ribosomal_L33; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01023; rpmG_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 48 50S ribosomal protein L33 2. FT /FTId=PRO_0000170191. SQ SEQUENCE 48 AA; 5863 MW; 93A1A3157098ABED CRC64; MRKKIIFVCQ DCLSRNYVMS WSKQVLNRLI INKYCKHCNQ KTKHLDSF // ID RL36_MYCPN Reviewed; 37 AA. AC P52864; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=50S ribosomal protein L36 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ {ECO:0000255|HAMAP-Rule:MF_00251}; GN OrderedLocusNames=MPN_188; ORFNames=MP643; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P23568:tuf; NbExp=1; IntAct=EBI-2259193, EBI-2259072; 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; U34795; AAC43693.1; -; Genomic_DNA. DR EMBL; U00089; AAB96291.1; -; Genomic_DNA. DR PIR; S62820; S62820. DR RefSeq; NP_109876.1; NC_000912.1. DR RefSeq; WP_010874545.1; NC_000912.1. DR ProteinModelPortal; P52864; -. DR SMR; P52864; 1-37. DR IntAct; P52864; 1. DR EnsemblBacteria; AAB96291; AAB96291; MPN_188. DR GeneID; 877068; -. DR KEGG; mpn:MPN188; -. DR PATRIC; 20021699; VBIMycPne110_0206. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR BioCyc; MPNE272634:GJ6Z-195-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 37 50S ribosomal protein L36. FT /FTId=PRO_0000126218. SQ SEQUENCE 37 AA; 4386 MW; 4DECEB0CC6B18324 CRC64; MKVRASVKPI CKDCKIIKRH QIVRVICKTQ KHKQRQG // ID RL5_MYCPN Reviewed; 180 AA. AC Q50306; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=MPN_177; ORFNames=MP654; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43704.1; -; Genomic_DNA. DR EMBL; U00089; AAB96302.1; -; Genomic_DNA. DR PIR; S62829; S62829. DR RefSeq; NP_109865.1; NC_000912.1. DR RefSeq; WP_010874534.1; NC_000912.1. DR ProteinModelPortal; Q50306; -. DR SMR; Q50306; 1-179. DR IntAct; Q50306; 4. DR EnsemblBacteria; AAB96302; AAB96302; MPN_177. DR GeneID; 876962; -. DR KEGG; mpn:MPN177; -. DR PATRIC; 20021677; VBIMycPne110_0195. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR BioCyc; MPNE272634:GJ6Z-184-MONOMER; -. DR Proteomes; UP000000808; 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 1 180 50S ribosomal protein L5. FT /FTId=PRO_0000124954. SQ SEQUENCE 180 AA; 20240 MW; D22BCFC36B6D7410 CRC64; MNNLKAHYQK TIAKELQKSF AFSSIMQVPR LEKIVINMGV GDAIRDSKFL ESALNELHLI SGQKPVATKA KNAISTYKLR AGQLIGCKVT LRGERMWAFL EKLIYVALPR VRDFRGLSLK SFDGRGNYTI GIKEQIIFPE IVYDDIKRIR GFDVTLVTST NKDSEALALL RALNLPLVKG // ID RNR_MYCPN Reviewed; 726 AA. AC P75529; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895}; DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895}; DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895}; DE AltName: Full=VacB protein homolog; GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB; GN OrderedLocusNames=MPN_243; ORFNames=MP589; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside CC monophosphates and is involved in maturation of structured RNAs. CC {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. {ECO:0000255|HAMAP- CC Rule:MF_01895}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|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; U00089; AAB96237.1; -; Genomic_DNA. DR PIR; S73915; S73915. DR RefSeq; NP_109931.1; NC_000912.1. DR RefSeq; WP_010874600.1; NC_000912.1. DR ProteinModelPortal; P75529; -. DR IntAct; P75529; 1. DR EnsemblBacteria; AAB96237; AAB96237; MPN_243. DR GeneID; 877231; -. DR KEGG; mpn:MPN243; -. DR PATRIC; 20021811; VBIMycPne110_0262. DR KO; K12573; -. DR OMA; IENFVVF; -. DR OrthoDB; EOG6Q5NRD; -. DR BioCyc; MPNE272634:GJ6Z-250-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01895; RNase_R; 1. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; 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; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 3. 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; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding. FT CHAIN 1 726 Ribonuclease R. FT /FTId=PRO_0000166409. FT DOMAIN 645 726 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01895}. SQ SEQUENCE 726 AA; 83219 MW; 6A58508593BE0596 CRC64; MKVLTDLQKR IFAIVKKENG KPIPPGIVVR MMENQAGFPG KQQVYRAIDD LLEWHIFRKS GGATNQLLIN YELADPVLDQ KFQGILNLGN KNTGFVRPLD DDKTVYYIHF SNLAGALDGD LVEFCPLDKP QVGDKFDAAV LKIVKRSRVL YAGNFLIEYS DFGQEFRIVA DNPRFYLTPI VNKASVPAEL ESNTKVAFQI DEYDPANNLC KVSIQQILGN NDEPLINLKA IMLDHSIVFE DNDVVEQQAA KLQFDEKEQS KPYRKDLTEL AFVTIDPATS KDLDDAIYVK RTDKGFVLYV AIADVAYYVQ RNSELDIEAR HKTSSIYLPG YYVVPMLPER LSNELCSLNP NEKRYVVVCE LNFDHEARLN FSEVYPATIV SQRRFAYSEV NDWLEDSDAL KDESATVLES LKAGFTLSEL IAEQRKKKGT IDLSHSETEV VVDQNYYPIE IRFLTHGKAE TMIENLMVVA NEAVAWTLTN HKVHLPYRVH PRPSKKKLQM LLENIVELKI TQPNFVLDTV TSTQIAAWLK ENKDNPSYDI FVILLLRTLG KAFYIVNPLI HFSIGSHHYT HFTSPIRRYA DLTVHRLLWM NLFTPERFTD TEREQLNAEL EQICETINDT EIKINGCERT ANDYLTTLYL SKQVGQTFHG FISAITSFGI FMRMDENNFD GLIKITSIPE DFFVFEKDRM VLRGKRTNKV FRIGDRLTAK LTEIDTVQKR AILTLV // ID RNC_MYCPN Reviewed; 282 AA. AC P75233; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104}; DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104}; GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=MPN_545; GN ORFNames=MP297; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 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; U00089; AAB95945.1; -; Genomic_DNA. DR PIR; S73623; S73623. DR RefSeq; NP_110234.1; NC_000912.1. DR RefSeq; WP_010874902.1; NC_000912.1. DR ProteinModelPortal; P75233; -. DR EnsemblBacteria; AAB95945; AAB95945; MPN_545. DR GeneID; 876735; -. DR KEGG; mpn:MPN545; -. DR PATRIC; 20022567; VBIMycPne110_0607. DR KO; K03685; -. DR OMA; HEDVSES; -. DR OrthoDB; EOG6T1WVS; -. DR BioCyc; MPNE272634:GJ6Z-590-MONOMER; -. DR Proteomes; UP000000808; 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:0003723; F:RNA binding; IEA:InterPro. 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 HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 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 rRNA processing; tRNA processing. FT CHAIN 1 282 Ribonuclease 3. FT /FTId=PRO_0000180411. FT DOMAIN 18 141 RNase III. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT ACT_SITE 63 63 {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 130 130 {ECO:0000255|HAMAP-Rule:MF_00104}. FT METAL 59 59 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 127 127 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 130 130 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. SQ SEQUENCE 282 AA; 32653 MW; 47C2BC66F7450D8C CRC64; MKNKKDKTQK PKVIDEKFVA FFKSLNIEPQ NWQFYEDAFV HSSYVNENED ARASYDRLEF LGDALIDFIV AKKLFELYPN YNEGMLTRTK IEIVKGENLN RIGKELNFGN FIKLGKGMPY TETLFGDVLE ALVAAIYEDL GIEKANQFVE EHIFKKTYSE ILKYNFFSLF QEQKLPEPRV RVSLTSNNLV LSIIELNGDI IWSQAVPNSK HYDDKSVLEH NAMSAFTQFL KSGKGINFFS DIKNKLDSQK PMRALTVRPK KINWKARKPK LKALKNKVKA DS // ID RNY_MYCPN Reviewed; 493 AA. AC P75506; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335}; DE Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335}; GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=MPN_269; GN ORFNames=A65_orf493, MP564; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay. CC {ECO:0000255|HAMAP-Rule:MF_00335}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00335}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96212.1; -; Genomic_DNA. DR PIR; S73890; S73890. DR RefSeq; NP_109957.1; NC_000912.1. DR RefSeq; WP_010874626.1; NC_000912.1. DR ProteinModelPortal; P75506; -. DR IntAct; P75506; 7. DR EnsemblBacteria; AAB96212; AAB96212; MPN_269. DR GeneID; 876964; -. DR KEGG; mpn:MPN269; -. DR PATRIC; 20021863; VBIMycPne110_0288. DR KO; K18682; -. DR OMA; KYTIANH; -. DR OrthoDB; EOG6QCD98; -. DR BioCyc; MPNE272634:GJ6Z-276-MONOMER; -. DR Proteomes; UP000000808; 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:0004521; F:endoribonuclease 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 Gene3D; 1.10.3210.10; -; 1. DR HAMAP; MF_00335; RNase_Y; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR017705; Ribonuclease_Y. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Endonuclease; Hydrolase; Membrane; KW Nuclease; Reference proteome; RNA-binding; Transmembrane; KW Transmembrane helix. FT CHAIN 1 493 Ribonuclease Y. FT /FTId=PRO_0000163784. FT TRANSMEM 19 39 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00335}. FT DOMAIN 172 241 KH. {ECO:0000255|HAMAP-Rule:MF_00335}. FT DOMAIN 300 391 HD. {ECO:0000255|HAMAP-Rule:MF_00335}. SQ SEQUENCE 493 AA; 56527 MW; E2D6DE7C8E2FE054 CRC64; MSAKLTLESI AKTFAETSIF AILFLIIVIL NLGLLVFLAY QYRVYKKKQR ANLTKQTYNN DYGQIVNLKQ QNGAKIKELA NLKDQLSELG QKFNTTLSEI INKPLVNVID EYLDEQFKQA ANFREAELNA VLDSNDQKTV FHKRLFNKFH FGVDKLANIN VKNPLNLCWV DSASFTVIES DFRKLNGVGG INKKLLIEKL RIEDIIFTNI DKKYYEVQIL SDSPVKVQKT VLTIRNILIN DYVDNEKIES YAREANGYFN DHCKLIGKQV LERLNIFEIS PKLHKFFGLL AFRYSFGQNV LSHCLETGFL TAYLALLVNF KPDVALKCGL YHDIGKADDE NGKKNHTVTG AKIGDEFYFE NDVKYTIANH HNKNVDNVYC RLTQIGDKLS AGRLGARSDS SVLFSQLKQE LKQIVEETLA QFKTTILLGQ SGRRLVIWLE TNQHNNIIDN QQLTDLATTI KSKIVQNNIT NRFPIKVVLR YNFEHSFDTK DKN // ID RNPA_MYCPN Reviewed; 118 AA. AC P75111; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. 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=MPN_681; ORFNames=MP161; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95809.1; -; Genomic_DNA. DR PIR; S73487; S73487. DR RefSeq; NP_110370.1; NC_000912.1. DR RefSeq; WP_010875038.1; NC_000912.1. DR ProteinModelPortal; P75111; -. DR EnsemblBacteria; AAB95809; AAB95809; MPN_681. DR GeneID; 876752; -. DR KEGG; mpn:MPN681; -. DR PATRIC; 20022851; VBIMycPne110_0748. DR KO; K03536; -. DR OMA; TFINAYF; -. DR OrthoDB; EOG654P5P; -. DR BioCyc; MPNE272634:GJ6Z-727-MONOMER; -. DR BRENDA; 3.1.26.5; 3534. DR Proteomes; UP000000808; 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 1 118 Ribonuclease P protein component. FT /FTId=PRO_0000198492. SQ SEQUENCE 118 AA; 14003 MW; 7B90F2E4A62CCA93 CRC64; MSAKTKHHLR DRKVFAALLR SKRRFFSTFL MAYFMPNRVR TWRAAVSISK TKYKLAVERN LIRRQVKAIM REQFCNLNAV DVLVIINQGF LELTFKEKQT IFLNLCQKLQ ELDAPKPK // ID RPIB_MYCPN Reviewed; 152 AA. AC P53527; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable ribose-5-phosphate isomerase B; DE EC=5.3.1.6; DE AltName: Full=Phosphoriboisomerase B; GN Name=rpiB; OrderedLocusNames=MPN_595; ORFNames=MP247; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative CC stage): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- INTERACTION: CC P75506:MPN_269; NbExp=1; IntAct=EBI-2261091, EBI-2260047; CC -!- SIMILARITY: Belongs to the LacAB/RpiB 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; U43738; AAC43662.1; -; Genomic_DNA. DR EMBL; U00089; AAB95895.1; -; Genomic_DNA. DR PIR; S62852; S62852. DR RefSeq; NP_110284.1; NC_000912.1. DR RefSeq; WP_010874952.1; NC_000912.1. DR ProteinModelPortal; P53527; -. DR IntAct; P53527; 2. DR EnsemblBacteria; AAB95895; AAB95895; MPN_595. DR GeneID; 877130; -. DR KEGG; mpn:MPN595; -. DR PATRIC; 20022671; VBIMycPne110_0658. DR KO; K01808; -. DR OMA; ISVGARM; -. DR OrthoDB; EOG679TJ4; -. DR BioCyc; MPNE272634:GJ6Z-641-MONOMER; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1400.10; -; 1. DR InterPro; IPR004785; RpiB. DR InterPro; IPR003500; RpiB_LacA_LacB. DR PANTHER; PTHR30345; PTHR30345; 1. DR Pfam; PF02502; LacAB_rpiB; 1. DR PIRSF; PIRSF005384; RpiB_LacA_B; 1. DR SUPFAM; SSF89623; SSF89623; 1. DR TIGRFAMs; TIGR01120; rpiB; 1. DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 152 Probable ribose-5-phosphate isomerase B. FT /FTId=PRO_0000208166. FT REGION 71 76 Substrate binding. {ECO:0000250}. FT ACT_SITE 70 70 Proton acceptor. {ECO:0000255}. FT ACT_SITE 103 103 Proton donor. {ECO:0000250}. FT BINDING 13 13 Substrate. {ECO:0000250}. FT BINDING 114 114 Substrate. {ECO:0000250}. FT BINDING 137 137 Substrate. {ECO:0000250}. FT BINDING 141 141 Substrate. {ECO:0000250}. SQ SEQUENCE 152 AA; 16699 MW; 0A7244F0C1ABE363 CRC64; MQMNHPIYIA SDHTGLELKS LVIKHLEQQK LQVIDLGPTE LDPLDDYPDY AFLLAQTMQA NPNSLGILIC GTGVGVCMAA NKAKGILAAL VVDSKTAALA RQHDDANVLC LSSRFVVPEE NIKIVDEFLQ AQFEGGRHSK RVGKIIAYER EK // ID RPOA_MYCPN Reviewed; 327 AA. AC Q50295; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 101. 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=MPN_191; ORFNames=MP640; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43690.1; -; Genomic_DNA. DR EMBL; U00089; AAB96288.1; -; Genomic_DNA. DR PIR; S62817; S62817. DR RefSeq; NP_109879.1; NC_000912.1. DR RefSeq; WP_010874548.1; NC_000912.1. DR ProteinModelPortal; Q50295; -. DR IntAct; Q50295; 21. DR EnsemblBacteria; AAB96288; AAB96288; MPN_191. DR GeneID; 876896; -. DR KEGG; mpn:MPN191; -. DR PATRIC; 20021705; VBIMycPne110_0209. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR BioCyc; MPNE272634:GJ6Z-198-MONOMER; -. DR Proteomes; UP000000808; 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 1 327 DNA-directed RNA polymerase subunit FT alpha. FT /FTId=PRO_0000175342. FT REGION 1 243 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. FT REGION 260 327 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. SQ SEQUENCE 327 AA; 36662 MW; D8FDF2FE075A3764 CRC64; MEKFLKYEIK VNNEQARANP NYGIFEVGPL ESGFVITIGN AMRRVLLSCI PGASVFALSI SGAKQEFAAV EGMKEDVTEV VLNFKQLVVK ISDLLFEDGE MVEPPLERWP LLTVTAEKAG PVYAKDLECP AGFEVVNKDL YLFSLQTDKK VTVNVYVKQG RGFVTFLENR EMINSLGIIA TDSNFSPVLH CGYEVQELKT SKQKITDHLT FKIATNGAIS AVDAFAMAAK ILIEHLNPIV NVNESIKALN IIQEKAEERR VRSFAKQIEE LDFTVRTFNC LKRSGIHTLQ ELLSKSLADI REIRNLGKKS EREIIKKVHE LGLKLRS // ID RPOC_MYCPN Reviewed; 1290 AA. AC P75271; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. 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=MPN_515; ORFNames=MP327; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95975.1; -; Genomic_DNA. DR PIR; S73653; S73653. DR RefSeq; NP_110203.1; NC_000912.1. DR RefSeq; WP_010874871.1; NC_000912.1. DR ProteinModelPortal; P75271; -. DR IntAct; P75271; 14. DR EnsemblBacteria; AAB95975; AAB95975; MPN_515. DR GeneID; 876810; -. DR KEGG; mpn:MPN515; -. DR PATRIC; 20022484; VBIMycPne110_0569. DR KO; K03046; -. DR OMA; YFAAYMI; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; MPNE272634:GJ6Z-556-MONOMER; -. DR Proteomes; UP000000808; 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; 1. 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 1290 DNA-directed RNA polymerase subunit FT beta'. FT /FTId=PRO_0000067763. SQ SEQUENCE 1290 AA; 144895 MW; 0A52BC2D70EA5146 CRC64; MTKRNKKNNK LYKNIKAIKL SIASNDTILN WSEGEVTKAE TINYKSLKPE PGGLFDEAIF GPVKDYECAC GKFKKIKYRG VRCDRCGVWV TESIVRRERM GHIALVSPVA HIWMSKELPS PSKISLVLNI SYKEVEQVLY FVNYIVLDTG KIKDPKIMPF KFKEVLDLAG KGSLTTRQKM RRVIGYIFRN LIKNRSSEDY RKGKIFYESL KNSSLPFSLN DAFNYIKKYT GFRVGIGAEA ILELLNKIDL NYEFSKLNDA LRKAKKDSVE DAKVKKILRQ LETISWFRNS KLHPKNMILH TVPVIPPDIR PIIQLDGAKF TTSDINNFYR RVIIRNDRLR RILEDGTVPA IVVNNEKRLL QESVDALFDN SSRHKPALSK DKRSLKSLTD RLKGKQGLFR HNLLGKRVDY SGRSVIVVGP ELKMYEVGIP ALMILKLFKP FIIHGLINKF DSNGNEIRPI ASSIRQAEDM IKNQDDLIWG IVYDVIKDRP VLLNRAPTLH RLGIQAFEPR IVDGKAIRLH PLVTTAFNAD FDGDQMAVHV PLSENAVNEA RAILLASKHI LGLKDGRPIV TPTQDMVLGN YYLTTERKGQ TGEGIIFGTV HEARAAYEAG KVHLHAIVGI STKAFPNKHF EAQGTLITTV GKIIFNDVLG DNIPYINEGE FDEHACPQKF IVPPSGDVRA AIAAHQVLPA FGKKVISKLI DLLYTVVEFK DLPRILENIK ALGFKYSTHS STTVSVFDIP KYSNKQQYFD EADQQVLKYK QFYNKGLLTD DERYKRVVKL WNGVKEKVSS EIQDLIKREE YRDNSIVVMA DSGARGNISN FTQLFGMRGL MSKSFNYERN NQSKIIKDTI EVPIKHSFLE GLTINEYFNS SYGARKGMTD TAMKTAKSGY MTRKLVDATH ELIINHDDCG TRKGIVVEAI VETKTRSLVE SLFDRIVNRY TIGPILDPET KAEIVPANSL ITQELAKQIC ATSIKQVLVR SVIYCERENG VCQYCFGVDL STGKLVELGT AVGVIAAQSI GEPGTQLTMR TFHTGGVSTE NNLAQGFERL KQIFEVVAPK DYERCVISEV KGVVKSITTT QNAQEVLIES SVDERTYSIP FSAQLRVKVG DAVELGSKIT EGSIDIRQLL RVAGIQRVRQ YMIVEIQKVY RIQGIEIADK YVEIIIRQLT SLLQVTDAGS SNLFVGQLVH SHHLNELNKS LLLSGKMPVI AINQVFGIDE AASKSNSFLS AASFQDTKKI LTDAAVKTQV DYLLGLKENV IIGGKIPAGT GFLTDEELAY LGAKTVQEEY // ID RPOE_MYCPN Reviewed; 144 AA. AC P75090; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 13-APR-2016, entry version 79. DE RecName: Full=Probable DNA-directed RNA polymerase subunit delta; DE AltName: Full=RNAP delta factor; GN Name=rpoE; OrderedLocusNames=MPN_024; ORFNames=MP130; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Participates in both the initiation and recycling phases CC of transcription. In the presence of the delta subunit, RNAP CC displays an increased specificity of transcription, a decreased CC affinity for nucleic acids, and an increased efficiency of RNA CC synthesis because of enhanced recycling (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: RNAP is composed of a core of 2 alpha, a beta and a beta' CC subunits. The core is associated with a delta subunit and one of CC several sigma factors (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95778.1; 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; U00089; AAB95778.1; ALT_INIT; Genomic_DNA. DR PIR; S73456; S73456. DR RefSeq; NP_109712.1; NC_000912.1. DR RefSeq; WP_010874381.1; NC_000912.1. DR IntAct; P75090; 1. DR EnsemblBacteria; AAB95778; AAB95778; MPN_024. DR GeneID; 876869; -. DR KEGG; mpn:MPN024; -. DR PATRIC; 20021323; VBIMycPne110_0023. DR KO; K03048; -. DR OMA; KVENWIG; -. DR OrthoDB; EOG6S26DH; -. DR BioCyc; MPNE272634:GJ6Z-26-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; 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:InterPro. DR HAMAP; MF_00357; RNApol_bact_RpoE; 1. DR InterPro; IPR007759; HB1/Asxl_HTH. DR InterPro; IPR029757; RpoE. DR Pfam; PF05066; HARE-HTH; 1. DR TIGRFAMs; TIGR04567; RNAP_delt_lowGC; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 144 Probable DNA-directed RNA polymerase FT subunit delta. FT /FTId=PRO_0000204319. FT COMPBIAS 93 144 Asp/Glu-rich (acidic). SQ SEQUENCE 144 AA; 17174 MW; 0157775EAD9E25A9 CRC64; MQVEYLDLIS QAKEIAETQF KAEPFSFDAI WKEVVKHFKI SKQDEPNLIS RFYQDFLEDP NFVYLGERNW KLRDFMKFDE WNKISQAMFV TKEIFEEGYE DLSNKKKENE EEVNDFIMGN DGDDNSTGDE IVQGLINDFR DDNQ // ID RNJ_MYCPN Reviewed; 569 AA. AC P75497; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491}; DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491}; GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=MPN_280; GN ORFNames=A65_orf569, MP555; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly CC endoonuclease activity. Involved in maturation of rRNA and in some CC organisms also mRNA maturation and/or decay (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491}; CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if CC Zn(2+) or Mg(2+) is physiologically important. {ECO:0000255|HAMAP- CC Rule:MF_01491}; CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. CC {ECO:0000255|HAMAP-Rule:MF_01491}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC RNA-metabolizing metallo-beta-lactamase-like family. Bacterial CC RNase J subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96203.1; -; Genomic_DNA. DR PIR; S73881; S73881. DR RefSeq; NP_109968.1; NC_000912.1. DR RefSeq; WP_010874637.1; NC_000912.1. DR ProteinModelPortal; P75497; -. DR IntAct; P75497; 6. DR EnsemblBacteria; AAB96203; AAB96203; MPN_280. DR GeneID; 877383; -. DR KEGG; mpn:MPN280; -. DR PATRIC; 20021887; VBIMycPne110_0300. DR KO; K12574; -. DR OMA; PYHGEYR; -. DR OrthoDB; EOG6P5ZDC; -. DR BioCyc; MPNE272634:GJ6Z-287-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro. DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01491; RNase_J_bact; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR InterPro; IPR004613; RNase_J. DR InterPro; IPR030854; RNase_J_bac. DR InterPro; IPR001587; RNase_J_CS. DR PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1. DR Pfam; PF00753; Lactamase_B; 1. DR Pfam; PF07521; RMMBL; 1. DR PIRSF; PIRSF004803; RnjA; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00649; MG423; 1. DR PROSITE; PS01292; UPF0036; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Exonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; RNA-binding; KW rRNA processing; Zinc. FT CHAIN 1 569 Ribonuclease J. FT /FTId=PRO_0000215272. FT REGION 373 377 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 81 81 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 83 83 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 85 85 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 86 86 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 150 150 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 172 172 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 172 172 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 399 399 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. SQ SEQUENCE 569 AA; 64086 MW; FB6A5470369B00DD CRC64; MIKDFDPSEF VGKTPTKIFA FGGIQEVGKN MYGIEYDDEI IIIDCGIKFA SDDLLGIDGI IPSFEYLIEN QAKVKALFIT HGHEDHIGGV PYLLKQVDVP VIYAPRIAAS LILKKVNEHK DAKLNKVVVY DDFSNFETKH FKIDFYRVNH SIPDAFGVCV QTPNGNIVES GDFRFDFAAG GEMLDVHKVV KIAERNVHVF MCETTNAEIP GFSQSEKLIY RNINKIIKEA RGRVILTTFA SNITRINEII EIAVNNKRKV CLLGKSMDVN VNISRKIGLM DIDSNDIVEV RDIKNYPDRS ILILCTGSQG EDSAALNTMA RGKHNWVSLK STDTIIMSSN PIPGNYAAVE NLLNELSKYG VTIFENSPNM KLHASGHATQ QELQLMLNLV FPRYLIPIHG EYKMMRTIKN IAQECGINGD DVGLLANGQV MYLIDGKLYY SGEVINADPI YIESRNSSPD LARVIKQRQI LSREGMFAVI VVFDKNNNIL GMPTLITRGC FFALDSSPLM TKITHSIKRG LENVIQNKRF NTREQMIKEL KRVCKETVSY FIWKNKSRNP LISTVLSWV // ID RNM5_MYCPN Reviewed; 178 AA. AC P75045; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Ribonuclease M5 {ECO:0000255|HAMAP-Rule:MF_01469}; DE EC=3.1.26.8 {ECO:0000255|HAMAP-Rule:MF_01469}; DE AltName: Full=RNase M5 {ECO:0000255|HAMAP-Rule:MF_01469}; DE AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000255|HAMAP-Rule:MF_01469}; GN Name=rnmV {ECO:0000255|HAMAP-Rule:MF_01469}; GN OrderedLocusNames=MPN_072; ORFNames=D09_orf178, MP083; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for correct processing of both the 5' and 3' CC ends of 5S rRNA precursor. Cleaves both sides of a double-stranded CC region yielding mature 5S rRNA in one step. {ECO:0000255|HAMAP- CC Rule:MF_01469}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 21 CC and 42 nucleotides, respectively, from the 5'- and 3'-termini of a CC 5S-rRNA precursor. {ECO:0000255|HAMAP-Rule:MF_01469}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01469}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01469}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01469}. CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. CC {ECO:0000255|HAMAP-Rule:MF_01469}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_01469}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95731.1; -; Genomic_DNA. DR PIR; S73409; S73409. DR RefSeq; NP_109760.1; NC_000912.1. DR RefSeq; WP_010874429.1; NC_000912.1. DR ProteinModelPortal; P75045; -. DR IntAct; P75045; 3. DR EnsemblBacteria; AAB95731; AAB95731; MPN_072. DR GeneID; 877159; -. DR KEGG; mpn:MPN072; -. DR PATRIC; 20021423; VBIMycPne110_0073. DR KO; K05985; -. DR OMA; ITKNANQ; -. DR OrthoDB; EOG6XQ3R3; -. DR BioCyc; MPNE272634:GJ6Z-74-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043822; F:ribonuclease M5 activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01469; RNase_M5; 1. DR InterPro; IPR004466; RNase_M5. DR InterPro; IPR025156; RNase_M5_C. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF13331; DUF4093; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR00334; 5S_RNA_mat_M5; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome; Ribosome biogenesis; KW RNA-binding; rRNA processing; rRNA-binding. FT CHAIN 1 178 Ribonuclease M5. FT /FTId=PRO_0000210402. FT DOMAIN 10 103 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01469}. FT METAL 16 16 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01469}. FT METAL 62 62 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01469}. FT METAL 62 62 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01469}. FT METAL 64 64 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01469}. SQ SEQUENCE 178 AA; 20412 MW; 50A5129B163B86D6 CRC64; MDKKTRLKLD GVIVCEGKTD QARLQQLFDV SVITTNGSAL NQRTINLIKA VAKKQPVILF LDPDVAGQKI RRQLEQHLDK YESCFIARKD MKPNSTKIGV AEATDAALIQ ALQQRQVFTK TTQPTLSWEQ YLELNLNSKS KRLALCNKLH LSYFNHKQLF RKLNLLQLTF DQVCQLLK // ID RPE_MYCPN Reviewed; 215 AA. AC P75522; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Probable ribulose-phosphate 3-epimerase; DE EC=5.1.3.1; DE AltName: Full=Pentose-5-phosphate 3-epimerase; DE Short=PPE; DE AltName: Full=R5P3E; GN Name=rpe; OrderedLocusNames=MPN_251; ORFNames=MP581; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- CC phosphate to D-xylulose 5-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5- CC phosphate. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 divalent metal cation per subunit. Active with CC Co(2+), Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase 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; U00089; AAB96229.1; -; Genomic_DNA. DR PIR; S73907; S73907. DR RefSeq; NP_109939.1; NC_000912.1. DR RefSeq; WP_010874608.1; NC_000912.1. DR ProteinModelPortal; P75522; -. DR IntAct; P75522; 2. DR EnsemblBacteria; AAB96229; AAB96229; MPN_251. DR GeneID; 876912; -. DR KEGG; mpn:MPN251; -. DR PATRIC; 20021827; VBIMycPne110_0270. DR KO; K01783; -. DR OMA; RISFHVE; -. DR OrthoDB; EOG67HK17; -. DR BioCyc; MetaCyc:MONOMER-582; -. DR BioCyc; MPNE272634:GJ6Z-258-MONOMER; -. DR Proteomes; UP000000808; 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 Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. 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 SUPFAM; SSF51366; SSF51366; 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; Cobalt; Complete proteome; Iron; Isomerase; KW Manganese; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 215 Probable ribulose-phosphate 3-epimerase. FT /FTId=PRO_0000171577. FT REGION 148 151 Substrate binding. {ECO:0000250}. FT REGION 196 197 Substrate binding. {ECO:0000250}. FT ACT_SITE 40 40 Proton acceptor. {ECO:0000250}. FT ACT_SITE 175 175 Proton donor. {ECO:0000250}. FT METAL 38 38 Divalent metal cation. {ECO:0000250}. FT METAL 40 40 Divalent metal cation. {ECO:0000250}. FT METAL 69 69 Divalent metal cation. {ECO:0000250}. FT METAL 175 175 Divalent metal cation. {ECO:0000250}. FT BINDING 13 13 Substrate. {ECO:0000250}. FT BINDING 69 69 Substrate. {ECO:0000250}. FT BINDING 177 177 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 215 AA; 24853 MW; 71A8B7D8955EFB42 CRC64; MLNLVVNREI AFSLLPLLHQ FDRKLLEQFF ADGLRLIHYD VMDHFVDNTV FQGEHLDELQ QIGFQVNVHL MVQALEQILP VYLHHQAVKR ISFHVEPFDI PTIKHFIAQI KQAGKQVGLA FKFTTPLVNY ERLVQQLDFV TLMSVPPGKG GQAFNSAVFN NLKQAHKYHC SIEIDGGIKL DNIHQIQDDV NFIVMGSGFI KLERWQRQQL LKTNQ // ID RS10_MYCPN Reviewed; 108 AA. AC P75581; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rpsJ {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=MPN_164; ORFNames=MP667; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in the binding of tRNA to the ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC 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; U00089; AAB96315.1; -; Genomic_DNA. DR PIR; S73993; S73993. DR RefSeq; NP_109852.1; NC_000912.1. DR RefSeq; WP_010874521.1; NC_000912.1. DR ProteinModelPortal; P75581; -. DR EnsemblBacteria; AAB96315; AAB96315; MPN_164. DR GeneID; 877180; -. DR KEGG; mpn:MPN164; -. DR PATRIC; 20021651; VBIMycPne110_0182. DR KO; K02946; -. DR OMA; IESLMHI; -. DR OrthoDB; EOG6VXFHB; -. DR BioCyc; MPNE272634:GJ6Z-171-MONOMER; -. DR Proteomes; UP000000808; 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 1 108 30S ribosomal protein S10. FT /FTId=PRO_0000146558. SQ SEQUENCE 108 AA; 12203 MW; 9E119800CB8C848E CRC64; MNAANAVKYP ELKIKLESYD STLLDLTTKK IVEVVKGVDV KIKGPLPLPT KKEVITIIRS PHVDKASREQ FEKNRHKRLM ILVDVNQGAI DSLKRIKIPV GVTLRFSK // ID RS12_MYCPN Reviewed; 139 AA. AC P75546; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=MPN_225; ORFNames=MP606; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that CC are involved in tRNA selection in the A site and with the mRNA CC backbone. Located at the interface of the 30S and 50S subunits, it CC traverses the body of the 30S subunit contacting proteins on the CC other side and probably holding the rRNA structure together. The CC combined cluster of proteins S8, S12 and S17 appears to hold CC together the shoulder and platform of the 30S subunit. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 CC and S17. May interact with IF1 in the 30S initiation complex. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SIMILARITY: Belongs to the ribosomal protein S12P family. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- CAUTION: Because the enzyme that would modify Asp-102 to 3- CC methylthioaspartic acid has not been found in the proteome of this CC organism, that modification is not predicted. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96254.1; -; Genomic_DNA. DR PIR; S73932; S73932. DR RefSeq; NP_109913.1; NC_000912.1. DR RefSeq; WP_010874582.1; NC_000912.1. DR ProteinModelPortal; P75546; -. DR SMR; P75546; 2-137. DR IntAct; P75546; 6. DR EnsemblBacteria; AAB96254; AAB96254; MPN_225. DR GeneID; 877067; -. DR KEGG; mpn:MPN225; -. DR PATRIC; 20021775; VBIMycPne110_0244. DR KO; K02950; -. DR OMA; LKSCPER; -. DR OrthoDB; EOG61ZTNF; -. DR BioCyc; MPNE272634:GJ6Z-232-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00403_B; Ribosomal_S12_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_S12/S23. DR InterPro; IPR005679; Ribosomal_S12_bac. DR PANTHER; PTHR11652; PTHR11652; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 139 30S ribosomal protein S12. FT /FTId=PRO_0000146268. SQ SEQUENCE 139 AA; 15629 MW; ADCF0F238AEDF3B4 CRC64; MATIAQLIRK PRKKKKVKSK SPALHYNLNL LNKKVTNVYS PLKRGVCTRV GTMTPKKPNS ALRKYAKVRL TNGFEVLTYI PGEGHNLQEH SVTLLRGGRV KDLPGVRYHI VRGTLDTVGV EKRRQQRSAY GAKKPKAKS // ID RPOB_MYCPN Reviewed; 1391 AA. AC P78013; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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=MPN_516; ORFNames=MP326; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95974.1; -; Genomic_DNA. DR PIR; S73652; S73652. DR RefSeq; NP_110204.1; NC_000912.1. DR RefSeq; WP_010874872.1; NC_000912.1. DR ProteinModelPortal; P78013; -. DR IntAct; P78013; 14. DR EnsemblBacteria; AAB95974; AAB95974; MPN_516. DR GeneID; 876806; -. DR KEGG; mpn:MPN516; -. DR PATRIC; 20022486; VBIMycPne110_0570. DR KO; K03043; -. DR OMA; DIRDVHY; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; MPNE272634:GJ6Z-557-MONOMER; -. DR Proteomes; UP000000808; 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; -; 1. DR Gene3D; 3.90.1110.10; -; 3. 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; 4. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. 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 1391 DNA-directed RNA polymerase subunit beta. FT /FTId=PRO_0000047922. SQ SEQUENCE 1391 AA; 155622 MW; B2F345AB24F18EAD CRC64; MSQKPSFFQK KYSPTATRRY YGKIATDFVQ PNLADIQIRS YQTFLDHDLE NLIAAYFPIK SPNDRYTINF KGLRRTAPER NEAQSRSESK TYEIGIYADL ELIDSATGTI KKPRKSKKNS ATSSVDGVFL TNLPLITRDG VFIVNGIEKF VIAQITRSPG IYMLTKSQLK LSSSRKRVQE GYVCEVLPAN GSVMLIYISN KKKIEDAFVQ ILLRDAVREG AKIFPITTLL KAFGMSGKEI LKVFKNNEFI TRSLEAEVYN AKDFLNNVDP EIKNLLREFR DGKTDLRRKG IASDQKIRSL VSDYVLLEKE HKALSEAKPN DPKVGQLEAD MDELMDKIIT ERAAKHIVHE LSISLRGLEN TDECPENSYH ALLCSRFFRQ RRYNLSAAGR YKVSRKLRIT ERIYQKTLAC DLHLKNGELL LKKGTLLVKE EIDKIKQAAQ NNQIDFVQKI KLTTDGSAVN LSPESLLYES LDVYVNNDNF DVSVPVVGIH NDNDLNKAIT LSDFIASISY VINIPSAIGK YDDIDHLGNK RVKLINELIS SRLESGITRM ERFLKEKLTI ADGVNRGQQI NEEGQVIEQA EKKELTIKSL INSKPIQIVI RDFFNTHQLT QFLDHQNPLS ELSNKRRISA MGPGGISRED PNLDIRDVHY SQYGRICPIE TPEGMNIGLI MSLASFAKID ENGFLMAPYR KIKNGVITDE VEYLTALRED EHIIAEISSL VNIDENNKIL DKEIIGRYRS MQGLYDPSKI DYIDVAPHQV VSIGSSLIPF LENDDSARAL MGTNMQRQAY PLIKPYAPVV GTGQEYKIAR DSGLTMLAPC SGTVKYVDNS KITIESDSGE QHTLDLIKFE RSNQNTCYNH VPLVEKGQRV TKDEVIADGP AVNKSELSLG QNVLVAFTTW NGYNYEDAIV ISERLVKDDV LTSLTINEYV AQCLSTKNGD EQITRDIPNV SDANKRYLDE NGIIMVGAEV KEGDVLVGKV SPKGQVEVSP EEKLFKAIFP ESVQNVRDSS LKLPHGGDGI VSCVKRFSIA NGNELNDGVI EMIKVYVVQK RKIQIGDKLA GRHGNKGVIS KVVPVADMPH LEDGTPVDIL LNPLGVPSRM NIGQIFEMHL GYAAHNLAKR MLISACFDDK KAQALSTEIN QPQYKLDRLI TGLKAQITNR GLKDEQAALA QLNNGDIALV LKEIGMSFDD LHFKVATPIF QGVNFQDLQD IMDEAGLKPA ETHGKFKLID GRTGLPFEKP ISLGIMYIMK LNHMVDDKIH ARAVGPYSKI TQQPLGGKSQ NGGQRFGEME VWALEAYGAA YNLQELLTIK SDDVQGRNKA YAAIVKGAAF PEPGIPESFK LLTKELQGLA LSVSFIYDDN TQQDSNNVSI LQADGEQDDL FNDFEFDTEG Y // ID RS14Z_MYCPN Reviewed; 61 AA. AC Q50305; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364}; GN Name=rpsZ {ECO:0000255|HAMAP-Rule:MF_01364}; GN Synonyms=rpsN {ECO:0000255|HAMAP-Rule:MF_01364}; GN OrderedLocusNames=MPN_178; ORFNames=MP653; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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_01364}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01364}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01364}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 CC and S10. {ECO:0000255|HAMAP-Rule:MF_01364}. CC -!- SIMILARITY: Belongs to the ribosomal protein S14P family. Zinc- CC binding S14P subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43703.1; -; Genomic_DNA. DR EMBL; U00089; AAB96301.1; -; Genomic_DNA. DR PIR; S62805; S62805. DR RefSeq; NP_109866.1; NC_000912.1. DR RefSeq; WP_010874535.1; NC_000912.1. DR ProteinModelPortal; Q50305; -. DR SMR; Q50305; 2-61. DR IntAct; Q50305; 1. DR EnsemblBacteria; AAB96301; AAB96301; MPN_178. DR GeneID; 876916; -. DR KEGG; mpn:MPN178; -. DR PATRIC; 20021679; VBIMycPne110_0196. DR KO; K02954; -. DR OMA; RAYTRCN; -. DR OrthoDB; EOG6BCT0K; -. DR BioCyc; MPNE272634:GJ6Z-185-MONOMER; -. DR Proteomes; UP000000808; 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:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01364_B; Ribosomal_S14_2_B; 1. DR InterPro; IPR001209; Ribosomal_S14. DR InterPro; IPR018271; Ribosomal_S14_CS. DR InterPro; IPR023053; Ribosomal_S14_Z. DR PANTHER; PTHR19836; PTHR19836; 1. DR Pfam; PF00253; Ribosomal_S14; 1. DR PROSITE; PS00527; RIBOSOMAL_S14; 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 61 30S ribosomal protein S14 type Z. FT /FTId=PRO_0000130908. FT METAL 24 24 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 27 27 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 40 40 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 43 43 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. SQ SEQUENCE 61 AA; 6885 MW; 552BA0FF662C481D CRC64; MAKKSLKVKQ TRIPKFAVRA YTRCQRCGRA RAVLSHFGVC RLCFRELAYA GAIPGVKKAS W // ID RS19_MYCPN Reviewed; 87 AA. AC P75576; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=30S ribosomal protein S19; GN Name=rpsS; OrderedLocusNames=MPN_169; ORFNames=MP662; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly CC to the 16S ribosomal RNA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S19P 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; U00089; AAB96310.1; -; Genomic_DNA. DR PIR; S73988; S73988. DR RefSeq; NP_109857.1; NC_000912.1. DR RefSeq; WP_010874526.1; NC_000912.1. DR ProteinModelPortal; P75576; -. DR SMR; P75576; 3-83. DR IntAct; P75576; 10. DR EnsemblBacteria; AAB96310; AAB96310; MPN_169. DR GeneID; 876872; -. DR KEGG; mpn:MPN169; -. DR PATRIC; 20021661; VBIMycPne110_0187. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR BioCyc; MPNE272634:GJ6Z-176-MONOMER; -. DR Proteomes; UP000000808; 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 87 30S ribosomal protein S19. FT /FTId=PRO_0000129862. SQ SEQUENCE 87 AA; 10037 MW; D548AD5A55371322 CRC64; MSRSAKKGAF VDAHLLKKVI DMNKQEKKRP IKTWSRRSTI FPEFVGNTFA VHNGKTFINV YVTDDMVGHK LGEFSPTRNF KQHTANR // ID RRF_MYCPN Reviewed; 184 AA. AC P75161; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. 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=MPN_636; GN ORFNames=MP206; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95854.1; -; Genomic_DNA. DR PIR; S73532; S73532. DR RefSeq; NP_110325.1; NC_000912.1. DR RefSeq; WP_010874993.1; NC_000912.1. DR ProteinModelPortal; P75161; -. DR IntAct; P75161; 1. DR EnsemblBacteria; AAB95854; AAB95854; MPN_636. DR GeneID; 876737; -. DR KEGG; mpn:MPN636; -. DR PATRIC; 20022753; VBIMycPne110_0699. DR KO; K02838; -. DR OMA; VQPWEKK; -. DR OrthoDB; EOG6SV5F9; -. DR BioCyc; MPNE272634:GJ6Z-682-MONOMER; -. DR Proteomes; UP000000808; 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 1 184 Ribosome-recycling factor. FT /FTId=PRO_0000167498. SQ SEQUENCE 184 AA; 21667 MW; 0091867172ECE9C2 CRC64; MSPEKYLNFF KETADKKFQW LKEELSKIRT GRPNPKLFDN LLVESYGDRM PMVALAQIAV NPPREIVIKP FDVKNNINAI YSEIQRANLG VQPVIDGDKI RINFPPMTQE SRLESIKQAK KVVEQIHQEL RSVRRDTLQM IKKDDHKDED FEEFLKEEVE KVNKQYIAQL ETIQKQKEKE LLVV // ID RS17_MYCPN Reviewed; 85 AA. AC Q50309; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=MPN_174; ORFNames=MP657; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43707.1; -; Genomic_DNA. DR EMBL; U00089; AAB96305.1; -; Genomic_DNA. DR PIR; S62832; S62832. DR RefSeq; NP_109862.1; NC_000912.1. DR RefSeq; WP_010874531.1; NC_000912.1. DR ProteinModelPortal; Q50309; -. DR SMR; Q50309; 5-84. DR IntAct; Q50309; 5. DR EnsemblBacteria; AAB96305; AAB96305; MPN_174. DR GeneID; 876867; -. DR KEGG; mpn:MPN174; -. DR PATRIC; 20021671; VBIMycPne110_0192. DR KO; K02961; -. DR OMA; VEDHDYP; -. DR OrthoDB; EOG63JRH2; -. DR BioCyc; MPNE272634:GJ6Z-181-MONOMER; -. DR Proteomes; UP000000808; 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 85 30S ribosomal protein S17. FT /FTId=PRO_0000128470. SQ SEQUENCE 85 AA; 9834 MW; 98AEB8355FB479BB CRC64; MKRNQRKVLI GIVKSTKNAK TATVQVESRF KHPLYHKSVV RHKKYQAHNE GEVLAKDGDK VQIVETRPLS ATKRFRIAKI IERAK // ID RS11_MYCPN Reviewed; 121 AA. AC Q50296; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=MPN_190; ORFNames=MP641; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43691.1; -; Genomic_DNA. DR EMBL; U00089; AAB96289.1; -; Genomic_DNA. DR PIR; S62818; S62818. DR RefSeq; NP_109878.1; NC_000912.1. DR RefSeq; WP_010874547.1; NC_000912.1. DR ProteinModelPortal; Q50296; -. DR EnsemblBacteria; AAB96289; AAB96289; MPN_190. DR GeneID; 876893; -. DR KEGG; mpn:MPN190; -. DR PATRIC; 20021703; VBIMycPne110_0208. DR KO; K02948; -. DR OMA; NTPYASQ; -. DR OrthoDB; EOG6ZSPF3; -. DR BioCyc; MPNE272634:GJ6Z-197-MONOMER; -. DR Proteomes; UP000000808; 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 1 121 30S ribosomal protein S11. FT /FTId=PRO_0000123182. SQ SEQUENCE 121 AA; 12687 MW; 2429E35585A9ED74 CRC64; MAKKKKINVS SGIIHVSCSP NNTIVSASDP GGNVLCWASS GTMGFKGSRK KTPYSAGIAA DKVAKTVKEM GMATVKLFVK GTGRGKDTAI RSFANAGLSI TEINEKTPIP HNGCKPPKRP R // ID RS21_MYCPN Reviewed; 60 AA. AC P57079; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=30S ribosomal protein S21; GN Name=rpsU; OrderedLocusNames=MPN_296; ORFNames=MP539.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein S21P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34754.1; -; Genomic_DNA. DR RefSeq; NP_109984.1; NC_000912.1. DR RefSeq; WP_010874653.1; NC_000912.1. DR EnsemblBacteria; AAG34754; AAG34754; MPN_296. DR GeneID; 877152; -. DR KEGG; mpn:MPN296; -. DR PATRIC; 20021927; VBIMycPne110_0320. DR KO; K02970; -. DR OMA; KRTAMRY; -. DR OrthoDB; EOG6FBX3Z; -. DR BioCyc; MPNE272634:GJ6Z-303-MONOMER; -. DR Proteomes; UP000000808; 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 TIGRFAMs; TIGR00030; S21p; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 60 30S ribosomal protein S21. FT /FTId=PRO_0000178353. SQ SEQUENCE 60 AA; 7515 MW; 30D87DCF4635F003 CRC64; MPKIEVKNDD LELALKKFKR VSLEIRRLAQ RHEYHLRKGM RLREKRKIAQ KKRRKFRNMV // ID RS4_MYCPN Reviewed; 205 AA. AC P46775; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; GN Synonyms=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN OrderedLocusNames=MPN_446; ORFNames=MP395; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; L38997; AAA61698.1; -; Genomic_DNA. DR EMBL; U00089; AAB96043.1; -; Genomic_DNA. DR PIR; S73721; S73721. DR RefSeq; NP_110134.1; NC_000912.1. DR RefSeq; WP_010874802.1; NC_000912.1. DR ProteinModelPortal; P46775; -. DR IntAct; P46775; 4. DR EnsemblBacteria; AAB96043; AAB96043; MPN_446. DR GeneID; 877128; -. DR KEGG; mpn:MPN446; -. DR PATRIC; 20022290; VBIMycPne110_0482. DR KO; K02986; -. DR OMA; EWVALQI; -. DR OrthoDB; EOG6N3CXM; -. DR BioCyc; MPNE272634:GJ6Z-475-MONOMER; -. DR Proteomes; UP000000808; 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 1 205 30S ribosomal protein S4. FT /FTId=PRO_0000132419. FT DOMAIN 95 156 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_01306}. SQ SEQUENCE 205 AA; 23775 MW; D6084DA86C47A43C CRC64; MKYTGSIFKR SRRLGFSLLE NNKEFSKGKK RKTIPGQHGN RFRSSTMSGY AQQLQEKQRM QYMYGITDKQ FRRLFRLVLK QRGNLAVNLF RVLESRLDNI VYRMGFAPTR RSARQLVNHG HVLLNDRTVD TPSIILNPGD KVRLKAKTIK IPIVKAASES GVVSPFVETN NKTFEGTYVR FPERSELPAG INESYVVEWY KRLVK // ID RS13_MYCPN Reviewed; 124 AA. AC Q50297; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=MPN_189; ORFNames=MP642; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43692.1; -; Genomic_DNA. DR EMBL; U00089; AAB96290.1; -; Genomic_DNA. DR PIR; S62819; S62819. DR RefSeq; NP_109877.1; NC_000912.1. DR RefSeq; WP_010874546.1; NC_000912.1. DR ProteinModelPortal; Q50297; -. DR SMR; Q50297; 2-120. DR IntAct; Q50297; 7. DR EnsemblBacteria; AAB96290; AAB96290; MPN_189. DR GeneID; 876976; -. DR KEGG; mpn:MPN189; -. DR PATRIC; 20021701; VBIMycPne110_0207. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR BioCyc; MPNE272634:GJ6Z-196-MONOMER; -. DR Proteomes; UP000000808; 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 1 124 30S ribosomal protein S13. FT /FTId=PRO_0000132110. SQ SEQUENCE 124 AA; 14180 MW; D54FA994AF2500D1 CRC64; MARILGIDIP NQKRIEIALT YIFGIGLSRS QAILKQANIN PDKRVKDLTE EEFVAIRNVA SAYKIEGDLR REIALNIKHL SEIGAWRGLR HRKNLPVRGQ RTRTNARTRK GPRKTVANKK IESK // ID RSMA_MYCPN Reviewed; 263 AA. AC P75113; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. 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=MPN_679; ORFNames=MP163; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95811.1; -; Genomic_DNA. DR PIR; S73489; S73489. DR RefSeq; NP_110368.1; NC_000912.1. DR RefSeq; WP_010875036.1; NC_000912.1. DR ProteinModelPortal; P75113; -. DR EnsemblBacteria; AAB95811; AAB95811; MPN_679. DR GeneID; 876770; -. DR KEGG; mpn:MPN679; -. DR PATRIC; 20022847; VBIMycPne110_0746. DR KO; K02528; -. DR OMA; HYPGRLE; -. DR OrthoDB; EOG66F08Z; -. DR BioCyc; MPNE272634:GJ6Z-725-MONOMER; -. DR Proteomes; UP000000808; 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 1 263 Ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101565. 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 105 105 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. SQ SEQUENCE 263 AA; 29794 MW; 1BDDD9A86739CE7C CRC64; MNSFYPSRKL GQNFTVDQSV IAKTCRLIKS LNPTALIEVG PGKGALTKAL LKLQLPYHGI ELDKRLAEYL LVNEILTEEQ LTIGDALKQN LDQYFPDTIP LLCGNIPYSI SSPLIANFLA SKLQQFVLVC QWEFGQRLVA PVNSPNYSAF GVFCQYHLQI KSVFKIDKVA FKPKPQVDSV LMLLKKKPQV AYEAHFGRFL KQCFHQRRKL LVNNLKQLLP PTLLTNVLQQ QDLAATVRAQ ELTPTQLFRL YLSLKPHLSD GKD // ID RS15_MYCPN Reviewed; 86 AA. AC P75173; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=MPN_622; ORFNames=MP220; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95868.1; -; Genomic_DNA. DR PIR; S73546; S73546. DR RefSeq; NP_110311.1; NC_000912.1. DR RefSeq; WP_010874979.1; NC_000912.1. DR ProteinModelPortal; P75173; -. DR IntAct; P75173; 1. DR EnsemblBacteria; AAB95868; AAB95868; MPN_622. DR GeneID; 877351; -. DR KEGG; mpn:MPN622; -. DR PATRIC; 20022727; VBIMycPne110_0686. DR KO; K02956; -. DR OMA; GSAYVQC; -. DR OrthoDB; EOG6B368J; -. DR BioCyc; MPNE272634:GJ6Z-668-MONOMER; -. DR Proteomes; UP000000808; 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 86 30S ribosomal protein S15. FT /FTId=PRO_0000115484. SQ SEQUENCE 86 AA; 9901 MW; 1C137064503D72B3 CRC64; MQIDKNGIIK SAQLHDKDVG SIQVQVSLLT SQIKQLTDHL LANKKDFISK RGLYAKVSKR KRLLKYLKHN DLEAYRNLVK TLNLRG // ID RS20_MYCPN Reviewed; 87 AA. AC P75237; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=MPN_541; ORFNames=MP301; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP- CC Rule:MF_00500}. CC -!- INTERACTION: CC P75545:rpsG; NbExp=1; IntAct=EBI-2259294, EBI-2259235; 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; U00089; AAB95949.1; -; Genomic_DNA. DR PIR; S73627; S73627. DR RefSeq; NP_110230.1; NC_000912.1. DR RefSeq; WP_010874898.1; NC_000912.1. DR ProteinModelPortal; P75237; -. DR IntAct; P75237; 1. DR EnsemblBacteria; AAB95949; AAB95949; MPN_541. DR GeneID; 877404; -. DR KEGG; mpn:MPN541; -. DR PATRIC; 20022559; VBIMycPne110_0603. DR KO; K02968; -. DR OMA; NFHKEIN; -. DR OrthoDB; EOG6HMXNQ; -. DR BioCyc; MPNE272634:GJ6Z-586-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 87 30S ribosomal protein S20. FT /FTId=PRO_0000167995. SQ SEQUENCE 87 AA; 9971 MW; 4CAB26530C6B1D0C CRC64; MANIKSNEKR LRQNIKRNLN NKGQKTKLKT NVKNFHKEIN LDNLGNVYSQ ADRLARKGII STNRARRLKS RNVAVLNKTQ VTAVEGK // ID RSMG_MYCPN Reviewed; 191 AA. AC P75220; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074}; DE EC=2.1.1.- {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=MPN_558; ORFNames=MP284; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in CC 16S 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; U00089; AAB95932.1; -; Genomic_DNA. DR PIR; S73610; S73610. DR RefSeq; NP_110247.1; NC_000912.1. DR RefSeq; WP_010874915.1; NC_000912.1. DR ProteinModelPortal; P75220; -. DR IntAct; P75220; 1. DR EnsemblBacteria; AAB95932; AAB95932; MPN_558. DR GeneID; 876918; -. DR KEGG; mpn:MPN558; -. DR PATRIC; 20022593; VBIMycPne110_0620. DR KO; K03501; -. DR OMA; GFGERIN; -. DR OrthoDB; EOG6HF639; -. DR BioCyc; MPNE272634:GJ6Z-603-MONOMER; -. DR Proteomes; UP000000808; 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 1 191 Ribosomal RNA small subunit FT methyltransferase G. FT /FTId=PRO_0000184289. FT REGION 111 112 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00074}. FT BINDING 59 59 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 124 124 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00074}. SQ SEQUENCE 191 AA; 22080 MW; 9F47ED53B443E2E3 CRC64; MNNSKLKQYV QLVQTANQNF NLTGLKTEGE IYEHLVQEII ELFNEYDSYF DHKKVADLGS GNGCPGVILK LLFPQIKTLD LIDSKHKKVN FLKEVIQTLE LNNTQALCAR IENHTEQYDT LCSRGLGSII EVNAFALKLL KPNGIIFHIK QSLDQYLEFE DSEQKDQFKP LFFKFFHGKR QQILIAMKKN V // ID RSMI_MYCPN Reviewed; 276 AA. AC P75046; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877}; DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN OrderedLocusNames=MPN_071; ORFNames=D09_orf276, MP084; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine CC 1402 (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(1402) in CC 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(1402) CC in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI CC family. {ECO:0000255|HAMAP-Rule:MF_01877}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95732.1; -; Genomic_DNA. DR PIR; S73410; S73410. DR RefSeq; NP_109759.1; NC_000912.1. DR RefSeq; WP_010874428.1; NC_000912.1. DR ProteinModelPortal; P75046; -. DR PRIDE; P75046; -. DR EnsemblBacteria; AAB95732; AAB95732; MPN_071. DR GeneID; 877160; -. DR KEGG; mpn:MPN071; -. DR PATRIC; 20021421; VBIMycPne110_0072. DR KO; K07056; -. DR OMA; KLHESHY; -. DR OrthoDB; EOG6677TH; -. DR BioCyc; MPNE272634:GJ6Z-73-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I. DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR00096; TIGR00096; 1. DR PROSITE; PS01296; RSMI; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 276 Ribosomal RNA small subunit FT methyltransferase I. FT /FTId=PRO_0000211944. SQ SEQUENCE 276 AA; 31062 MW; 2A071E7A17FCD0CD CRC64; MPALKVIATP IGNIEEVSPR VKAALTKCEV LFCEDTRVTK KLLGLLGIDF SNKQFIINNE FKEKQNLSKV ANLIHQYHCG LVSDAGYPSV SDPGHILVEY VRTQLPQIAI EVINGPSALV CGLVTSGFPE SPLLFLGFLD HKPTQVTQTL KHYQNFQGTI VLFEAVHRLQ QTLEVIQTVF SNTEVFVGRE LTKLHESHYW FNTSAPLPDI TLKGEFVIVI NNHHTQPVGQ YSDQLLKQEI TQLVQMGVKV KDACHYLAKR LQLKSNKLYT LFHESD // ID RS18_MYCPN Reviewed; 104 AA. AC P75541; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; GN OrderedLocusNames=MPN_230; ORFNames=MP601; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96249.1; -; Genomic_DNA. DR PIR; S73927; S73927. DR RefSeq; NP_109918.1; NC_000912.1. DR RefSeq; WP_010874587.1; NC_000912.1. DR ProteinModelPortal; P75541; -. DR IntAct; P75541; 6. DR PRIDE; P75541; -. DR EnsemblBacteria; AAB96249; AAB96249; MPN_230. DR GeneID; 877081; -. DR KEGG; mpn:MPN230; -. DR PATRIC; 20021785; VBIMycPne110_0249. DR KO; K02963; -. DR OMA; YKRPDIL; -. DR OrthoDB; EOG6PCQ4R; -. DR BioCyc; MPNE272634:GJ6Z-237-MONOMER; -. DR Proteomes; UP000000808; 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 1 104 30S ribosomal protein S18. FT /FTId=PRO_0000111188. SQ SEQUENCE 104 AA; 12386 MW; 0C424229C79CC1B5 CRC64; MMNNEHDNFQ KEVETTTETT FNREEGKRMV RPLFKRSKKY CRFCAIGQLR IDLIDDLEAL KRFLSPYAKI NPRRITGNCQ MHQRHVAKAL KRARYLALVP FVKD // ID RS8_MYCPN Reviewed; 142 AA. AC Q50304; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; GN OrderedLocusNames=MPN_179; ORFNames=MP652; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43702.1; -; Genomic_DNA. DR EMBL; U00089; AAB96300.1; -; Genomic_DNA. DR PIR; S62828; S62828. DR RefSeq; NP_109867.1; NC_000912.1. DR RefSeq; WP_010874536.1; NC_000912.1. DR ProteinModelPortal; Q50304; -. DR IntAct; Q50304; 2. DR EnsemblBacteria; AAB96300; AAB96300; MPN_179. DR GeneID; 876779; -. DR KEGG; mpn:MPN179; -. DR PATRIC; 20021681; VBIMycPne110_0197. DR KO; K02994; -. DR OMA; RIYKNTR; -. DR OrthoDB; EOG6Z0QH1; -. DR BioCyc; MPNE272634:GJ6Z-186-MONOMER; -. DR Proteomes; UP000000808; 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 1 142 30S ribosomal protein S8. FT /FTId=PRO_0000126446. SQ SEQUENCE 142 AA; 15877 MW; B5850BAD123CF67E CRC64; MITTTKPIKA HFDPVADLLT KINNARKAKL MTVTTIASKL KIAILEILVK EGYLANFQVL ENKSKTKRIV TFNLKYTQRR IPSINGVKQI SKPGLRIYRP FEKLPLVLNG LGIAIISTSD GVMTDKVARL KKIGGEILAY VW // ID RS16_MYCPN Reviewed; 88 AA. AC P75131; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=30S ribosomal protein S16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN Name=rpsP {ECO:0000255|HAMAP-Rule:MF_00385}; GN OrderedLocusNames=MPN_660; ORFNames=MP182; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95830.1; -; Genomic_DNA. DR PIR; S73508; S73508. DR ProteinModelPortal; P75131; -. DR IntAct; P75131; 2. DR EnsemblBacteria; AAB95830; AAB95830; MPN_660. DR PATRIC; 20022805; VBIMycPne110_0725. DR OMA; QANANVN; -. DR OrthoDB; EOG6CVVKH; -. DR BioCyc; MPNE272634:GJ6Z-706-MONOMER; -. DR Proteomes; UP000000808; 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 88 30S ribosomal protein S16. FT /FTId=PRO_0000167211. SQ SEQUENCE 88 AA; 10042 MW; 95D4F396F976A7CC CRC64; MRMGRVHYPT YRIVAVDSRV KRDGKYIALI GHLNPALKEN KCKIDEAVAL EWLNKGAKPT DTVRSLFSQT GLWKKFVESK KKPVAKSK // ID RS3_MYCPN Reviewed; 273 AA. AC P41205; P75574; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 104. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; GN OrderedLocusNames=MPN_171; ORFNames=MP660; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-236. RC STRAIN=ATCC 29342 / M129; RA Wenzel R., Pirkl E., Herrmann R.; RL Submitted (AUG-1992) 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; U00089; AAB96308.1; -; Genomic_DNA. DR EMBL; X67652; CAA47894.1; -; Genomic_DNA. DR PIR; S73986; S73986. DR RefSeq; NP_109859.1; NC_000912.1. DR RefSeq; WP_010874528.1; NC_000912.1. DR ProteinModelPortal; P41205; -. DR IntAct; P41205; 12. DR EnsemblBacteria; AAB96308; AAB96308; MPN_171. DR GeneID; 876958; -. DR KEGG; mpn:MPN171; -. DR PATRIC; 20021665; VBIMycPne110_0189. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR BioCyc; MPNE272634:GJ6Z-178-MONOMER; -. DR Proteomes; UP000000808; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 273 30S ribosomal protein S3. FT /FTId=PRO_0000130156. FT DOMAIN 40 110 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 273 AA; 30614 MW; AFEEAA4D0C9C1C51 CRC64; MGQKVNSNGL RFGINKNWIS RWTANSHAQT AKWLIEDEKI RNLFFVNYRN AQVSNVEIER TQATVDVFVY AAQPAFLIGS ENKNIQKITK QIKQIIGRTT NLDLTINEIG SPMLSARIIA RDLANAIEAR VPLRTAMRQS LIKVLKAGAN GIKVLVSGRL NGAEIARDKM YIEGNMPLST LRADIDYALE KAQTTYGVIG VKVWINRGMI YTKGLNRTPA HILHPQKKQP NRQNQQPRHF NQGQVLSANK LTGSDVETSS IQALTKPNKE DKQ // ID RS2_MYCPN Reviewed; 294 AA. AC P75560; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=30S ribosomal protein S2; GN Name=rpsB; OrderedLocusNames=MPN_208; ORFNames=MP623; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S2P 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; U00089; AAB96271.1; -; Genomic_DNA. DR PIR; S73949; S73949. DR RefSeq; NP_109896.1; NC_000912.1. DR RefSeq; WP_010874565.1; NC_000912.1. DR ProteinModelPortal; P75560; -. DR IntAct; P75560; 7. DR EnsemblBacteria; AAB96271; AAB96271; MPN_208. DR GeneID; 876805; -. DR KEGG; mpn:MPN208; -. DR PATRIC; 20021741; VBIMycPne110_0227. DR KO; K02967; -. DR OMA; RYIYCAR; -. DR OrthoDB; EOG6XWV6P; -. DR BioCyc; MPNE272634:GJ6Z-215-MONOMER; -. DR Proteomes; UP000000808; 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; PS00963; RIBOSOMAL_S2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 294 30S ribosomal protein S2. FT /FTId=PRO_0000134201. SQ SEQUENCE 294 AA; 33426 MW; 60D111400C5F350D CRC64; MSELITTPVE TTAKAELVSL AKLGEMRTHV GMVKRYWNPK MGFFIEPERK HNNDHFVLEL QRQSLQTAYN YVKEVAQNNG QILFVGTKND YVKKLVNNIA KRVDVAFITQ RWLGGTLTNF KTLSISINKL NKLVEKQAEN AADLTKKENL MLSREIERLE KFFGGVKSLK RLPNLLIVDD PVYEKNAVAE ANILRIPVVA LCNTNTNPEL VDFIIPANNH QPQSTCLLMN LLADAVAEAK AMPTMFAYKP DEEIQIEIPQ KQEAPRQVVN RANSKQITSQ RLNITRNPEV LTRE // ID RS9_MYCPN Reviewed; 132 AA. AC P75179; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=30S ribosomal protein S9; GN Name=rpsI; OrderedLocusNames=MPN_616; ORFNames=MP226; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S9P 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; U00089; AAB95874.1; -; Genomic_DNA. DR PIR; S73552; S73552. DR RefSeq; NP_110305.1; NC_000912.1. DR RefSeq; WP_010874973.1; NC_000912.1. DR ProteinModelPortal; P75179; -. DR IntAct; P75179; 2. DR EnsemblBacteria; AAB95874; AAB95874; MPN_616. DR GeneID; 876980; -. DR KEGG; mpn:MPN616; -. DR PATRIC; 20022715; VBIMycPne110_0680. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR BioCyc; MPNE272634:GJ6Z-662-MONOMER; -. DR Proteomes; UP000000808; 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 1 132 30S ribosomal protein S9. FT /FTId=PRO_0000111377. SQ SEQUENCE 132 AA; 15119 MW; CA8E61887204F98A CRC64; MEKQSYYGLG RRKSSSAKVY LTPTQDKGKI TVNRRDPSEY FPNKLVIQDM EQPLDLTDLK KNFDINVVVK GGGFTGQAGA IRLGIVRALL QFNPELKKIL KSKKLTTRDK RVKERKKFGL YGARRAPQFT KR // ID RS5_MYCPN Reviewed; 219 AA. AC Q50301; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; GN OrderedLocusNames=MPN_182; ORFNames=MP649; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43699.1; -; Genomic_DNA. DR EMBL; U00089; AAB96297.1; -; Genomic_DNA. DR PIR; S62804; S62804. DR RefSeq; NP_109870.1; NC_000912.1. DR RefSeq; WP_010874539.1; NC_000912.1. DR ProteinModelPortal; Q50301; -. DR IntAct; Q50301; 11. DR EnsemblBacteria; AAB96297; AAB96297; MPN_182. DR GeneID; 876768; -. DR KEGG; mpn:MPN182; -. DR PATRIC; 20021687; VBIMycPne110_0200. DR KO; K02988; -. DR OMA; HKYNASK; -. DR OrthoDB; EOG6FJNM5; -. DR BioCyc; MPNE272634:GJ6Z-189-MONOMER; -. DR Proteomes; UP000000808; 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 1 219 30S ribosomal protein S5. FT /FTId=PRO_0000131554. FT DOMAIN 66 129 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 219 AA; 24090 MW; 50B176BEAABD80FD CRC64; MTDQNQKANQ GNGLQTTNLQ AHAQRKHNLR PSSEGIKKAV SKKEGGGHNR NNQNRRFQKP AFKSEFEERI VKLKRISKTT KGGRNMRFSV LVVVGNRKGK IGYGIAKALE VPNAIKKAIK AAHNSLHTIE IHKGSIYHEV IGRSGASRVL LKPAPQGTGI IAGGAIRAII ELAGYSDIYT KNLGRNTPIN MIHATMDGIL KQLSPRRVAI LRNKNLNEL // ID RUVB_MYCPN Reviewed; 307 AA. AC P75242; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 98. 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=MPN_536; ORFNames=MP306; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95954.1; -; Genomic_DNA. DR PIR; S73632; S73632. DR RefSeq; NP_110225.1; NC_000912.1. DR RefSeq; WP_010874893.1; NC_000912.1. DR ProteinModelPortal; P75242; -. DR IntAct; P75242; 2. DR EnsemblBacteria; AAB95954; AAB95954; MPN_536. DR GeneID; 877371; -. DR KEGG; mpn:MPN536; -. DR PATRIC; 20022549; VBIMycPne110_0598. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR BioCyc; MPNE272634:GJ6Z-581-MONOMER; -. DR Proteomes; UP000000808; 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 1 307 Holliday junction ATP-dependent DNA FT helicase RuvB. FT /FTId=PRO_0000165560. FT NP_BIND 45 52 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. SQ SEQUENCE 307 AA; 35012 MW; B1947D0C7AFFAF3A CRC64; MKLQIKPPNN FAEFVGKQEI INQIQLSIKA SRINKAQLDH ILLYGPPGVG KTTLARLIAS EMNTKLQIIQ GGHLQRPSDF LNAVSLIKKG DVLFVDEIHA VAPSVMELMF PVMDDFRVQV LIGKDFNSKM VEMKVNPFTW IGATTQFGKI INPLEDRFGM ILNIDYYSNQ EIERIVSIYG EQMELELKPE EITQITQHSK QTPRIAIRIV KRLFEQKIVN KKIDLAALFK SLMIYKNGLQ SIDVQYLKAL NGQYEPQGIK SICSMLGIDK STVENKIEPF LLRENMIQKT KKGRIITRTG RNYLTSC // ID RS6_MYCPN Reviewed; 215 AA. AC P75543; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=30S ribosomal protein S6; GN Name=rpsF; OrderedLocusNames=MPN_228; ORFNames=MP603; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S6P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96251.1; -; Genomic_DNA. DR PIR; S73929; S73929. DR RefSeq; NP_109916.1; NC_000912.1. DR RefSeq; WP_010874585.1; NC_000912.1. DR ProteinModelPortal; P75543; -. DR IntAct; P75543; 24. DR EnsemblBacteria; AAB96251; AAB96251; MPN_228. DR GeneID; 876983; -. DR KEGG; mpn:MPN228; -. DR PATRIC; 20021781; VBIMycPne110_0247. DR KO; K02990; -. DR OMA; RAANINK; -. DR OrthoDB; EOG6QK4TF; -. DR BioCyc; MPNE272634:GJ6Z-235-MONOMER; -. DR Proteomes; UP000000808; 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 1 215 30S ribosomal protein S6. FT /FTId=PRO_0000176800. SQ SEQUENCE 215 AA; 25391 MW; 955B72832038372D CRC64; MQYNIILLVD GSLSLEQANQ VNEKQQQTLT NVEGLQTEYL GLKELAYPIK KQLSAHYYRW KFSGDNQSTK DFKRTANINK QVLRELIINL EREYGYLASI NPKKQQLALQ KRAKYDEIIA RENNPENPDV PVTSGLASTQ PRLSRTEKAQ KPKEELWDVV QKMGNFDSVQ ANPYRPRFKR FNAEHVNQRQ NQQNNNNNRF DRNRNRQHNR FKDKQ // ID RS7_MYCPN Reviewed; 155 AA. AC P75545; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; GN OrderedLocusNames=MPN_226; ORFNames=MP605; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96253.1; -; Genomic_DNA. DR PIR; S73931; S73931. DR RefSeq; NP_109914.1; NC_000912.1. DR RefSeq; WP_010874583.1; NC_000912.1. DR ProteinModelPortal; P75545; -. DR SMR; P75545; 9-147. DR IntAct; P75545; 18. DR EnsemblBacteria; AAB96253; AAB96253; MPN_226. DR GeneID; 877063; -. DR KEGG; mpn:MPN226; -. DR PATRIC; 20021777; VBIMycPne110_0245. DR KO; K02992; -. DR OMA; EVHRMAD; -. DR OrthoDB; EOG6P5ZKW; -. DR BioCyc; MPNE272634:GJ6Z-233-MONOMER; -. DR Proteomes; UP000000808; 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 1 155 30S ribosomal protein S7. FT /FTId=PRO_0000124303. SQ SEQUENCE 155 AA; 17863 MW; 417A809447B32330 CRC64; MRKNRAPKRT VLPDPVFNNT LVTRIINVIM EDGKKGLAQR ILYGAFDLIE QRTKEKPLTV FERAVGNVMP RLELRVRRIA GSNYQVPTEV PQDRKIALAL RWIAMFARKR HEKTMLEKIA NEIIDASNNT GAAIKKKDDT HKMAEANKAF AHMRW // ID RUVA_MYCPN Reviewed; 206 AA. AC P75243; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 100. 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=MPN_535; ORFNames=MP307; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95955.1; -; Genomic_DNA. DR PIR; S73633; S73633. DR RefSeq; NP_110224.1; NC_000912.1. DR RefSeq; WP_010874892.1; NC_000912.1. DR ProteinModelPortal; P75243; -. DR IntAct; P75243; 2. DR EnsemblBacteria; AAB95955; AAB95955; MPN_535. DR GeneID; 877275; -. DR KEGG; mpn:MPN535; -. DR PATRIC; 20022547; VBIMycPne110_0597. DR KO; K03550; -. DR OMA; IVEHNWI; -. DR OrthoDB; EOG679THG; -. DR BioCyc; MPNE272634:GJ6Z-580-MONOMER; -. DR Proteomes; UP000000808; 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 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; IPR000085; RuvA. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF07499; RuvA_C; 1. DR Pfam; PF01330; RuvA_N; 1. DR SUPFAM; SSF47781; SSF47781; 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 1 206 Holliday junction ATP-dependent DNA FT helicase RuvA. FT /FTId=PRO_0000094651. SQ SEQUENCE 206 AA; 23660 MW; 6239A84AA31F013D CRC64; MIASIFGKIT FVGKRKIIVE ANCISYWFNV KENHSFEKNL EKPRQVFCQI IKRMVTNQIL EEGFAFNTLE EKEWFSKFIE LNGIGSKTAL NLLNNNLEEM RDYIKNSNYH ALTKLTGSNS KVARALLALE LYDRDDGGKR IKPNTAMAND YDEMFDTLKS LGYKPQDIQN ALSKIEIKPN FDVSEVIAEV IKLMSFQNNE VTNKTA // ID RSGA_MYCPN Reviewed; 278 AA. AC P75523; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. 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}; Synonyms=engC; GN OrderedLocusNames=MPN_249; ORFNames=MP583; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96231.1; -; Genomic_DNA. DR PIR; S73909; S73909. DR RefSeq; NP_109937.1; NC_000912.1. DR RefSeq; WP_010874606.1; NC_000912.1. DR ProteinModelPortal; P75523; -. DR PRIDE; P75523; -. DR EnsemblBacteria; AAB96231; AAB96231; MPN_249. DR GeneID; 876910; -. DR KEGG; mpn:MPN249; -. DR PATRIC; 20021823; VBIMycPne110_0268. DR KO; K06949; -. DR OMA; IGESEIW; -. DR OrthoDB; EOG69SKDD; -. DR BioCyc; MPNE272634:GJ6Z-256-MONOMER; -. DR Proteomes; UP000000808; 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 1 278 Putative ribosome biogenesis GTPase RsgA. FT /FTId=PRO_0000171496. FT DOMAIN 62 218 CP-type G. FT NP_BIND 112 115 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT NP_BIND 162 170 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT MOTIF 241 254 Knuckle-like cysteine cluster. FT METAL 241 241 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 246 246 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 248 248 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 254 254 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. SQ SEQUENCE 278 AA; 31568 MW; C1367801C67E4C40 CRC64; MSIRKTGIVF QRFGKQFKVF VENQTLVAFA QKKLQWKRDF KLLVGDKVTL ENGVIVAVEE RKNTLVRPKV VNVDQVVIVQ SLIEPKINWQ QLFKLLIHFH AQNVARLVLV ITKNDLEFEP AEKARLSELT SFGYQLFFTA PNADLPLTLF TELQNRFSVF MGQSGVGKSS LINRLDSQIH QAIQALSAHQ FGKNTTTSTV MFPFQNGFIC DTPGFNVIDF PNLKQLAAQH FVGFASLIGQ CHFSNCTHQS EKGCFIVSAV TQKSYSLWLY ESYLKLIN // ID RSMH_MYCPN Reviewed; 308 AA. AC P75466; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 92. 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=MPN_315; ORFNames=MP521; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96169.1; -; Genomic_DNA. DR PIR; S73847; S73847. DR RefSeq; NP_110003.1; NC_000912.1. DR RefSeq; WP_010874671.1; NC_000912.1. DR ProteinModelPortal; P75466; -. DR IntAct; P75466; 2. DR EnsemblBacteria; AAB96169; AAB96169; MPN_315. DR GeneID; 876936; -. DR KEGG; mpn:MPN315; -. DR PATRIC; 20021982; VBIMycPne110_0338. DR KO; K03438; -. DR OMA; ADGCYLD; -. DR OrthoDB; EOG6X9MQ1; -. DR BioCyc; MPNE272634:GJ6Z-332-MONOMER; -. DR Proteomes; UP000000808; 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 1 308 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108665. FT REGION 35 37 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 54 54 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 80 80 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01007}. FT BINDING 101 101 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 108 108 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. SQ SEQUENCE 308 AA; 35243 MW; 72EC0F4BD5B8743C CRC64; MLSNQPHKSV LLDEVIHNLN IKGDGNYLDL TVGFGGHSQH ILEQLTTGTL TGNDMDKDSI TFCTELFKDK KNVVLVHDNF ANFFNHLKQL KVTKFDGILI DLGVSSYQLD KPERGFSFKH AGPFDMRMHQ SDRVPTALDI LERLSEEELT HVLKKFGEIA HPKPIAKALK TLINNTKNPT TVEVAETVKA AASNFEKYKS RNYLAKVFQA IRIYLNRELE SLEIVLQHIP KLLNNKGRFL VIVFHSLEEK LVRNYIFKLT HFVQPPELPV KLTPPFELIT KKPILPTEQE IKTNPRVRSA KLFVIEKK // ID SCPB_MYCPN Reviewed; 208 AA. AC P75477; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804}; GN Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; GN OrderedLocusNames=MPN_301; ORFNames=MP535; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Participates in chromosomal partition during cell CC division. May act via the formation of a condensin-like complex CC containing Smc and ScpA that pull DNA away from mid-cell into both CC cell halves. {ECO:0000255|HAMAP-Rule:MF_01804}. CC -!- SUBUNIT: Homodimer. Homodimerization may be required to stabilize CC the binding of ScpA to the Smc head domains. Component of a CC cohesin-like complex composed of ScpA, ScpB and the Smc homodimer, CC in which ScpA and ScpB bind to the head domain of Smc. The CC presence of the three proteins is required for the association of CC the complex with DNA. {ECO:0000255|HAMAP-Rule:MF_01804}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01804}. CC Note=Associated with two foci at the outer edges of the nucleoid CC region in young cells, and at four foci within both cell halves in CC older cells. {ECO:0000255|HAMAP-Rule:MF_01804}. CC -!- SIMILARITY: Belongs to the ScpB family. {ECO:0000255|HAMAP- CC Rule:MF_01804}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96183.1; -; Genomic_DNA. DR PIR; S73861; S73861. DR RefSeq; NP_109989.1; NC_000912.1. DR RefSeq; WP_010874658.1; NC_000912.1. DR ProteinModelPortal; P75477; -. DR IntAct; P75477; 1. DR EnsemblBacteria; AAB96183; AAB96183; MPN_301. DR GeneID; 877283; -. DR KEGG; mpn:MPN301; -. DR PATRIC; 20021937; VBIMycPne110_0325. DR KO; K06024; -. DR OMA; ETHAFAK; -. DR OrthoDB; EOG6CZQQQ; -. DR BioCyc; MPNE272634:GJ6Z-308-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051304; P:chromosome separation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR HAMAP; MF_01804; ScpB; 1. 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. DR TIGRFAMs; TIGR00281; TIGR00281; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; Reference proteome. FT CHAIN 1 208 Segregation and condensation protein B. FT /FTId=PRO_0000211142. SQ SEQUENCE 208 AA; 23681 MW; AFB97DB3071E7068 CRC64; MDATIKVTKP VLKQKDSSAA NLVAAIYGLL FVSGEKGLTL AELNRVLRKV GLEKIKAALV QLERKLSLDD ESGIEIKKFG HSFRLVTKME IKDFIHRYLP NKIKNPLNSK TMEVLAIIAY NQPCTRPRIN EIRGADSFQI VDDLLEKELI VELGRKDTPG RPFIYEVSPK FYDLFGINSL DELPKVENFD LDKFRQGSFF DSNRYGDD // ID SECA_MYCPN Reviewed; 808 AA. AC P75559; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=MPN_210; ORFNames=MP621; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 as an ATP-driven molecular CC motor driving the stepwise translocation of polypeptide chains CC across the membrane. {ECO:0000255|HAMAP-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. Other proteins may also be involved. CC {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell 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; U00089; AAB96269.1; -; Genomic_DNA. DR PIR; S73947; S73947. DR RefSeq; NP_109898.1; NC_000912.1. DR RefSeq; WP_010874567.1; NC_000912.1. DR ProteinModelPortal; P75559; -. DR SMR; P75559; 455-497. DR IntAct; P75559; 3. DR EnsemblBacteria; AAB96269; AAB96269; MPN_210. DR GeneID; 877088; -. DR KEGG; mpn:MPN210; -. DR PATRIC; 20021745; VBIMycPne110_0229. DR KO; K03070; -. DR OMA; KLPMETD; -. DR OrthoDB; EOG654P48; -. DR BioCyc; MPNE272634:GJ6Z-217-MONOMER; -. DR Proteomes; UP000000808; 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: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; 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; 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; 1. 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 membrane; Complete proteome; Cytoplasm; Membrane; KW Nucleotide-binding; Protein transport; Reference proteome; KW Translocation; Transport. FT CHAIN 1 808 Protein translocase subunit SecA. FT /FTId=PRO_0000109596. FT NP_BIND 102 109 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. SQ SEQUENCE 808 AA; 91810 MW; E768F0B8915F892F CRC64; MGLFNFLKLV SPRHRIYHKA SKIANEVEGH KNYYRNLTDV QLLEESNKLV DLVTKQNYTI LDVAVAALAL IREVVYRETG EFAYRVQIIG AYIVLIGDFA EMMTGEGKTL TIVLAAYVSA LEKRGVHVVT VNEYLAQRDA TNATKILKRV GMTVGCNFAN LAPHLKQAAF ACDVTYTTNS ELGFDYLRDN MVHRFEDKKI RELHFAIVDE GDSVLIDEAR TPLIISGPAK NEFAAYVAVD RFVKKLKEDE YKIDPESRAP ALTELGIKHA EKNFKTDNLF ALENSDLFHK IINALTAVKV FEQGKEYIVR DGKVLIVDHF TGRILEGRSY SNGLHQAVQA KEMVEIEPEN VIVATITYQS FFRLYNRLSA VSGTAFTESE EFLKIYNMVV VPVPTNRPNI RKDRADSVFG TPNIKWLAVV KEVKRIHETG RPILIGTANI DDSELLHNYL QEANIPHEVL NAKNHSREAE IVAKAGQKGA VTISTNMAGR GTDIRLGEGV AEMGGLYVLG TERNESRRID NQLRGRAGRQ GDRGETKFFI SLGDALFKRF AHDRIERAIT KLGNDTFDSS FFSKMLSRTQ KRVEAINFDT RKNLIDYDHV LASQRELIYK QRDKFLLATD LSDMIDKMLE KFVEQFCDQY RNPKNQNLVN HIALSEALNL ELNMHGVISP KLFENMTFDA TVHKTHSLIG EKITNKVKVL TPPIALIRFR EIMITAMDKH WIEHLDNVFK LREGVTLRSM EQTSPLNVYI RETDILFQTM LQKIARDVII QIANLATPEE FDEELMKANA LKKLQALREA HEKSNEGQ // ID SECY_MYCPN Reviewed; 477 AA. AC Q59548; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; GN OrderedLocusNames=MPN_184; ORFNames=MP647; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP- CC Rule:MF_01465}. 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:0000255|HAMAP-Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01465}. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. CC {ECO:0000255|HAMAP-Rule:MF_01465}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34795; AAC43697.1; -; Genomic_DNA. DR EMBL; U00089; AAB96295.1; -; Genomic_DNA. DR PIR; S62824; S62824. DR RefSeq; NP_109872.1; NC_000912.1. DR RefSeq; WP_010874541.1; NC_000912.1. DR ProteinModelPortal; Q59548; -. DR EnsemblBacteria; AAB96295; AAB96295; MPN_184. DR GeneID; 876763; -. DR KEGG; mpn:MPN184; -. DR PATRIC; 20021691; VBIMycPne110_0202. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR BioCyc; MPNE272634:GJ6Z-191-MONOMER; -. DR Proteomes; UP000000808; 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 membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 477 Protein translocase subunit SecY. FT /FTId=PRO_0000131736. FT TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 67 89 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 130 150 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 165 185 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 196 216 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 234 254 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 286 306 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 329 349 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 387 407 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 413 433 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. SQ SEQUENCE 477 AA; 51967 MW; 0301F8F0D8D4BD88 CRC64; MQAKPTTAVK QKQNFGQRLF TLLRNRDFMI SFLITVVLLV LFRVLAIIPL PGIQVNQTGL DQNSNDFFSL FNLLGGGGLN QLSLFAVGIS PYISAQIVMQ LLSTDLIPPL SKLVNSGEVG RRKIEMITRI ITLPFALVQS FAVIQIATNS GGGSSPITLK NNGSDFVAFY IIAMTAGTYL SVFLGDTISK KGIGNGITLL ILSGILAQLP EGFIAAYSVL SGVVVTINAT LTTAISFFIY FMAFVTLLFA TTFITQETRK IPIQQSGQGL VTESSALPYL PIKVNSAGVI PVIFASSIMS IPVTIAQFQP QTESRWFVED YLSLSKPTGI VLYGILVILF SFFYSYIQIN PERLAKNFEK SGRFIPGIRP GKDTEKHIAR VLVRINFIGA PFLTVIAIIP YIVSALIHLP NSLSLGGTGI IIIVTAVVEF MSALRSAATA TNYQQLRRNL AIEVQKTAQQ DKEEQLRAET PGIGNLW // ID SCPA_MYCPN Reviewed; 506 AA. AC P75478; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Segregation and condensation protein A; GN Name=scpA; OrderedLocusNames=MPN_300; ORFNames=MP536; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. 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 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated CC with two foci at the outer edges of the nucleoid region in young CC cells, and at four foci within both cell halves in older cells. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ScpA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00660}. CC -!- CAUTION: Fused to a domain highly related to the dihydrofolate CC reductase family in its N-terminus. It is however unknown whether CC it contains such enzymatic activity. {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; U00089; AAB96184.1; -; Genomic_DNA. DR PIR; S73862; S73862. DR RefSeq; NP_109988.1; NC_000912.1. DR RefSeq; WP_010874657.1; NC_000912.1. DR ProteinModelPortal; P75478; -. DR IntAct; P75478; 5. DR PRIDE; P75478; -. DR EnsemblBacteria; AAB96184; AAB96184; MPN_300. DR GeneID; 877194; -. DR KEGG; mpn:MPN300; -. DR PATRIC; 20021935; VBIMycPne110_0324. DR KO; K05896; -. DR OMA; DDELYIC; -. DR OrthoDB; EOG6X9MN8; -. DR BioCyc; MPNE272634:GJ6Z-307-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR012259; DHFR. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR001796; DHFR_dom. DR InterPro; IPR003768; ScpA. DR Pfam; PF00186; DHFR_1; 1. DR Pfam; PF02616; SMC_ScpA; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; Reference proteome. FT CHAIN 1 506 Segregation and condensation protein A. FT /FTId=PRO_0000211097. FT DOMAIN 1 166 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT REGION 167 506 ScpA. SQ SEQUENCE 506 AA; 59521 MW; 578FA071E57CD6CF CRC64; MITLIWCQDK HFGIGRDNTI PWKLTEANQH FYNTTKNQTV VMGYNTFQEL GDKLTDHNVV VLSKKHFEEL QNNTNIKVFN SIEKLLQHHF NRDLYVIGGK QIFHHFIELA DRLIISVLPV DFKCNLRLKL GLDSFELMQE QQHSQFKVQY WHKKHPERLS FNVFLEDYNG TLPNLLELLI DKKFNLHQVD IAKITTQYLH LINTNLNKQA IEPITDYLVI TSRIVEQKAN NLLQINDIAL DSDFLDNKLR DKLVAQLVEY KRYRESLDDF EKLRINRLAY FSKDNDFNRF IQTVDKSNTE PVKIEDELPN YVSVLKLHHA MNKLMQRWRA QFLANKNISI QELSIEQVQA EILATIKQFG YHSVSLKRVL LKVNHHISLM YFITAFVALL VLINNQIIDI EQTSFDDELY ICLLDSSRIE QLQETPEAMV ERAVKQRQEA QELARQVARE KAIANAQKRE AYLKAKYGKD YLTREQFLKL SPEERAAHVA KMKQLKLVKN DNGRDN // ID SECG_MYCPN Reviewed; 76 AA. AC Q9EXD0; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Probable protein-export membrane protein SecG; GN Name=secG; OrderedLocusNames=MPN_242; ORFNames=MP589.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- FUNCTION: Involved in protein export. Participates in an early CC event of protein translocation (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SecG 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; U00089; AAG34757.1; -; Genomic_DNA. DR RefSeq; NP_109930.1; NC_000912.1. DR RefSeq; WP_010874599.1; NC_000912.1. DR EnsemblBacteria; AAG34757; AAG34757; MPN_242. DR GeneID; 877254; -. DR KEGG; mpn:MPN242; -. DR PATRIC; 20021809; VBIMycPne110_0261. DR KO; K03075; -. DR OMA; IVMFIMA; -. DR OrthoDB; EOG6DC6SJ; -. DR BioCyc; MPNE272634:GJ6Z-249-MONOMER; -. DR Proteomes; UP000000808; 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: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 TIGRFAMs; TIGR00810; secG; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 76 Probable protein-export membrane protein FT SecG. FT /FTId=PRO_0000157232. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. SQ SEQUENCE 76 AA; 8345 MW; 18D0AF4AE7635C55 CRC64; MDAIQIVMFV MAILCLIIGL LLSNHGSTGG LASLSGQDLE IFRKTKDRGI VKILQITMFI LVVLFLILGL VFHFAL // ID SIGA_MYCPN Reviewed; 499 AA. AC P78022; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963}; DE AltName: Full=Sigma-A; GN Name=sigA {ECO:0000255|HAMAP-Rule:MF_00963}; Synonyms=rpoD; GN OrderedLocusNames=MPN_352; ORFNames=MP484; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP-Rule:MF_00963}. CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic CC core. {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00963}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96132.1; -; Genomic_DNA. DR PIR; S73810; S73810. DR RefSeq; NP_110040.1; NC_000912.1. DR RefSeq; WP_010874708.1; NC_000912.1. DR ProteinModelPortal; P78022; -. DR SMR; P78022; 248-385. DR IntAct; P78022; 5. DR EnsemblBacteria; AAB96132; AAB96132; MPN_352. DR GeneID; 876928; -. DR KEGG; mpn:MPN352; -. DR PATRIC; 20022064; VBIMycPne110_0379. DR KO; K03086; -. DR OMA; YHEVLEA; -. DR OrthoDB; EOG6XHC70; -. DR BioCyc; MPNE272634:GJ6Z-369-MONOMER; -. DR Proteomes; UP000000808; 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; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007624; RNA_pol_sigma70_r3. DR InterPro; IPR007630; RNA_pol_sigma70_r4. 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; 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 Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Sigma factor; Transcription; Transcription regulation. FT CHAIN 1 499 RNA polymerase sigma factor SigA. FT /FTId=PRO_0000093900. FT DNA_BIND 453 472 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00963}. FT REGION 252 322 Sigma-70 factor domain-2. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 331 412 Sigma-70 factor domain-3. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 425 480 Sigma-70 factor domain-4. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT MOTIF 276 279 Interaction with polymerase core subunit FT RpoC. SQ SEQUENCE 499 AA; 57797 MW; 7981C3EBDEF7C1E1 CRC64; MSSPKKNFKK PQPKTENQKQ ALNEERIAEL KKSRILGKNR PFKKMIYVDT KAQRKQKHEN VAFLKTLQEN KESDVPKKRR GRKPKHAPLK EKNNLKLFDI LEGSLKSHTE NDDTNKVISL LVEVWEKKNK KKDNNSLSNK DIVNVLSKFE LPDDEIIFVL DELRDKGIEL PHDVEEHIHE FRANQDLSII DEDIEELTTK NISNRDKVDD NVRFFLGSLD SSKMLDFESE QRIAKVLNST DEESRKYAIN QLVTSNLRLV VSIAKKHLER GLDFNDLIQE GNLGLLKAIS KFNWSLGNKF STYATWWIKQ AITRAIADQA RTVRIPVHMV ETINRLAKAE RALNQELGRE PTAEELAEKM GGQAEGFTVK KIAEIKRLSL DPVSLDKTVG HDEESQFGDF VRDTDAQMPD EFTESRSNYE KIDELLNNCL SEQEELIVRM RIGMPPYNET KTLDEVSQKI KIPREKIRQI ETKAIRKLRQ AVRNNHMSLS FMRGNEKKD // ID SMC_MYCPN Reviewed; 982 AA. AC P75361; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894}; DE AltName: Full=Protein P115 homolog; GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; Synonyms=p115; GN OrderedLocusNames=MPN_426; ORFNames=MP415; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Required for chromosome condensation and partitioning. CC {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01894}. CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|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; U00089; AAB96063.1; -; Genomic_DNA. DR PIR; S73741; S73741. DR RefSeq; NP_110114.1; NC_000912.1. DR RefSeq; WP_010874782.1; NC_000912.1. DR ProteinModelPortal; P75361; -. DR IntAct; P75361; 3. DR EnsemblBacteria; AAB96063; AAB96063; MPN_426. DR GeneID; 876913; -. DR KEGG; mpn:MPN426; -. DR PATRIC; 20022248; VBIMycPne110_0461. DR KO; K03529; -. DR OMA; THRQGTM; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; MPNE272634:GJ6Z-455-MONOMER; -. DR Proteomes; UP000000808; 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; IPR010935; SMC_hinge. DR InterPro; IPR011890; SMC_prok. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR SUPFAM; SSF75553; SSF75553; 1. PE 3: Inferred from homology; KW ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 982 Chromosome partition protein Smc. FT /FTId=PRO_0000119027. FT NP_BIND 33 40 ATP. {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 171 235 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 263 377 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 568 627 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 669 713 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 753 818 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COMPBIAS 884 912 Ala/Asp-rich (DA-box). SQ SEQUENCE 982 AA; 110833 MW; C9D5F765B752E228 CRC64; MVFLKRFRAY GFKSYADEIT INFTHSMTGI VGPNGSGKSN VVDALKWVLG ERSMKHLRSK SGDDMIFFGS KDKPASKLAE VELTFDNSQK LLHDPRPEIS VMRRIYRGSG QSEYYINGEL VTLKEISGIF ADIGLEKGSL GIISQGSVSW FVEAKPEERR KIFEDASGIG RYTKRKEEVT NQLARTVQNL KQVSIVLNEL KKDLKKLTIQ ADKAQRFVKL KEELKELELS VLVADYLKSQ GELDRFNHQI GYIEQDFKLH EPQLQLLEDQ LNIFNQRFRD ADEQSIKLQQ ELQAVYQTIN ELEQRKAVID VQLKNELSKK DEKHKIQALK KLIRVDQAQL ESLQAQVLKT TSEITLLTNE LSTVQTELDT TKLNLNQNSA ALVYQQAQQE FLKAQNEEWV KTNPAHVLVK NVKALTGLLN TLNTFLKFEK QYEKALLKAL GKSIGYLVVN NNLAALKAID FLLTNQIGQV TFLPIDDIAF DTKIAPEHME ILQQLDGFLG VGSDHVSCDE SLQPIVNALL GQVIIASDLQ AALKLSSYTY KLYRVVTLNG ETVYAGGIIQ GGYVKDNLSL YNLQEKLASS EANITQLEHN EKQLRTNLTS LETKLNELNK KLKYEEILLE KFNERVNHTN KAILSYKIEY EQLTNESFDG TPHSFDETRL VESLNRAWAE RDELNSQLKL NQELKETLAK SIKLAEAKTA DLRALLDEQR SQLVLAREGK IRFENTIHNI TDKINGGYKL TMEFAIANYN KPIKLSTMQA QNKIARMQSQ LDEMGPINLE SIAEIADKQK RFDDINGEYE SLQTAIKDLQ TAIGEIDELA CKEFDELIQK VNAELPKTFN YLFGGGSCQI RYTDTDNVLL SGIEVFANPP GKNVANLMLL SGGEKTLVAL SVLFSILRVS AFPLVILDEA ESALDPANVE RFANIIGNSS NNTQFLIITH RQGTMMKCDM LLGAAMQTKG VTKTFAVSLE KAEQYISKDK QN // ID SSB_MYCPN Reviewed; 166 AA. AC P75542; Q50347; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Single-stranded DNA-binding protein; DE Short=SSB; GN Name=ssb; OrderedLocusNames=MPN_229; ORFNames=MP602; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-158. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|PROSITE- CC ProRule:PRU00252}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96250.1; -; Genomic_DNA. DR EMBL; Z32660; CAA83579.1; -; Genomic_DNA. DR PIR; S73928; S73928. DR RefSeq; NP_109917.1; NC_000912.1. DR RefSeq; WP_010874586.1; NC_000912.1. DR ProteinModelPortal; P75542; -. DR IntAct; P75542; 1. DR EnsemblBacteria; AAB96250; AAB96250; MPN_229. DR GeneID; 877060; -. DR KEGG; mpn:MPN229; -. DR PATRIC; 20021783; VBIMycPne110_0248. DR KO; K03111; -. DR OMA; PIFENDV; -. DR OrthoDB; EOG6M9F32; -. DR BioCyc; MPNE272634:GJ6Z-236-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF002070; SSB; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 166 Single-stranded DNA-binding protein. FT /FTId=PRO_0000096064. FT DOMAIN 1 103 SSB. {ECO:0000255|PROSITE- FT ProRule:PRU00252}. FT COMPBIAS 160 166 Asp/Glu-rich (acidic). FT CONFLICT 158 158 Q -> N (in Ref. 2; CAA83579). FT {ECO:0000305}. SQ SEQUENCE 166 AA; 18424 MW; 12ED9C88C0E6FE10 CRC64; MNRVFLFGKL SFDPNKLQTR TNNIGASFSL ACIDSSGFND SKSYIRITAW GKVASFVLTL KPGDSVFVEG RLSTYKMNNR SDDPNSKATY ALQVIADKVY RPDEENSLEQ PVDKATVIDS PFLAAKTNAT ENELAQAFPI SLDDEDDDIN PILNNDSQLE EESDDE // ID SPOT_MYCPN Reviewed; 733 AA. AC P75386; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Probable guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; DE EC=3.1.7.2; DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase; DE Short=(ppGpp)ase; GN Name=spoT; OrderedLocusNames=MPN_397; ORFNames=MP441; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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. This enzyme catalyzes the CC degradation of ppGpp into GDP. It may also be capable of CC catalyzing the synthesis of ppGpp (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Guanosine 3',5'-bis(diphosphate) + H(2)O = CC guanosine 5'-diphosphate + diphosphate. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: CC step 1/1. CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HD 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; U00089; AAB96089.1; -; Genomic_DNA. DR PIR; S73767; S73767. DR RefSeq; NP_110085.1; NC_000912.1. DR RefSeq; WP_010874753.1; NC_000912.1. DR ProteinModelPortal; P75386; -. DR IntAct; P75386; 4. DR EnsemblBacteria; AAB96089; AAB96089; MPN_397. DR GeneID; 877121; -. DR KEGG; mpn:MPN397; -. DR PATRIC; 20022170; VBIMycPne110_0428. DR OMA; IIVENEF; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; MPNE272634:GJ6Z-420-MONOMER; -. DR UniPathway; UPA00908; UER00886. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Reference proteome. FT CHAIN 1 733 Probable guanosine-3',5'-bis(diphosphate) FT 3'-pyrophosphohydrolase. FT /FTId=PRO_0000166573. FT DOMAIN 62 167 HD. SQ SEQUENCE 733 AA; 86404 MW; 8F45E41A34BB3940 CRC64; MFYNWLKLYK FSKMATLVEI ERDFLQKTAQ KFAPEVVALI TKALDYSKKW HGEQKRLSGE PFFIHPLRTA LRLVEWNMDS NTVCAGLLHD IIEDTQVTEA DLTAIFGKEI TDLVVKVTKI TSESKKQRQL NRKKEDLNLK SLVNIAMSSQ QEVNALVLKL ADRLDNISSI EFLAVEKQKI IAKETLELYA KIAGRIGMYP VKTQLADLSF KVLDPKNFNN TLSKINQQKV FYDNEWGNFK KQLEEMLEQN QIEYRLESRI KGIYSTYQKL TFHEQNIAKI HDLFAIRLIV KSELDCYHLL GLIHLNFTVL MKHFKDYIAS PKQNFYQSIH TTVRLKGLNV EIQIRTQRMD HVSKYGFASH WIYKEKKEGL LASALQVNYL NSKQMHSRDF FKRIFGTDII KVNVSSDNEP NIVKKLNVES NSKLLDIAYE LYPKQFNKLE KIKLDGVEVM SFDVTAENEM VIEFCFGKTN NLKRRWLRYM NNHVFRERVK KDLNKLKKAV KYSELPLYEK ALEELHLKLA DETQIKQRLN ALGIKKLTEF LELIEYPHFP KNEHLYFLAS NNQKWRELIK PIKFALSQAV FQNSYFEQIE GIYITKIVIE TCCTKIPDMP EQVIGILMKN ILRVHLHDCR ELANQKQPKI IPLYWNAHQL KMRPRKFRCQ INIRGVWSET TVNKIVQTII EGDSYLERII PKIDKQKDEF ELNITMFIDN YHQLITIMEQ ITTKNISYVW KYL // ID SRP54_MYCPN Reviewed; 450 AA. AC P75054; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=MPN_061; GN ORFNames=MP093; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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. {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. CC {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000255|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; U00089; AAB95741.1; -; Genomic_DNA. DR PIR; S73419; S73419. DR RefSeq; NP_109749.1; NC_000912.1. DR RefSeq; WP_010874418.1; NC_000912.1. DR ProteinModelPortal; P75054; -. DR IntAct; P75054; 4. DR PRIDE; P75054; -. DR EnsemblBacteria; AAB95741; AAB95741; MPN_061. DR GeneID; 876948; -. DR KEGG; mpn:MPN061; -. DR PATRIC; 20021401; VBIMycPne110_0062. DR KO; K03106; -. DR OMA; QFHPERI; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; MPNE272634:GJ6Z-63-MONOMER; -. DR Proteomes; UP000000808; 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; SSF47364; SSF47364; 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 Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; KW Reference proteome; Ribonucleoprotein; RNA-binding; KW Signal recognition particle. FT CHAIN 1 450 Signal recognition particle protein. FT /FTId=PRO_0000101161. FT NP_BIND 106 113 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 188 192 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 246 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. SQ SEQUENCE 450 AA; 50141 MW; 7EFE42ECEA4FE679 CRC64; MFKSMISSIV MRSMQKKINA QTISETDVQA VLKEIRIALL DADVNLLVVK NFIKAIREQT VGQTVEPGQD LQKWLLKVIK QELINILSQP NQEITSKRPL KVMVVGLQGS GKTTTCGKLA VWLKKQFQQK AMLVALDIYR PAAIDQLATL AEQTESVFFA KGTQAPDQTT KEAVKTFKES GCQAIICDTA GRLQTNQELM DELVAIKNEL HPDEILMVVD GLSGQEIINV AKEFHNRLKL TGFIITKLDS DARAGAALSL TSLLEVPIKL MGTSEKLTGL EQFHPERIAS RILGLGDVMT LVEKAEEVFD KQSLTKTVSK MFLGKMDLED LLLYMEQMNQ MGSVSSIVKM LPGNLTVSDD HVESIEAKVK LWKVLINSMT REERRHPKLI NRDPSRKQRI IKGSGRKMDE LNKLMKEWSK LQTKTAEMGR MLKGGKNPFS GFGGLGGLGF // ID SYA_MYCPN Reviewed; 900 AA. AC P75368; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. 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=MPN_419; ORFNames=MP422; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96070.1; -; Genomic_DNA. DR PIR; S73748; S73748. DR RefSeq; NP_110107.1; NC_000912.1. DR RefSeq; WP_010874775.1; NC_000912.1. DR ProteinModelPortal; P75368; -. DR IntAct; P75368; 3. DR EnsemblBacteria; AAB96070; AAB96070; MPN_419. DR GeneID; 877316; -. DR KEGG; mpn:MPN418; -. DR PATRIC; 20022234; VBIMycPne110_0454. DR KO; K01872; -. DR OMA; LDVTHYK; -. DR OrthoDB; EOG6Q2SQ2; -. DR BioCyc; MPNE272634:GJ6Z-448-MONOMER; -. DR Proteomes; UP000000808; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. 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 1 900 Alanine--tRNA ligase. FT /FTId=PRO_0000075156. FT METAL 567 567 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 571 571 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 671 671 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 675 675 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. SQ SEQUENCE 900 AA; 103635 MW; 59C1A9F5A0140E6E CRC64; MKWTTDKVRQ TWLDYFTAKG HLALPSKSLI PVNDPSLLWI NSGVATLKDY FSAKKTPPSK RLANAQICLR VNDIENVGFT SRHQTLFEML GNFSIGDYFK EEAIGFANDL LVNHYHLDPK RFYITVYQDD ELTFNTWLKH GIPASRIIKC DRDRNFWDLG LGPCGPCTEI YYDRGERFDP HKVGEKLFFE DIENDRYVEV WNIVFSQFNN DGNGNYSELA QKNIDTGAGI ERLVAILQDA PTNFDTDIFL KLIGIIEQHC KHKYDTNLYF KFDQKLNEAQ SAFRIISDHF KAITFTIAEG VLPGPNERSY IVRRLLRRAL LACKKLDLDL KFIDPMVDAI ISVYGSYYQQ LQGKNQVVQQ AIWKEVTAFD KTINLGLMLF EKSIAHNALQ PQVAFQLYET YGFPIEMIKE LVDKRQLQVD WKAVEQLMEQ HRLISKQNSN TLSFEKQNEH LVNFKTASEF LYEANEITAK VIGLFDEQYQ PVQKLHNQSG YVVFDQTVLY ATSGGQRYDE GYCINHSQND QRVSFQGVFK GPNKQHFHFF LTGSFQLGDK VILVHDGKWR QLVKNNHSLE HLLHAALQNE IDPLIKQDGA FKSAQKATID FNFSRALTWA ELERVEHRIR QIIQQDIQRE EIFTDLEGSQ KLNAIAYFEE EYSNHELLRV IRFGDFSVEL CGGTHVEHTG LIENCFITDY YARGTGRWRI EIISSNETIA AYLNEQNGKL SETINSLHNT LNNIANPALN KQKTALTKQL NHFHLPQVIT DLRKCQALLN ELKITVNELK TEDFKWKQKQ LAEKIKQELL ELAKQDKAYV LASFAAVDPK LLSQVAQAVL NQHKNKLFVL LNQFNNSPSF MLLGQDVSKC IQLLKAHFEL KGGGSNNFFR GSFNESVDVS KLQAILDTLQ // ID SSRP_MYCPN Reviewed; 147 AA. AC P75043; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. 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=MPN_074; ORFNames=MP081; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 29342 / M129; RX PubMed=10591650; DOI=10.1126/science.286.5447.2165; RA Hutchison C.A., Peterson S.N., Gill S.R., Cline R.T., White O., RA Fraser C.M., Smith H.O., Venter J.C.; RT "Global transposon mutagenesis and a minimal Mycoplasma genome."; RL Science 286:2165-2169(1999). 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 -!- DISRUPTION PHENOTYPE: May not be essential, 1 disruption mutant CC has been isolated. {ECO:0000269|PubMed:10591650}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP- CC Rule:MF_00023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95729.1; -; Genomic_DNA. DR PIR; S73407; S73407. DR RefSeq; NP_109762.1; NC_000912.1. DR RefSeq; WP_010874431.1; NC_000912.1. DR ProteinModelPortal; P75043; -. DR EnsemblBacteria; AAB95729; AAB95729; MPN_074. DR GeneID; 876876; -. DR KEGG; mpn:MPN074; -. DR PATRIC; 20021427; VBIMycPne110_0075. DR KO; K03664; -. DR OMA; FLLNAHI; -. DR OrthoDB; EOG6HXJ9P; -. DR BioCyc; MPNE272634:GJ6Z-76-MONOMER; -. DR Proteomes; UP000000808; 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 1 147 SsrA-binding protein. FT /FTId=PRO_0000102989. SQ SEQUENCE 147 AA; 17087 MW; 6F4AF3E5A4412C40 CRC64; MRVLVNNPRA QYDYYLLTGY CAGLVLKGSE VKSLALGQGS LKEAYVFIDK HEVYIKDFSI SPYAFSGEFN HPFKRVKKLL LNRNEIKQIT ARQKQEGLSI IPLKVFFKNG KIKMEIWLAK PKKKFDKREA IKSKTIQREL RQQYGSP // ID SYI_MYCPN Reviewed; 861 AA. AC P75258; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. 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=MPN_520; ORFNames=MP322; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 -!- 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; U00089; AAB95970.1; -; Genomic_DNA. DR PIR; S73648; S73648. DR RefSeq; NP_110208.1; NC_000912.1. DR RefSeq; WP_010874876.1; NC_000912.1. DR ProteinModelPortal; P75258; -. DR EnsemblBacteria; AAB95970; AAB95970; MPN_520. DR GeneID; 876906; -. DR KEGG; mpn:MPN520; -. DR PATRIC; 20022500; VBIMycPne110_0577. DR KO; K01870; -. DR OMA; THGFIVD; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; MPNE272634:GJ6Z-561-MONOMER; -. DR Proteomes; UP000000808; 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: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 Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 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; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 861 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098424. FT MOTIF 57 67 "HIGH" region. FT MOTIF 590 594 "KMSKS" region. FT BINDING 549 549 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 593 593 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. SQ SEQUENCE 861 AA; 99527 MW; 6A521066C0EE235D CRC64; MNLKKTLLMP QTAFEMQGKL TTKEQQFQAF WQSKRIYQKL HRQNKDKPQK ILHDGPPYAN GNIHVGHALN KILKDFVLRS WNLQGFGTVF IPGWDCHGLP IEHAVSKKDP QHYASLSLSE KRDLCKQFAL SQIAIQKAQF QRLGLLNDFS KYYKTIDESF QQNELDLFLQ AVKKDLIFQA LKPTYWSPVS RTSLAEAEIE YKEVKTIGLY LTFTVVQSAV LNSGTKLLVW TTTPWTLPTN QAIAVHPQFE YLLFTYNNEQ YVVLASLFES LKTKFGWTDA IQVQTISGSQ LQNTTYKHCL YDKVNPVLLG NHVLCNEGTG LVHTSPAYGL DDFYLCKQNK LNEALVSLDE KGVFNDTLND PVLTGLFYLK ANDVIIERLK QHHNFVFSES FLHREPHDWR SKTPVIYRAS KQLFIKTKSI QSKLKRQIKR VKFVNNKNKE RLQEMLLQRA EWCISRQRVW GLPIPLIYAD NQPLLDVTTI KYTIQQLKKY GIDSWFEKDI NFFLNPKKIQ PGVEYKKETD TLEVWFDSGS TYNVLISNKL NFPADLYLEG SDQYRGWFNS SASCGIIQTD QLPFKSLISH GFTLDEHGNK MSKSLGNVVD PLKLCDQYGA DILRLWVTNV DWQVDNRIGD NIIKQIVEQY RRIRNSLLRF ILGNLNHFNF GEMKDYRFAL EDKIVIHKTN ALVQELHQWL KQYNFLNCLK AINKFVLWLS GWYFEIIKDT LYCDAKTNPN RVAKQAVLNY IFTQLIGFLN IFIPHTAEDA WQNYLLPKKP VSVNLFAGPA MFKVANVKGL DRLHESFSAI KDRAYAAIEQ ARQNGVITKN NQVVLTLGVD STSAIDPTSC KTFSSLAKRK PGKYNEWPQR N // ID SYK_MYCPN Reviewed; 489 AA. AC P75500; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Lysine--tRNA ligase; DE EC=6.1.1.6; DE AltName: Full=Lysyl-tRNA synthetase; DE Short=LysRS; GN Name=lysS; OrderedLocusNames=MPN_277; ORFNames=MP558; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96206.1; -; Genomic_DNA. DR PIR; S73884; S73884. DR RefSeq; NP_109965.1; NC_000912.1. DR RefSeq; WP_010874634.1; NC_000912.1. DR ProteinModelPortal; P75500; -. DR IntAct; P75500; 2. DR EnsemblBacteria; AAB96206; AAB96206; MPN_277. DR GeneID; 876870; -. DR KEGG; mpn:MPN277; -. DR PATRIC; 20021881; VBIMycPne110_0297. DR KO; K04567; -. DR OMA; MAQVADK; -. DR OrthoDB; EOG69PQ2M; -. DR BioCyc; MPNE272634:GJ6Z-284-MONOMER; -. DR Proteomes; UP000000808; 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 1 489 Lysine--tRNA ligase. FT /FTId=PRO_0000152651. FT METAL 399 399 Magnesium 1. {ECO:0000250}. FT METAL 406 406 Magnesium 1. {ECO:0000250}. FT METAL 406 406 Magnesium 2. {ECO:0000250}. SQ SEQUENCE 489 AA; 56081 MW; E3D643B73DEDBCA0 CRC64; MSDRLNDQAQ NRLQKLLNLK QTGNDPYLIT KIENTHSAAS FQKAFANQSD AELKQYQVIL TGRIIALRQT FIIIQDFSGK MQLYINKKTA PELFEYFNNY IDLGDQIVAT GHPMMTKTGV LTLNVERLQI VAKCLQTPPE KWHGLTDPEA RARKRYLDLT YNRAQVEVFL KRTQIITAIR TFLNEAGFLE VETPILQAVL GGANAKPFKT HYNALKGDFY LRIANEIALK KLIVGGLPKV YEMGRMFRNE GVDTTHNPEF TSIEMYQANA DYAVMMDLTE NLIKFVCKTL NQWSFNWNGQ TLDLAKPFKK VKMVDLICQV TGVNFDDVKD DQTAIALAKQ HKVELKKHEQ NKQHIINRFF EQFCEHTLIQ PTFVTHYPKA VSPLAKQDPH NPEFTERFEL FINTKELANA YSELNDPLEQ RARFEQQLQE KRMGNDEASE LDESFLDALS FGLPPTGGLG IGVDRLVMLL CECSSIRDVV FFPQLRELK // ID SYD_MYCPN Reviewed; 557 AA. AC P75068; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.12 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; GN OrderedLocusNames=MPN_046; ORFNames=MP108; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Asp) in a CC two-step reaction: aspartate is first activated by ATP to form CC Asp-AMP and then transferred to the acceptor end of tRNA(Asp). CC {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP + CC diphosphate + L-aspartyl-tRNA(Asp). {ECO:0000255|HAMAP- CC Rule:MF_00044}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95756.1; -; Genomic_DNA. DR PIR; S73434; S73434. DR RefSeq; NP_109734.1; NC_000912.1. DR RefSeq; WP_010874403.1; NC_000912.1. DR ProteinModelPortal; P75068; -. DR IntAct; P75068; 1. DR EnsemblBacteria; AAB95756; AAB95756; MPN_046. DR GeneID; 877157; -. DR KEGG; mpn:MPN046; -. DR PATRIC; 20021369; VBIMycPne110_0046. DR KO; K01876; -. DR OMA; YQLDVEM; -. DR OrthoDB; EOG68Q0NX; -. DR BioCyc; MPNE272634:GJ6Z-48-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1360.30; -; 1. DR HAMAP; MF_00044; Asp_tRNA_synth; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004524; Asp-tRNA-ligase_bac/mit. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR004115; GAD-like. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 2. DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 2. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF55261; SSF55261; 1. DR TIGRFAMs; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 557 Aspartate--tRNA ligase. FT /FTId=PRO_0000110907. FT NP_BIND 214 216 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 505 508 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 192 195 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 168 168 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 214 214 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 223 223 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 423 423 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 457 457 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 460 460 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 464 464 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. SQ SEQUENCE 557 AA; 64114 MW; 65EBE73A85F8A424 CRC64; MNLDNAKCFK QRVFIGNLTS EHLNKTVTIA GWVKRIKKLG ELNFVIVGDK TNTIQVTCKN KEQVKYLTRE DLVIVKGKLK RLDSVRFEIT NPTITLFAKS KTPPLIIEDK TDALEEVRLR YRYLDLRRPV MQKRLALRHK VTLAVRNWLD QMGFIEVETP TLTKSTPEGA RDFLVPARIR EHSFYALPQS PQIYKQLLMV GGTEKYFQIA HVYRDEDSRK DRQPEHTQID LEVAFYTKEM VMDLIQRLFV DVFRQVLNIK LKKPFPVLKF AEAFNRFGSD KPDLRYGFEL EDCTDLFQDS PNQFTNLINA GGIVGGIQLP NLYLDEVSFK ALRKLAKDNG VSLEFYSDKA SSLKQPLDLP LAGTILLVAH KSKTQAWTAL GAIRNELKYH LNLVKPNQYS FCWIVDFPLY EFDEKEQKWV SAHNMFSNPQ PQWLVNFENH KAEALSEQYD LVLNGFELGS GSIRIHDPEV QTRLMQSLGV DPQQFGFVME AYQYGAPVHA GMGLGLDRLM MIINNVDNIR EVMAFPKNAQ GIEMHTNAPD QVDIKDITTI WSKHPVK // ID SYFA_MYCPN Reviewed; 341 AA. AC P75564; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit; DE Short=PheRS; GN Name=pheS; OrderedLocusNames=MPN_105; ORFNames=MP049; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95697.1; -; Genomic_DNA. DR PIR; S73375; S73375. DR RefSeq; NP_109793.1; NC_000912.1. DR RefSeq; WP_010874462.1; NC_000912.1. DR ProteinModelPortal; P75564; -. DR IntAct; P75564; 2. DR EnsemblBacteria; AAB95697; AAB95697; MPN_105. DR GeneID; 877225; -. DR KEGG; mpn:MPN105; -. DR PATRIC; 20021507; VBIMycPne110_0111. DR KO; K01889; -. DR OMA; ICEGPEI; -. DR OrthoDB; EOG6WX4QN; -. DR BioCyc; MPNE272634:GJ6Z-111-MONOMER; -. DR Proteomes; UP000000808; 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; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR Pfam; PF01409; tRNA-synt_2d; 1. DR TIGRFAMs; TIGR00468; pheS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 341 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126731. FT METAL 254 254 Magnesium. {ECO:0000250}. SQ SEQUENCE 341 AA; 39241 MW; 3F8955E8B3EF916F CRC64; MIDQSKLIER WKTTFETAQN PTELLAFKNS FRNADLKPLL SQIKETTDIE TKRHLGQLYK QLESTLQTLH DTQLQVFTQA QSSSVLTHGD VMLLATSFAP GSSNIIYQVI DELVNYFKKF LFTVNYDSEL TTIADCFDLL NIPKDHPSRN LTDTFYLDKN RLLRTHCTAA TLRAVKETKK SNNPDIRIAS FGAVFRKDDD DATHSHQFNQ LDFMWIKKDF SLTNLKWFMQ NMINHIFGEN TSARFRLSHF PFTEPSFEID IRCWLCQNGC GVCKKTRWIE VLGAGILHPQ VMANMGFSDT DNIRGIAAGI GIERLVMLKH GISDIRDLYD NNFKFLAQFT D // ID SYC_MYCPN Reviewed; 437 AA. AC P75423; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Cysteine--tRNA ligase; DE EC=6.1.1.16; DE AltName: Full=Cysteinyl-tRNA synthetase; DE Short=CysRS; GN Name=cysS; OrderedLocusNames=MPN_356; ORFNames=MP480; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96128.1; -; Genomic_DNA. DR PIR; S73806; S73806. DR RefSeq; NP_110044.1; NC_000912.1. DR RefSeq; WP_010874712.1; NC_000912.1. DR ProteinModelPortal; P75423; -. DR EnsemblBacteria; AAB96128; AAB96128; MPN_356. DR GeneID; 876889; -. DR KEGG; mpn:MPN356; -. DR PATRIC; 20022072; VBIMycPne110_0383. DR KO; K01883; -. DR OMA; ENENAMH; -. DR OrthoDB; EOG6RVFXC; -. DR BioCyc; MPNE272634:GJ6Z-373-MONOMER; -. DR Proteomes; UP000000808; 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; 1. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. 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 1 437 Cysteine--tRNA ligase. FT /FTId=PRO_0000159433. FT MOTIF 33 43 "HIGH" region. FT MOTIF 262 266 "KMSKS" region. FT METAL 31 31 Zinc. {ECO:0000250}. FT METAL 205 205 Zinc. {ECO:0000250}. FT METAL 230 230 Zinc. {ECO:0000250}. FT METAL 234 234 Zinc. {ECO:0000250}. FT BINDING 265 265 ATP. {ECO:0000250}. SQ SEQUENCE 437 AA; 50665 MW; A94BE766B9A948BD CRC64; MNQFEPKFTL IDTVSNQSVV LEQKQINIYL CGPTVYNDLH LGNTRPLIVF DVLQRVLQAA QYKVQFVQNI TDIDDKIIKI AQQQEISEAQ LCKQQITAYK SLLKKLNILP IKHLQVTDKI DKMPGYIARL VKKGFAYVSP LGNTYFSVSQ LPQYGILANR VVETIEDEAT DKRNKLDFVL WKQTTAGVKW NSPWGWGRPG WHVECAFLID YSFKDQLTIH GGGVDLKFPH HENENAMHMA LYDKPLTQHW MHIGHLMFEN QKMSKSLQNF LLAVDFLTIH DFRILRWLFY QKHYYHPLDL SQSLIEQACS DIKRIQKAVN VCRTWFVYSE QSAIPAPKQF EPVFKALLNN LNFANAITHI WKLVKQINHD VSKQNLSGLK EHLSHLEWAL NILGIGFKSI HTKLNVQLIK KWASLRKNGQ LDKADEVRQK LIKKGLL // ID SYR_MYCPN Reviewed; 537 AA. AC P75222; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Arginine--tRNA ligase; DE EC=6.1.1.19; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=argS; OrderedLocusNames=MPN_556; ORFNames=MP286; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + CC diphosphate + L-arginyl-tRNA(Arg). CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95934.1; -; Genomic_DNA. DR PIR; S73612; S73612. DR RefSeq; NP_110245.1; NC_000912.1. DR RefSeq; WP_010874913.1; NC_000912.1. DR ProteinModelPortal; P75222; -. DR IntAct; P75222; 2. DR EnsemblBacteria; AAB95934; AAB95934; MPN_556. DR GeneID; 877288; -. DR KEGG; mpn:MPN556; -. DR PATRIC; 20022589; VBIMycPne110_0618. DR KO; K01887; -. DR OMA; QDLIYHL; -. DR OrthoDB; EOG6JB13C; -. DR BioCyc; MPNE272634:GJ6Z-601-MONOMER; -. DR Proteomes; UP000000808; 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; 3.40.50.620; -; 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; 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; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 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 1 537 Arginine--tRNA ligase. FT /FTId=PRO_0000151578. FT MOTIF 113 123 "HIGH" region. SQ SEQUENCE 537 AA; 62121 MW; 099B1C0DC33A39B2 CRC64; MLFINTDLQE CLNALNLEFD EHKELVKLVK NNSFSGFAST VVFHLKGVNQ KETAQQIAAW LLKHKKAHYR RVFVANNNFI NFEISPQKYL DFLKTKPTFA PKPTKVLIEW VSANPTGELH LGHVRNAFFG HVLNNLMVFL GFQTVREYWV NDYGQQARVF GFSVYQALHL QQNIKVTPHP DGYEGELVDS IAKTITGIPL DKLSFEEFLQ QPFLDQLLAD CTAKVLEVIK QDLATIHIHF DSWKFESQVV KETDYKKLLT QFKDEAHYEK DGAIWLKTTL YGDDKDRVLV RQDNRPSYFG TDVAYHLDKA ARGFDLLYDI WGSDHEGHIK RMHCVYEGLK IHQKCQLKIT ALQLVMLYKN KEIVRLSKRA GNVITIKQML QMLSEDAARW FMLSQTNNSI IKIDLDTANL QNSSNPVYYV QYAYARMCSV LKVVDQAALA QVNDCSLLTH EKEIALLDQL VYFKSLLEKV QVSHELHLLT NYLYETATLF HSWYKACKIN DPAQYNLTQQ RLLLLQSLHH VFGQLLQILN ITAPQQM // ID SYS_MYCPN Reviewed; 420 AA. AC P75107; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. 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=MPN_005; ORFNames=MP149; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95797.1; -; Genomic_DNA. DR PIR; S73475; S73475. DR RefSeq; NP_109693.1; NC_000912.1. DR RefSeq; WP_010874362.1; NC_000912.1. DR ProteinModelPortal; P75107; -. DR IntAct; P75107; 1. DR EnsemblBacteria; AAB95797; AAB95797; MPN_005. DR GeneID; 877292; -. DR KEGG; mpn:MPN005; -. DR PATRIC; 20021283; VBIMycPne110_0005. DR KO; K01875; -. DR OMA; NTVRESI; -. DR OrthoDB; EOG61KBH9; -. DR BioCyc; MPNE272634:GJ6Z-5-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000808; 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 1 420 Serine--tRNA ligase. FT /FTId=PRO_0000122083. FT NP_BIND 256 258 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT NP_BIND 343 346 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT REGION 225 227 Serine binding. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 279 279 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 379 379 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. SQ SEQUENCE 420 AA; 47924 MW; 9BC071823D20998E CRC64; MLDRNKLRNN LDFFKKKLVE RGVSESQFEA YVQADKAMRK LLHQIELANQ KQTLLAQQVA KKKGDPKLLK ESKELKQKLE QLNIAFKEAE TLSQELLLNL PNIADESVPV GRDETANLEL LKEGRKPVFD FTPLPHWELC ERLQLVAFDK ATKLTGARFV AYTDKAAKLL RAIASLMIDL NKNKYQEWNV PVIVNETSLT GTGQLPKFKD DVFKLENTRY YLSPTLEVQL ANLHANEIFT EGELPKYYTA TGVNFRQEAG SAGKQTKGTI RLHQFQKVEL VKFCKPSEAI HELEEMTRDA EQILLELKIP FRRLLLCSGD MGFSAQKTYD LEVWMAGCNE YREVSSCSSC GDFQARRAMI RYKDLTTGKN TYVATLNGTA LAIDRIFAAI LEHYQTKAGE VMIPQALLKY LDFDKITKPK // ID T1SC_MYCPN Reviewed; 268 AA. AC P75416; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_365; DE AltName: Full=S.MpnORFCP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_365; DE Short=S protein; GN OrderedLocusNames=MPN_365; ORFNames=H91_orf268, MP471; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB96119.1; -; Genomic_DNA. DR PIR; S73797; S73797. DR ProteinModelPortal; P75416; -. DR IntAct; P75416; 4. DR REBASE; 6706; S.MpnORF365P. DR EnsemblBacteria; AAB96119; AAB96119; MPN_365. DR PATRIC; 20022096; VBIMycPne110_0392. DR OMA; NNACVIP; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-385-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 268 Putative type-1 restriction enzyme FT specificity protein MPN_365. FT /FTId=PRO_0000198046. SQ SEQUENCE 268 AA; 31147 MW; 2B7E2D3F826824DA CRC64; MEAPKHVNNA CVIPNLTLKK MREIELDFPS KKIQEKIATI LDTFTELSAE LRERKKQYAF YRDYLLNQEN IRKIYGANIP FETFQVKDIC EIRRGRAITK AYIRNNPGEN PVYSAATTND GELGRIKDCD FDGEYITWTT NGYAGVVFYR NGKFNASQDC GVLKVKNKKI CTKFLSFLLK IEAPKFVHNL ASRPKLSQKV MAEIELSFPP LEIQEKIADI LFAFEKLCND LVEGIPAEVE MRKKQLDYYQ NFLFNWVQEQ KTQLEQIM // ID T1SF_MYCPN Reviewed; 238 AA. AC Q50287; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_201; DE AltName: Full=S.MpnORFFP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_201; DE Short=S protein; GN OrderedLocusNames=MPN_201; ORFNames=GT9_orf238, MP630; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U34795; AAC43680.1; -; Genomic_DNA. DR EMBL; U00089; AAB96278.1; -; Genomic_DNA. DR PIR; S62809; S62809. DR ProteinModelPortal; Q50287; -. DR REBASE; 6700; S.MpnORF201P. DR EnsemblBacteria; AAB96278; AAB96278; MPN_201. DR PATRIC; 20021727; VBIMycPne110_0220. DR OMA; DGELGHI; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-208-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 238 Putative type-1 restriction enzyme FT specificity protein MPN_201. FT /FTId=PRO_0000198050. SQ SEQUENCE 238 AA; 27550 MW; 2A5188B9DFC701F5 CRC64; MAEIPIDFPP LKIQEKIATI LDTFTELRAR KKQYAFYRDY LLNQENIRKI YGANIPFETF QVKDICEIRR GRAITKAYIR NNPGENPVYS AATTNDGELG HIKDCDFDGE YITWTTNGYA GVVFYRNGKF NASQDCGVLK VKNKKICTKF LSLLLEIEAT KFVHNLASRP KLSQKVMAEI ELSFPPLEIQ EKIADILCAF EKLCNDLVEG IPAEIELRKK QLDYYQNFLF NWVQKIRN // ID T1SX_MYCPN Reviewed; 375 AA. AC P75159; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative type I restriction enzyme specificity protein MPN_638; DE Short=S protein; GN OrderedLocusNames=MPN_638; ORFNames=E30_orf375, MP204; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2259703, EBI-2259703; CC P75310:MPN_474; NbExp=1; IntAct=EBI-2259703, EBI-2260075; CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB95852.1; -; Genomic_DNA. DR PIR; S73530; S73530. DR RefSeq; NP_110327.1; NC_000912.1. DR RefSeq; WP_010874995.1; NC_000912.1. DR ProteinModelPortal; P75159; -. DR SMR; P75159; 1-375. DR IntAct; P75159; 1. DR REBASE; 6863; S.MpnORF638P. DR EnsemblBacteria; AAB95852; AAB95852; MPN_638. DR GeneID; 876991; -. DR KEGG; mpn:MPN638; -. DR PATRIC; 20022757; VBIMycPne110_0701. DR OMA; RDEYAHK; -. DR OrthoDB; EOG654P1V; -. DR BioCyc; MPNE272634:GJ6Z-684-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 375 Putative type I restriction enzyme FT specificity protein MPN_638. FT /FTId=PRO_0000198043. SQ SEQUENCE 375 AA; 42650 MW; 4DBAE8BED64A45FA CRC64; MTPKLKLNTN SNWTKKTLGS LFELKKGEML EKELLAPDGK YEYFNGGIKA SGRTNEFNTF KNTISIIIGG SCGYVRLADK DYFCGQSSCT LTVLDPLEID LKFAYYALKS QEEKITSLAS GTTIKNIRLS DLKDLPIPLV KSIQDQRTIA HALSVFDLRI EHLNELIEVN RKLRDEYAHK LFTLDPDFLT HWNLHELHEQ MGEISLGEVF HLKSGKYLKA DERFEDGKFP YYGAGIESTS FVNEPNTKGD TLSMIANGYS IGNIRYHTIP WFNGTGGIAM EALKPNKTYV PFFYCALKYM QKDLKERFKR DESPFISLKL AGEIKVPFVK SFALQRKAGK IIYLLDKTLE ECKEEAKSLI SIRDNLLGKL FPTLS // ID SYE_MYCPN Reviewed; 484 AA. AC P75114; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. 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=MPN_678; ORFNames=MP164; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95812.1; -; Genomic_DNA. DR PIR; S73490; S73490. DR RefSeq; NP_110367.1; NC_000912.1. DR RefSeq; WP_010875035.1; NC_000912.1. DR ProteinModelPortal; P75114; -. DR IntAct; P75114; 2. DR EnsemblBacteria; AAB95812; AAB95812; MPN_678. DR GeneID; 877376; -. DR KEGG; mpn:MPN678; -. DR PATRIC; 20022845; VBIMycPne110_0745. DR KO; K01885; -. DR OMA; NWINSQY; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; MPNE272634:GJ6Z-724-MONOMER; -. DR Proteomes; UP000000808; 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 1 484 Glutamate--tRNA ligase. FT /FTId=PRO_0000119608. FT MOTIF 10 20 "HIGH" region. FT MOTIF 252 256 "KMSKS" region. FT BINDING 255 255 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}. SQ SEQUENCE 484 AA; 55621 MW; FD7B7F4742B09A50 CRC64; MEKIRTRYAP SPTGYLHVGG ARTAIFNFLL AKHFNGEFII RIEDTDTERN VEGGIESQLE NLRWLGIIPD ESIYNPGNYG PYIQSQKLAT YKKLAYELVG KGLAYRCFCT KEKLEHERQL ALEHHQTPKY LGTCRNLHSK HIQTNLDNQV PFTIRLKINQ DAEFAWNDQV RGKITIPGNS LTDIVLLKAN GIATYNFAVV IDDHDMEITD VLRGAEHISN TAYQLAINQA LGYQRIPRFG HLSVIVDKSG KKLSKRDTKT IQFIEQFKQE GYLPEAVVNF LALLGWNSDF NREFFTINQL IESFTVNRVV GAPAFFDIKK LQWINAHYIK ELSDNAYFNF IDNYLTIDFD YLKNKRKEVS LLFKNQLAFG IEINQLIKET FAPKLGVQHL SVKHRELFKE LQSALQQLSE QLQALPDWTK DNVKSTLTQI GEQFNLKGKK LFMPLRLIFT NKEHGPDLAG IMVLHGKTQV LALLQEFIHA TNLF // ID SYFB_MYCPN Reviewed; 805 AA. AC P75563; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit; DE Short=PheRS; GN Name=pheT; OrderedLocusNames=MPN_106; ORFNames=MP048; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95696.1; -; Genomic_DNA. DR PIR; S73374; S73374. DR RefSeq; NP_109794.1; NC_000912.1. DR RefSeq; WP_010874463.1; NC_000912.1. DR ProteinModelPortal; P75563; -. DR IntAct; P75563; 6. DR EnsemblBacteria; AAB95696; AAB95696; MPN_106. DR GeneID; 877228; -. DR KEGG; mpn:MPN106; -. DR PATRIC; 20021509; VBIMycPne110_0112. DR KO; K01890; -. DR OMA; YFRFYGY; -. DR OrthoDB; EOG6CCH1J; -. DR BioCyc; MPNE272634:GJ6Z-112-MONOMER; -. DR Proteomes; UP000000808; 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 Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.56.20; -; 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; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 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 1 805 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000126915. FT DOMAIN 40 162 tRNA-binding. FT DOMAIN 412 486 B5. FT METAL 464 464 Magnesium. {ECO:0000250}. FT METAL 470 470 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 473 473 Magnesium. {ECO:0000250}. FT METAL 474 474 Magnesium. {ECO:0000250}. SQ SEQUENCE 805 AA; 91714 MW; 937B7614E789547A CRC64; MLISKKTLAV LIPEITHVSN NEICEKLQQI GIEVEAIRAF KNPDYLQLGI LRAVTPHPHD NHLYVCQVQI DKNKQLNVVT GAVNIVDPNN LNKHVIVAKK GAELLNGLII KTKNIKGIIS DGMLCSYVDI NPFSKHLIAD GDDTHAIVLD NINRDEFGDY LSFLNLDDVV FEVTLPTNRS DLQSLIFLAK ELAAVLKRPV FLEQKTTMTL REFYRFPLNL RNRAQANFFG GLFLRDVAIT SSPWTTKGLL INQELRPVNC FVDQANMVTV YTGQPIHCHD ADKIHGSVEL KLATQLETML ALDNKEYEIK PGDLVVADEQ GTIAIVGIIG SKRTMVDNTT NNIFFEVVNY NHERIKQTAQ RLGVANFASR LMSKPISLQA TENCLNYLQN NFLNPESIGK ISKFSSTIKA PAFNRKIYLN FNQLRELIGV TKKQLNDHMI RNYLTSLGFK MENQIARAPA YRQDITVWQD ISEELLKILD LNKIKEDEIL SSTKLEKHEK LNAYDALQKL RTKLQTLGFH NVITYQLISP ERARNFNLFG LSNLWEIKNP LSNERSVLRV GLIDSLLRVI QKNAAYKNKL GNIFEFSFVK TKDSNQLHIA ALWLEKMFGS TYQKDQGVSV DIPAMKGLAQ LIISNFGFNC DFEPITEGEY FTKNVGLKLV VFNEQIGYVG LIKDELLAPY DLKGRPVYGL EINLDRLLNS LNRLERSYTP ISKLQDVFKD ITFSFPRDES HFETFVKAIK KLQTIFKWEL ISVFDTEKDG VPITKYTVRY YLKNFTNTPL TLEQIKAVET QLKQQCELAK IALDL // ID SYG_MYCPN Reviewed; 449 AA. AC P75425; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253}; DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253}; GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; Synonyms=glyS; GN OrderedLocusNames=MPN_354; ORFNames=MP482; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96130.1; -; Genomic_DNA. DR PIR; S73808; S73808. DR RefSeq; NP_110042.1; NC_000912.1. DR RefSeq; WP_010874710.1; NC_000912.1. DR ProteinModelPortal; P75425; -. DR IntAct; P75425; 1. DR EnsemblBacteria; AAB96130; AAB96130; MPN_354. DR GeneID; 876926; -. DR KEGG; mpn:MPN354; -. DR PATRIC; 20022068; VBIMycPne110_0381. DR KO; K01880; -. DR OMA; TQQGVVE; -. DR OrthoDB; EOG6R87F8; -. DR BioCyc; MPNE272634:GJ6Z-371-MONOMER; -. DR Proteomes; UP000000808; 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; ISS:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR022961; Gly_tRNA_ligase_bac. DR InterPro; IPR002315; tRNA-synt_gly. DR PANTHER; PTHR10745; PTHR10745; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00389; glyS_dimeric; 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 1 449 Glycine--tRNA ligase. FT /FTId=PRO_0000072968. FT NP_BIND 190 192 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 200 205 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 275 276 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 319 322 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT REGION 205 209 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT REGION 315 319 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 100 100 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 158 158 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. SQ SEQUENCE 449 AA; 52304 MW; B6FFACD1550C27A5 CRC64; MAQVYSQEVY VQYLKRYGFV FQSSELYNGL ANSWDFGPLG AVLKQQIKTA LYNFFIKNKR DVLLIDTPII LNEQIWKASG HLANFTDALV DCKSCKLRFR VDHLDEQIKS ATQWNPKQVN CPNCKANNWS EVRDFNLLFQ TEIGVVNSEK RLVYLRPETA QGIFINFKQL LQLKKRPLPF GVAQFGKSFR NEVTPGNFLF RVREFEQFEM EWFCNPQASL SVFESQQQAI AHFLFKVLQL NPALVKQYEY DKNELAHYAN KTVDFLFQFP HGLRELWGLA DRGTFDLEQH QKYAKKPLDF FDGENNEHFI PAVVEPSVGI ERLFYALIVS SYQQEQLEGE MREVLRLPFH LCPEQIVVLP LVNKLKETAQ TLFEALSQTH WRIGFESAGS IGKRYRKADA IGTKFAITFD FESLEDQAVT IRERDSLKQV RVPIKELKAW FAQHDDQSH // ID SYL_MYCPN Reviewed; 793 AA. AC P75398; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 104. 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=MPN_384; ORFNames=MP453; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96101.1; -; Genomic_DNA. DR PIR; S73779; S73779. DR RefSeq; NP_110072.1; NC_000912.1. DR RefSeq; WP_010874740.1; NC_000912.1. DR ProteinModelPortal; P75398; -. DR EnsemblBacteria; AAB96101; AAB96101; MPN_384. DR GeneID; 877105; -. DR KEGG; mpn:MPN384; -. DR PATRIC; 20022144; VBIMycPne110_0415. DR KO; K01869; -. DR OMA; EGAHRFI; -. DR OrthoDB; EOG63Z74X; -. DR BioCyc; MPNE272634:GJ6Z-405-MONOMER; -. DR Proteomes; UP000000808; 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; -; 2. 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; 4. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. 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 1 793 Leucine--tRNA ligase. FT /FTId=PRO_0000152050. FT MOTIF 39 50 "HIGH" region. FT MOTIF 569 573 "KMSKS" region. FT BINDING 572 572 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. SQ SEQUENCE 793 AA; 91084 MW; DAD90195932B62D9 CRC64; MYNHNLLEEK WLQLWKTKQV NRFFDDKTKP KYYILDMFPY PSAAGLHLGH VRAYTITDVL SRYHKAKGFN VIHPIGFDAF GLPAEQYAIA SNKHPGDWTD KNITNFIEQL TAFGFDYDYQ LSLKTTDPRY YQYTQWIFGQ LFEAGLAEVK EIDVNWCAEL GTVLANEEVL IDSNGNAVSE RGEFPVTKRK MKQWVLKITA FAESLLNGLA ELDWHQSIKE MQTNWIGKSE GVEVTFDIEN SKETITIFTT KVQTIFGVTF LALSNSHPLV KEVAKTNPKI AQFLQKQAQK TTTVKQPETL HDGVDLKLKA INPATNTAIP LYVANYVVEG YGTDAVMGVP AHNENDNFFA RKQKLPIITV IDKQERLQHS GQFSGLNSQT ANTQITQMLV ERQKAKKTTV YKLRDWIFSR QRYWGEPFPI LFDENNQPHL VKELPVTLPA LANYQPDGST NPPLWRNQEW AKVKQGNQTF TRETSTMPQW AGSCWYYLGY LMLINNENFW PIDSREAKDL FERYLPVDLY VGGAEHAVLH LLYARFWHQF LYQKGIVTTK EPFKKLINQG MVLGPDGKKM SKSKGNTINP TPLIDSHGAD ALRLYLMFMG PISAALTWLD DGLNGMRRWL DRVHNFFHKE NIIKETVDQE TVYGYNLFLK RSFEHLEKQE LNLVISQMMI FLNLLYKTKQ LTLAYAKGFL TVLSFFAPYL AEELNAKLGM EPFIVHAQLP NVDNSVLETD KVKIILSVNG RFKGTKEFAK GVDEQTVLKA FKTDPEFQAL FDQPLARVVF VPNRIINVLL KSE // ID SYP_MYCPN Reviewed; 483 AA. AC P75382; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571}; DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571}; DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571}; GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; GN OrderedLocusNames=MPN_402; ORFNames=MP436; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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). CC {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP- CC Rule:MF_01571}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the anticodon-binding domain and the C-terminal extension. CC {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96084.1; -; Genomic_DNA. DR PIR; S73762; S73762. DR RefSeq; NP_110090.1; NC_000912.1. DR RefSeq; WP_010874758.1; NC_000912.1. DR ProteinModelPortal; P75382; -. DR IntAct; P75382; 1. DR EnsemblBacteria; AAB96084; AAB96084; MPN_402. DR GeneID; 877119; -. DR KEGG; mpn:MPN402; -. DR PATRIC; 20022194; VBIMycPne110_0435. DR KO; K01881; -. DR OMA; GVNSESA; -. DR OrthoDB; EOG6G7R2R; -. DR BioCyc; MPNE272634:GJ6Z-430-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; 3.30.110.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type. DR InterPro; IPR016061; Pro-tRNA_ligase_II_C. DR InterPro; IPR017449; Pro-tRNA_synth_II. DR PANTHER; PTHR11451:SF6; PTHR11451:SF6; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF09180; ProRS-C_1; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SMART; SM00946; ProRS-C_1; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF64586; SSF64586; 1. DR TIGRFAMs; TIGR00408; proS_fam_I; 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 1 483 Proline--tRNA ligase. FT /FTId=PRO_0000139335. SQ SEQUENCE 483 AA; 55455 MW; D5F4205B325951A6 CRC64; MANKDQNLTL WYDQLLSKAQ LVSYGDVKGT NCFLPNSWNL WLQIQRLYNN ATALIKLKDK VILKQFIPIE PLPYTVEQVQ LPTLSFYSEY QKEKRHVEGF NPELFLIEQI GTKKLHDPLV LRPTSEIAFC NLWKKQSFSY QNLPVIYNQW TCVFRAEKNT RPFLRNSEFY WQETHGLFSD GVNSESAAIA FWKLYQDIIV NQLCIPAFVG LKSPNERFAG AQNTWTVESI MPDGQALQCA TSHDLGQTFT KPFGLTFQNQ ANQQAIPYSF SCGISTRILG ALLLTHSDDF GLVLPWKVAP IQVKLYLFDK KGDTKTVELA QKVQTLLEQL AIRFQFIKVE NQLGKQLGQG EVNGIPFQLI VDNPQTVNIF NRLTRVKTAY SFEQLASRFV ELVQQYHQAM YDKAKAVVQQ KVVQATTLKQ IEQAFNDKKA VLCAVRLTDT LEQQLKERYQ VTVRCCLEQL QKPQICPFSG ESAQDYVLIA RAY // ID SYT_MYCPN Reviewed; 564 AA. AC P75225; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Threonine--tRNA ligase; DE EC=6.1.1.3; DE AltName: Full=Threonyl-tRNA synthetase; DE Short=ThrRS; GN Name=thrS; OrderedLocusNames=MPN_553; ORFNames=MP289; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95937.1; -; Genomic_DNA. DR PIR; S73615; S73615. DR RefSeq; NP_110242.1; NC_000912.1. DR RefSeq; WP_010874910.1; NC_000912.1. DR ProteinModelPortal; P75225; -. DR IntAct; P75225; 4. DR EnsemblBacteria; AAB95937; AAB95937; MPN_553. DR GeneID; 877305; -. DR KEGG; mpn:MPN553; -. DR PATRIC; 20022583; VBIMycPne110_0615. DR KO; K01868; -. DR OMA; DNSGREW; -. DR OrthoDB; EOG61KBFJ; -. DR BioCyc; MPNE272634:GJ6Z-598-MONOMER; -. DR Proteomes; UP000000808; 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; 3.40.50.800; -; 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; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55186; SSF55186; 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 1 564 Threonine--tRNA ligase. FT /FTId=PRO_0000101010. FT REGION 167 464 Catalytic. FT METAL 260 260 Zinc; catalytic. {ECO:0000250}. FT METAL 311 311 Zinc; catalytic. {ECO:0000250}. FT METAL 441 441 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 564 AA; 64922 MW; 0A2F531884CAD06D CRC64; MLAGVLLLQS WLKANYPQVQ FGSYGVQEGE FYLDFKVEKS FSIKEFEQLE QDLNAYFNQL NNVVQTKIDK TKSLKFFQAD PFTTTLIESI ESNSLVVTTV NEQTFWVHDL VLPLPKQGFV KLLNVSANYF LGDPTKPQLQ RLVGIFAASK EQLKSLIAAN EQKYQNDHRA IGKRLEIFTF DPLVGAGFPI WLEKGAVLKK IIGDFVHYQQ LMFGFKTVSS PVLANLELYK ISGHYVHYSE DMFPSVKLEN QMMMLRPMTC PHHCLIFKHK RRSYKELPQR FCEDSILHRF EASGGLTGLE RVRCMTLLDN HIFCRTDQIK AEIKNAFKLI QTVNNKFGFS FDRIDLALHD PNNKAKFIDN DQLWANSESQ IESVFKELNV PYKIDVGAAA FYGPKIDFQF KTALNKMITI ATIQLDFLLP ERFELRYFDE QSNAQTPVII HVGIVGTYER FIAALLEKTH GNLPLWMAPV QVVVIPVNID KHEKAAKKLY QKLLKENIRV SLDESEDRLG KKVRTAIVNK IPLQIIVGDK EMQDLTRITC RGFKGEKVQK LYWANFVKKV RKDG // ID SYV_MYCPN Reviewed; 838 AA. AC P75304; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 103. 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=MPN_480; ORFNames=MP361; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96009.1; -; Genomic_DNA. DR PIR; S73687; S73687. DR RefSeq; NP_110168.1; NC_000912.1. DR RefSeq; WP_010874836.1; NC_000912.1. DR ProteinModelPortal; P75304; -. DR IntAct; P75304; 1. DR EnsemblBacteria; AAB96009; AAB96009; MPN_480. DR GeneID; 877380; -. DR KEGG; mpn:MPN480; -. DR PATRIC; 20022384; VBIMycPne110_0519. DR KO; K01873; -. DR OMA; CETAISQ; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; MPNE272634:GJ6Z-521-MONOMER; -. DR Proteomes; UP000000808; 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; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. 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; 1. 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 1 838 Valine--tRNA ligase. FT /FTId=PRO_0000106231. FT COILED 768 838 {ECO:0000255|HAMAP-Rule:MF_02004}. FT MOTIF 46 56 "HIGH" region. FT MOTIF 514 518 "KMSKS" region. FT BINDING 517 517 ATP. {ECO:0000255|HAMAP-Rule:MF_02004}. SQ SEQUENCE 838 AA; 95720 MW; B44C80058F7F223C CRC64; MDKQFSFQGQ YDFKTVSTGL YDSWSSASFF KPQKNKVPFT AILPPPNLTG TLHIGHAFEV SITDQIMRFK RLRGYGVNWI PGFDHAGIAT QTKYEKLARE TNPEYFQAPR KQKVKMIMDW ALTQGDTIQS QIKSLGASLN WNQVNFTLSK KASQIVNDSF IQLFEQGFIY QAETLVNWDT KLNTAISNIE VINKPVDQQL YYIAYKLANN PKKRLVVATT RPETIFVDVC LFVHPKDKHY HSFVKQKVVN PLTGALMPVF TDSYVDKKFG TGVLKCTPAH DFNDFALNEK YRLPFVSCID HNGLLNEHAK QFTGLTVSAA RQQVVEFLQT QKLLVKTMPL TSNVGFSERS DTVVEPLLSK QWFVDLPKLK KALAIKKYPE LIPKRFNKQV TRWLSQLKPW CISRQLIWGH PIPVWTHKQS GALHVGSTAP TDKQNYTQST DVLDTWFSSS LWPLICLDWH KNKHFVPTDL LVTGYDILFF WVLRMTFNSY FQTKQLPFKQ VLIHGLVRDA QNRKMSKSLN NGINPMDLIR DYGADATRLF LTSNHTPGDD LIFNEQKLKS AANFLNKLWN VTKYVLQLGE QAKTVPSTHL PSTLSERWIW AKLKQLIVQT TKLLDKYQLA LANQALVNFI WNDFCNTFIE TIKQEDTALL PQLYTTAKTV LSTAVVMLST VTPFLAERIY QQFHSGSVMQ ASWPTAKAVK PPKLFADVVE AVSSLRHYKA NNQLVANQNL AVVLSGKAAP VVQNYFHFNW VDLRIEVNKT PGFQIKIVDN AANNLAHLEK QRSFYLAEVQ RSQAITTNPA FLKKAPPHKV KAELLKLEEY QKKLAEVNHL IAKLTKAE // ID SYH_MYCPN Reviewed; 414 AA. AC P75069; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Histidine--tRNA ligase; DE EC=6.1.1.21; DE AltName: Full=Histidyl-tRNA synthetase; DE Short=HisRS; GN Name=hisS; OrderedLocusNames=MPN_045; ORFNames=MP109; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + CC diphosphate + L-histidyl-tRNA(His). CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95757.1; -; Genomic_DNA. DR PIR; S73435; S73435. DR RefSeq; NP_109733.1; NC_000912.1. DR RefSeq; WP_010874402.1; NC_000912.1. DR ProteinModelPortal; P75069; -. DR EnsemblBacteria; AAB95757; AAB95757; MPN_045. DR GeneID; 877181; -. DR KEGG; mpn:MPN045; -. DR PATRIC; 20021367; VBIMycPne110_0045. DR KO; K01892; -. DR OMA; VRGMRDW; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; MPNE272634:GJ6Z-47-MONOMER; -. DR BRENDA; 6.1.1.21; 3534. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 414 Histidine--tRNA ligase. FT /FTId=PRO_0000136205. SQ SEQUENCE 414 AA; 47262 MW; 6FFC3C5F4C92B2D5 CRC64; MSVLQKPRGV KDWYGEELIY FNWTVHQITN LAWKWGFSEV KTPLLEYAEA FKRTNANADI VKKELYEFHD KSNRLLALRP EATAGIVRLV CENKLLQPQN YPLRLFTIGT MYRYERPQSN RYREHYQFSC EVIGDTNPTV LLDTLLLGHA IIQQLGIEGV ILKLNNLGNS ATIQQWNQAL QAYLTQFKAQ LTELSQSRLS TNPLRILDDK VDGQLPFISD APQIEQFLDA EQQALNTWLQ QQLTQQQVPF EWNPTLVRGL DYYTGVVFEF VKDDTTVLAG GVYDNLVEEL GGTPTKALGF ACGIERSINC LSAVKKQAIL ANQPPRLLVI GLTEAALEKL LQLSLGWRAY HPVTIYPKVI RIINGIRAAQ RLGYRFLGVI GGNNLEQQTI TVKDLATEQQ TTYTWDEFRQ RQVL // ID SYN_MYCPN Reviewed; 455 AA. AC P75521; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534}; DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534}; DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534}; DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534}; GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; GN OrderedLocusNames=MPN_252; ORFNames=MP580; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP + CC diphosphate + L-asparaginyl-tRNA(Asn). {ECO:0000255|HAMAP- CC Rule:MF_00534}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00534}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96228.1; -; Genomic_DNA. DR PIR; S73906; S73906. DR RefSeq; NP_109940.1; NC_000912.1. DR RefSeq; WP_010874609.1; NC_000912.1. DR ProteinModelPortal; P75521; -. DR IntAct; P75521; 3. DR EnsemblBacteria; AAB96228; AAB96228; MPN_252. DR GeneID; 877339; -. DR KEGG; mpn:MPN252; -. DR PATRIC; 20021829; VBIMycPne110_0271. DR KO; K01893; -. DR OMA; WWYLDTR; -. DR OrthoDB; EOG6ZSP6X; -. DR BioCyc; MPNE272634:GJ6Z-259-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00534; Asn_tRNA_synth; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004522; Asn-tRNA-ligase. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 1. DR PANTHER; PTHR22594:SF6; PTHR22594:SF6; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00457; asnS; 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 1 455 Asparagine--tRNA ligase. FT /FTId=PRO_0000176433. SQ SEQUENCE 455 AA; 51898 MW; 1AB74ADF708E09C9 CRC64; MSATAISDLF EKPAQFKNKK IKLTGWLKNK RTSANIIFLE VNDGSTLLNL QAVVKQDQPE LFALAESISL ASAVSVSGTV ALTPKSKQPL ELVVKQINVL STARADYPLQ KKEHSLEFFR NNAYLRVRAR TYFAIMKVRS LLSQAIFDYF FKNDFVLVHS PILTSNDCEG AGETFELKQG KEFFNKTTYL TVSGQFGAEC YAQAFKKVFT FGPTFRAEKS HTSRHLSEFW MIEPEVAFAN LKDLIKLIES TVKTVIKQVM QKAKQELDFL EKQFDVKLME RLKQITSTKN FHVLEYTKAL EILKTAQASG QANFEVQDFN FGLDLKTEHE RFLCEQHFHN QPVFVINYPK DFKAFYMKQN ADGRTVGAVD LLFPQIGEIC GGSEREGNLE KLVERCQAMQ IDTQTLNWYL DMRKWGYFAS AGFGLGFDRL LAYICGLENI RDAIPFPRAH GSINY // ID T1SA_MYCPN Reviewed; 335 AA. AC P75604; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_089; DE AltName: Full=S.MpnORFAP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_089; DE Short=S protein; GN OrderedLocusNames=MPN_089; ORFNames=MP066, R02_orf335; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- INTERACTION: CC P75290:MPN_497; NbExp=1; IntAct=EBI-2259729, EBI-2259752; CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB95713.1; -; Genomic_DNA. DR PIR; S73392; S73392. DR RefSeq; NP_109777.1; NC_000912.1. DR RefSeq; WP_010874446.1; NC_000912.1. DR ProteinModelPortal; P75604; -. DR IntAct; P75604; 3. DR REBASE; 6708; S.MpnORF89P. DR EnsemblBacteria; AAB95713; AAB95713; MPN_089. DR GeneID; 877140; -. DR KEGG; mpn:MPN089; -. DR PATRIC; 20021455; VBIMycPne110_0088. DR KO; K01154; -. DR OMA; ASSNCGI; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-92-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 335 Putative type-1 restriction enzyme FT specificity protein MPN_089. FT /FTId=PRO_0000198044. SQ SEQUENCE 335 AA; 38602 MW; 4657C6877C29354C CRC64; MGRIKTYDFD GEYVTWTTRW SYAGSIYYRN GKFSASSNCG ILKVLNKEIN PKFLAYALKK EAKKFVNTTS AIPILRTQKV VEIPIDFPPL QIQEKIATIL DTFTELSAEL SAELSAELSA ELSAELRERK KQYAFYRDYL LNLKNWKEEN KYYKLGEIAQ KVLVGGEKPA DFSKEKNEVY KYPILSNNSK AEEFLVYSKT FRVEEKSITV SARGTIGAVF YRDFAYLPAV SLICFVPKEE FDIRFLFHAL RAIKFKKQGS ATGQLTVAQF KEYGIHVPSL KKQKEIAAIL DPLYSFFTDL NEGIPAEIEL RKKQLDYYQN FLFNWVQNQK AASIL // ID T1SY_MYCPN Reviewed; 145 AA. AC P75487; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_290; DE AltName: Full=S.MpnORFEAP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_290; DE Short=S protein; GN OrderedLocusNames=MPN_290; ORFNames=H10_orf145L, MP545; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB96193.1; -; Genomic_DNA. DR PIR; S73871; S73871. DR RefSeq; NP_109978.1; NC_000912.1. DR RefSeq; WP_010874647.1; NC_000912.1. DR ProteinModelPortal; P75487; -. DR REBASE; 6702; S.MpnORF289P. DR EnsemblBacteria; AAB96193; AAB96193; MPN_290. DR GeneID; 877414; -. DR KEGG; mpn:MPN290; -. DR PATRIC; 20021915; VBIMycPne110_0314. DR OMA; FLFNWIQ; -. DR OrthoDB; EOG6SJJQT; -. DR BioCyc; MPNE272634:GJ6Z-297-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 145 Putative type-1 restriction enzyme FT specificity protein MPN_290. FT /FTId=PRO_0000198048. SQ SEQUENCE 145 AA; 16827 MW; DABD6EA23F708DE4 CRC64; MVYSKTFRVE EKSITVSARG TIGVVFYRDF AYLPAVSLIC FVPKEEFDIR FLFHALRAIK FKKQGSATGQ LTVAQFKEYG IHVPSLKKQK EIAAILDPLY SFFTDLNEGL PAEIELRKKQ LDYYQNFLFN WIQKQKELVE QASTN // ID SYM_MYCPN Reviewed; 512 AA. AC P75091; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Methionine--tRNA ligase; DE EC=6.1.1.10; DE AltName: Full=Methionyl-tRNA synthetase; DE Short=MetRS; GN Name=metG; Synonyms=metS; OrderedLocusNames=MPN_023; ORFNames=MP131; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Is required not only for elongation of protein synthesis CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 2A 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; U00089; AAB95779.1; -; Genomic_DNA. DR PIR; S73457; S73457. DR RefSeq; NP_109711.1; NC_000912.1. DR RefSeq; WP_010874380.1; NC_000912.1. DR ProteinModelPortal; P75091; -. DR IntAct; P75091; 9. DR EnsemblBacteria; AAB95779; AAB95779; MPN_023. DR GeneID; 876981; -. DR KEGG; mpn:MPN023; -. DR PATRIC; 20021321; VBIMycPne110_0022. DR KO; K01874; -. DR OMA; TYPAFCT; -. DR OrthoDB; EOG6CVV9B; -. DR BioCyc; MPNE272634:GJ6Z-25-MONOMER; -. DR Proteomes; UP000000808; 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-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR023457; Met-tRNA_synth_2. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF09334; tRNA-synt_1g; 2. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00398; metG; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 512 Methionine--tRNA ligase. FT /FTId=PRO_0000139229. FT MOTIF 11 21 "HIGH" region. FT MOTIF 301 305 "KMSKS" region. FT METAL 126 126 Zinc. {ECO:0000250}. FT METAL 129 129 Zinc. {ECO:0000250}. FT METAL 143 143 Zinc. {ECO:0000250}. FT METAL 147 147 Zinc. {ECO:0000250}. FT BINDING 304 304 ATP. {ECO:0000250}. SQ SEQUENCE 512 AA; 59263 MW; B5C3861CEC30A6AA CRC64; MKRCYITTPI YYASGKPHIG HAFTTILADV IKRYKQQNGY EAYFLTGTDE HGNKIESKAK SLGLDPQTFV DQNVAYFQQM WKQLDINFDH FIRTTDLSHK AQVQHAFQLL YDKGLIYQSN WEGAYCVECE QNYFTYDKQT MLCEIGHQLT LVQEPSLFIA FKDSKDWIGE MIATNKLNIT PESRAAELKN NFLDGGLNDL ALTRQNVTWG IPVPFDNKQT IYVWFDALFN YITNLGFAHN DPKFNKWWNN NDEEHEVIHL ISREITRFHC IYWPIFLHQL GFKLPTQFLS HGWIVDGNGH KMSKSLGNVI SPEELLAQFG VDGTRYCLLK EMRLDKDNRC SMAIFKDIYN ADLANSFGNH ASRTFGMIKK YLGGQLDFIE VQDPQVKQLM DQANQAMVQF DTAWNNFQFY KGINGLLQLV FQASKLIDQL KPWELVKQTD YTLLKQLLFA CVRCTQVCFV LLAPILVHTS TQIFDLFNFS AQARSKTHLA DPQQLQKISL APVIQPLFKR LD // ID SYY_MYCPN Reviewed; 399 AA. AC P75122; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. 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=MPN_669; ORFNames=MP173; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95821.1; -; Genomic_DNA. DR PIR; S73499; S73499. DR RefSeq; NP_110358.1; NC_000912.1. DR RefSeq; WP_010875026.1; NC_000912.1. DR ProteinModelPortal; P75122; -. DR IntAct; P75122; 1. DR EnsemblBacteria; AAB95821; AAB95821; MPN_669. DR GeneID; 877033; -. DR KEGG; mpn:MPN669; -. DR PATRIC; 20022823; VBIMycPne110_0734. DR KO; K01866; -. DR OMA; FSVNRMM; -. DR OrthoDB; EOG6B09VR; -. DR BioCyc; MPNE272634:GJ6Z-715-MONOMER; -. DR Proteomes; UP000000808; 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; PF01479; S4; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR SMART; SM00363; S4; 1. 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 1 399 Tyrosine--tRNA ligase. FT /FTId=PRO_0000055658. FT DOMAIN 332 395 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT MOTIF 41 50 "HIGH" region. FT MOTIF 226 230 "KMSKS" region. FT BINDING 36 36 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 166 166 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 170 170 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 229 229 ATP. {ECO:0000255|HAMAP-Rule:MF_02006}. SQ SEQUENCE 399 AA; 44650 MW; 50E6B8A3FE3E9A4E CRC64; MTKDLLALLK ERGLFVQANF EKELKQLLNQ GSFAFYVGFD PTAPSLHIGN YVLLHVAQIF QAMGHIPHVL LGSGTALIGD PTGRMELRQM MSRETIAENT RNIKKQIRRF LGSNVVFCQN ETWLKKLNYI EVIRELGPCF SVNKMLATDA FSARWERGLT LMELNYMVLQ AYDFYYLNQK YGVQLQIGGS DQWANILAGA DLIRRKTQKQ VYGMTTNLLV KANGEKMGKS ASGALWLDPQ KTSPYDFYQY WINLDDASLQ KVFLMLTKLD TKAIETLCNL KGAAIKEAKA KLAFELTDAI HGTKAALVAQ AKSARIFAFQ PDTETKTVRA GTRLVDVIVD LGLVVSRSEA RRVIQQGGLT INQEKVTDVE MVLQASSQPL VIGKGKKRFV TVQVIANTK // ID T1MD_MYCPN Reviewed; 543 AA. AC P75436; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Putative type I restriction enzyme MpnORFDP M protein; DE Short=M.MpnORFDP; DE EC=2.1.1.72; GN OrderedLocusNames=MPN_342; ORFNames=H91_orf543, MP494; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Methylation of specific adenine residues; required for CC both restriction and modification activities. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase 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; U00089; AAB96142.1; -; Genomic_DNA. DR PIR; S73820; S73820. DR RefSeq; NP_110030.1; NC_000912.1. DR RefSeq; WP_010874698.1; NC_000912.1. DR ProteinModelPortal; P75436; -. DR IntAct; P75436; 2. DR REBASE; 6703; M.MpnII. DR EnsemblBacteria; AAB96142; AAB96142; MPN_342. DR GeneID; 876775; -. DR KEGG; mpn:MPN342; -. DR PATRIC; 20022038; VBIMycPne110_0366. DR KO; K03427; -. DR OMA; FDTTSTR; -. DR OrthoDB; EOG64JFNB; -. DR BioCyc; MPNE272634:GJ6Z-359-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 543 Putative type I restriction enzyme FT MpnORFDP M protein. FT /FTId=PRO_0000088028. FT REGION 208 213 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 240 242 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 265 265 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 543 AA; 61975 MW; 618EE22B4FE03064 CRC64; MEKKRTEQRN GVEKKIWEIA DKLRGTIDGW DFKSYVLIGL FYRFLSENLC KYFNDSERRN NPDFSYENLT DDYEAIDALK DAAIASKGFF IKPSQLFQNV VKSIRENKNN EDLNTTLRDI FDDIEKSTEL GDGRSKESFK GLFKDFNVSE VKLGSTLTIR TEKLKELLTS IDTMELDEFE KNSIDAFGDA YEFLISMYAQ NAGKSGGEFF TPQDISELLA RIAIGKKDTV DDVYDMACGS GSLLLQVIKV LGKEKTSLVS YYGQEINHTT YNLCRMNMIL HNIDYANFNI INADTLTTKE WEKHYVNCSN ENGFEVVVSN PPYSISWAGD KKSNLVSDVR FKDAGTLAPN SKADLAFVLH ALYVLGQEGT AAIVCFPGIL YREGKEQTIR KYLVDQNFVD AVIQLPSNLF STTSIATSIL VLKKNRDKKD PIFFIDGSNE FVREKKNNRL SPKNIEKIVD CFNSKKEEAN FAKSVERDKI RESNYDLTVG KYVNSEAEKE ELDIKVLNHS IDEIVDKQKD LRTKIKDIIQ DIKVDFDNID INN // ID SYW_MYCPN Reviewed; 346 AA. AC P75510; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 101. DE RecName: Full=Tryptophan--tRNA ligase; DE EC=6.1.1.2; DE AltName: Full=Tryptophanyl-tRNA synthetase; DE Short=TrpRS; GN Name=trpS; OrderedLocusNames=MPN_265; ORFNames=MP568; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + CC diphosphate + L-tryptophyl-tRNA(Trp). CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96216.1; -; Genomic_DNA. DR PIR; S73894; S73894. DR RefSeq; NP_109953.1; NC_000912.1. DR RefSeq; WP_010874622.1; NC_000912.1. DR PDB; 2YY5; X-ray; 2.55 A; A/B/C/D=1-346. DR PDBsum; 2YY5; -. DR ProteinModelPortal; P75510; -. DR SMR; P75510; 1-346. DR IntAct; P75510; 2. DR EnsemblBacteria; AAB96216; AAB96216; MPN_265. DR GeneID; 877342; -. DR KEGG; mpn:MPN265; -. DR PATRIC; 20021855; VBIMycPne110_0284. DR KO; K01867; -. DR OMA; ATTDSFN; -. DR OrthoDB; EOG686NJQ; -. DR BioCyc; MPNE272634:GJ6Z-272-MONOMER; -. DR EvolutionaryTrace; P75510; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 346 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136648. FT MOTIF 11 19 "HIGH" region. FT MOTIF 200 204 "KMSKS" region. FT BINDING 203 203 ATP. {ECO:0000250}. FT STRAND 4 9 {ECO:0000244|PDB:2YY5}. FT HELIX 17 22 {ECO:0000244|PDB:2YY5}. FT HELIX 24 26 {ECO:0000244|PDB:2YY5}. FT HELIX 27 33 {ECO:0000244|PDB:2YY5}. FT STRAND 34 40 {ECO:0000244|PDB:2YY5}. FT HELIX 42 45 {ECO:0000244|PDB:2YY5}. FT HELIX 52 68 {ECO:0000244|PDB:2YY5}. FT TURN 73 75 {ECO:0000244|PDB:2YY5}. FT STRAND 76 80 {ECO:0000244|PDB:2YY5}. FT HELIX 81 83 {ECO:0000244|PDB:2YY5}. FT HELIX 85 97 {ECO:0000244|PDB:2YY5}. FT HELIX 100 105 {ECO:0000244|PDB:2YY5}. FT HELIX 107 110 {ECO:0000244|PDB:2YY5}. FT HELIX 129 142 {ECO:0000244|PDB:2YY5}. FT STRAND 147 150 {ECO:0000244|PDB:2YY5}. FT HELIX 153 155 {ECO:0000244|PDB:2YY5}. FT HELIX 156 173 {ECO:0000244|PDB:2YY5}. FT STRAND 181 183 {ECO:0000244|PDB:2YY5}. FT TURN 186 190 {ECO:0000244|PDB:2YY5}. FT HELIX 208 210 {ECO:0000244|PDB:2YY5}. FT HELIX 218 226 {ECO:0000244|PDB:2YY5}. FT TURN 240 242 {ECO:0000244|PDB:2YY5}. FT HELIX 244 256 {ECO:0000244|PDB:2YY5}. FT HELIX 260 262 {ECO:0000244|PDB:2YY5}. FT HELIX 263 269 {ECO:0000244|PDB:2YY5}. FT HELIX 273 276 {ECO:0000244|PDB:2YY5}. FT HELIX 277 279 {ECO:0000244|PDB:2YY5}. FT HELIX 282 305 {ECO:0000244|PDB:2YY5}. FT HELIX 309 338 {ECO:0000244|PDB:2YY5}. FT HELIX 342 344 {ECO:0000244|PDB:2YY5}. SQ SEQUENCE 346 AA; 39079 MW; 66CF4FFCCE9C2F95 CRC64; MMKRALTGIQ ASGKQHLGNY LGVMQSLIEL QEQCQLFVFV ADLHSITVDF QPQALKQNNF DLVRTLLAVG LDPQKACLFL QSDLLEHSMM GYLMMVQSNL GELQRMTQFK AKKAEQTRNP NGTLNIPTGL LTYPALMAGD ILLYQPDIVP VGNDQKQHLE LTRDLAQRIQ KKFKLKLRLP QFVQNKDTNR IMDLFDPTKK MSKSSKNQNG VIYLDDPKEV VVKKIRQATT DSFNKIRFAP KTQPGVTNML TILKALLKEP VNQSLTNQLG NDLEAYFSTK SYLDLKNALT EATVNLLVNI QRKREQISRE QVFNCLQAGK NQAQATARTT LALFYDGFGL GSQNIK // ID T1RY_MYCPN Reviewed; 206 AA. AC P75433; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Putative type-1 restriction enzyme MpnORFDP R protein part 2; DE EC=3.1.21.3; DE AltName: Full=MpnORFDBP; DE AltName: Full=Putative type I restriction enzyme MpnORFDP R protein part 2; GN OrderedLocusNames=MPN_345; ORFNames=H91_orf206, MP491; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase CC activities, but not for modification. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give random CC double-stranded fragments with terminal 5'-phosphates; ATP is CC simultaneously hydrolyzed. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96139.1; -; Genomic_DNA. DR PIR; S73817; S73817. DR ProteinModelPortal; P75433; -. DR REBASE; 6705; MpnIIP. DR EnsemblBacteria; AAB96139; AAB96139; MPN_345. DR PATRIC; 20022046; VBIMycPne110_0370. DR OrthoDB; EOG6JTCB4; -. DR BioCyc; MPNE272634:GJ6Z-362-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. 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 Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Hydrolase; KW Nucleotide-binding; Reference proteome; Restriction system. FT CHAIN 1 206 Putative type-1 restriction enzyme FT MpnORFDP R protein part 2. FT /FTId=PRO_0000077264. SQ SEQUENCE 206 AA; 23957 MW; E69EB18CF7185F20 CRC64; MRWSDSENNK IDYIEDFATH FLNKNALLNV ICKFCVFRSN SDLWVMRPYQ ICATERILEK IKEDNRNSKN SKNASKGGCI WHSTGSGKTL TSFKAVQLAS EIDFVDKVLF VVDRKDLDNQ TIEEYEKFQA GSVSETENTN DLKEKILDDS TATRAIVTTI HKLKRLIDQR SKLKDEDLKK KNIVLIFDEC HRSQFGKMKQ EIDEFF // ID T1SB_MYCPN Reviewed; 363 AA. AC P75279; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_507; DE AltName: Full=S.MpnORFBP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_507; DE Short=S protein; GN OrderedLocusNames=MPN_507; ORFNames=MP335, P02_orf363V; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB95983.1; -; Genomic_DNA. DR PIR; S73661; S73661. DR RefSeq; NP_110195.1; NC_000912.1. DR RefSeq; WP_010874863.1; NC_000912.1. DR ProteinModelPortal; P75279; -. DR IntAct; P75279; 1. DR REBASE; 6709; S.MpnORF507P. DR EnsemblBacteria; AAB95983; AAB95983; MPN_507. DR GeneID; 876821; -. DR KEGG; mpn:MPN507; -. DR PATRIC; 20022458; VBIMycPne110_0556. DR KO; K01154; -. DR OMA; YYIFANS; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-548-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 363 Putative type-1 restriction enzyme FT specificity protein MPN_507. FT /FTId=PRO_0000198045. SQ SEQUENCE 363 AA; 42006 MW; 381106066DB1DF1F CRC64; MQIRTYKIKD ICDIQRGRGI TKEYIKNNSG KYPVYSAATT NNGELGFINT YDFAGEYVTW TTNGYAGVVF YRNGKFSASQ DCGVLKVRNK EINAQFLAFA LSLKTPQFVH NLGSRPKLNR KVVAEISLDF PPLEVQEKIA HFLKSFNELS SQLKAELIKR QKQYAFYSDY LLNPKHSQGE EYKLFKLKDI AKKILVGGEK PSDFQKEKDQ VYKYPILSNS RKADDFLGYS KTFRIAEKSI TVSARGTIGA VFYRDFSYLP AVSLICFIPK PEFNINFLFH ALKATKFHKQ GSGTGQLTMA QFKEYQVYIP SLKKQQEIAA TLDPLYYIFA NSNWGIYKEI ELRKKQMQYY QERLFQWIEN QKV // ID T1SD_MYCPN Reviewed; 330 AA. AC P75435; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_343; DE AltName: Full=S.MpnORFDP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_343; DE Short=S protein; GN OrderedLocusNames=MPN_343; ORFNames=H91_orf330, MP493; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB96141.1; -; Genomic_DNA. DR PIR; S73819; S73819. DR ProteinModelPortal; P75435; -. DR IntAct; P75435; 1. DR REBASE; 6704; S.MpnII. DR EnsemblBacteria; AAB96141; AAB96141; MPN_343. DR PATRIC; 20022040; VBIMycPne110_0367. DR OMA; NACPIPN; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-360-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 330 Putative type-1 restriction enzyme FT specificity protein MPN_343. FT /FTId=PRO_0000198047. SQ SEQUENCE 330 AA; 37222 MW; 85B577796FFB31CE CRC64; MEAPKFVNNA CPIPNLNLSR TEEIELDFPP LQIQQKIATI LDTFTELSAE LSAELSAELS AELSAELSAE LSAELSAELS AELSAELSAE LSAELSAELS AELSAELSAE LRERKKQYAF YRDYLLNQEN IRKIYGANIP FETFQVKDIC EIRRGRAITK AYIRNNPGEN PVYSAATTND GELGRIKDCD FDGEYITWTT NGYAGVVFYR NGKFNASQDC GVLKVKNKKI CTKFLSFLLK IEAPKFVHNL ASRPKLSQKV MAEIELSFPP LEIQEKIADI LFAFEKLCND LVEGIPAEIE LRKKQLDYYQ NFLFNWVQEQ KKNSLSTNLN // ID T1SH_MYCPN Reviewed; 249 AA. AC P75180; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 22-JUL-2015, entry version 79. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_615; DE AltName: Full=S.MpnORFHP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_615; DE Short=S protein; GN OrderedLocusNames=MPN_615; ORFNames=C12_orf249, MP227; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB95875.1; -; Genomic_DNA. DR PIR; S73553; S73553. DR ProteinModelPortal; P75180; -. DR IntAct; P75180; 2. DR REBASE; 6707; S.MpnORF615P. DR EnsemblBacteria; AAB95875; AAB95875; MPN_615. DR PATRIC; 20022713; VBIMycPne110_0679. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-661-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 249 Putative type-1 restriction enzyme FT specificity protein MPN_615. FT /FTId=PRO_0000198052. SQ SEQUENCE 249 AA; 28758 MW; 14AC1D1350DB5855 CRC64; MQGILAEIEL DFPPLQIQEK IATILDTFTE LSAELRERKK QYAFYRDYLL NQENIRKIYG ANIPFETFQV KDICEIRRGR AITKAYIRNN PGENPVYSAA TTNDGELGRI KDCDFDGEYI TWTTNGYAGV VFYRNGKFNA SQDCGVLKVK NKKICTKFLS FLLKIEAPKF VHNLASRPKL SQKVMAEIEL SFPPLEIQEK IADILFAFEK LCNDLVEGIP AEIEMRKKQL DYYYHLIFSK IAHFSKQLA // ID T1SZ_MYCPN Reviewed; 187 AA. AC P75488; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_289; DE AltName: Full=S.MpnORFEBP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_289; DE Short=S protein; GN OrderedLocusNames=MPN_289; ORFNames=H10_orf187V, MP546; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB96194.1; -; Genomic_DNA. DR PIR; S73872; S73872. DR RefSeq; NP_109977.1; NC_000912.1. DR RefSeq; WP_010874646.1; NC_000912.1. DR ProteinModelPortal; P75488; -. DR IntAct; P75488; 1. DR REBASE; 6702; S.MpnORF289P. DR EnsemblBacteria; AAB96194; AAB96194; MPN_289. DR GeneID; 877345; -. DR KEGG; mpn:MPN289; -. DR PATRIC; 20021913; VBIMycPne110_0313. DR OMA; RVISKLY; -. DR OrthoDB; EOG6V7BS3; -. DR BioCyc; MPNE272634:GJ6Z-296-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 187 Putative type-1 restriction enzyme FT specificity protein MPN_289. FT /FTId=PRO_0000198049. SQ SEQUENCE 187 AA; 21289 MW; 610CCDE0592453B6 CRC64; MQIKTYKIKD ICDIKRGRVI SKLYIKNNPG EFPVYSSATV NNGEIGRIKD CDLKGEYVTW TTDGAQAGSV FYRNGQFNAT NVCGILKVNN DEIYPKFLAY ALRLKAPKFV NYACPIPKLM QGTLAEIELD FTSKKIQEKI ATILDTFTEL SAELSAELSA ELSAELRERK KQYVFYSDYL LNPKNWK // ID T1RX_MYCPN Reviewed; 376 AA. AC P75431; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Putative type I restriction enzyme MpnORFDP R protein part 1; DE EC=3.1.21.3; DE AltName: Full=MpnORFDAP; GN OrderedLocusNames=MPN_347; ORFNames=H91_orf376, MP489; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase CC activities, but not for modification. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give random CC double-stranded fragments with terminal 5'-phosphates; ATP is CC simultaneously hydrolyzed. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96137.1; -; Genomic_DNA. DR PIR; S73815; S73815. DR ProteinModelPortal; P75431; -. DR IntAct; P75431; 1. DR REBASE; 6705; MpnIIP. DR EnsemblBacteria; AAB96137; AAB96137; MPN_347. DR PATRIC; 20022050; VBIMycPne110_0372. DR OMA; FRDIREN; -. DR OrthoDB; EOG6JTCB4; -. DR BioCyc; MPNE272634:GJ6Z-364-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR022625; TypeI_RM_Rsu_C. DR Pfam; PF12008; EcoR124_C; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Hydrolase; KW Nucleotide-binding; Reference proteome; Restriction system. FT CHAIN 1 376 Putative type I restriction enzyme FT MpnORFDP R protein part 1. FT /FTId=PRO_0000077263. SQ SEQUENCE 376 AA; 45087 MW; 691BB674F64988D9 CRC64; MFLTGFDAPT LNTLWVDKNL SEHTLIQAFS RTNRCFGETK KFGNIFSFRD IRENFDQALK MYADKRGLKD IKSNMVMREF EEVFEKFKDW TEKIKQKYPN PDEILNLEKE EKWDFSDLFG EFLGDYRTVK SYHEFDKDNP YLPSDEFNKY FAAFSQIQEE IRKEKAEKKA LEVQEEDLSN EVRKEPQIFS WEYGEGIQAN LDYIFHLIKD LYNCDNEQDR QKVLDKIKTA IRTNPEIQVN EDILNEFIED LGKSFEKEKL EEVWKTEGKL RECLKDFCKK KEESNKKKII NDFLVKGVFL VEWVADKQLN TAKKKGEYSP SWSDTEKLIW KEKSTNLPTM TEKDEDGNFK WRKLITDISE AFKNHFERFI RFVEIR // ID T1SG_MYCPN Reviewed; 306 AA. AC P75492; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MPN_285; DE AltName: Full=S.MpnORFGP; DE AltName: Full=Type I restriction enzyme specificity protein MPN_285; DE Short=S protein; GN OrderedLocusNames=MPN_285; ORFNames=A65_orf306, MP550; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; U00089; AAB96198.1; -; Genomic_DNA. DR PIR; S73876; S73876. DR ProteinModelPortal; P75492; -. DR REBASE; 6701; S.MpnORF285P. DR EnsemblBacteria; AAB96198; AAB96198; MPN_285. DR PATRIC; 20021901; VBIMycPne110_0307. DR OMA; DICEINR; -. DR OrthoDB; EOG6PKF94; -. DR BioCyc; MPNE272634:GJ6Z-292-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 306 Putative type-1 restriction enzyme FT specificity protein MPN_285. FT /FTId=PRO_0000198051. SQ SEQUENCE 306 AA; 34693 MW; DC16E8CD9A79A9F7 CRC64; MAEIPIDFPP LKIQEKIATI LDTFTELSAE LSAELSAELS AELSAELSAE LSAELSAELS AELSAELSAE LSAELSAELS AELSAELRER RKQYAFYRDY LLNQENIRKI YGANIPFETF QIRDICEINR GREINEKYLR ENPGEFPVYS SATTNGGLIG KINDYDFHGE YVTWTTGGAH AGNVFYRNEK FSCSQNCGLL EVKNKNKFSS KFLCFALKLQ SKKFVNYASA IPVLTIKRIA EIELSFPPLE IQEKIADILF AFEKLCNDLT EGIPAEIELR KKQLDYYQNF LFNWVQNKKL ESLKSL // ID THIO_MYCPN Reviewed; 102 AA. AC P75512; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Thioredoxin; DE Short=Trx; GN Name=trxA; Synonyms=trx; OrderedLocusNames=MPN_263; ORFNames=MP570; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9202470; RA Ben-Menachem G., Himmelreich R., Herrmann R., Aharonowitz Y., RA Rottem S.; RT "The thioredoxin reductase system of mycoplasmas."; RL Microbiology 143:1933-1940(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Participates in various redox reactions through the CC reversible oxidation of its active center dithiol to a disulfide CC and catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U51987; AAC45450.1; -; Genomic_DNA. DR EMBL; U00089; AAB96218.1; -; Genomic_DNA. DR PIR; S73896; S73896. DR RefSeq; NP_109951.1; NC_000912.1. DR RefSeq; WP_010874620.1; NC_000912.1. DR ProteinModelPortal; P75512; -. DR IntAct; P75512; 1. DR EnsemblBacteria; AAB96218; AAB96218; MPN_263. DR GeneID; 876921; -. DR KEGG; mpn:MPN263; -. DR PATRIC; 20021851; VBIMycPne110_0282. DR KO; K03671; -. DR OMA; SEDRNDI; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; MPNE272634:GJ6Z-270-MONOMER; -. DR Proteomes; UP000000808; 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; Disulfide bond; Electron transport; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1 102 Thioredoxin. FT /FTId=PRO_0000120114. FT DOMAIN 2 102 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 30 33 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 102 AA; 11215 MW; 0D17B97E976FC144 CRC64; MVTEIKSLKQ LGELFASNNK VIIDFWAEWC GPCKITGPEF AKAASEVSTV AFAKVNVDEQ TDIAAAYKIT SLPTIVLFEK GQEKHRAIGF MPKAKIVQLV SQ // ID THII_MYCPN Reviewed; 387 AA. AC P75228; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Probable tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021}; GN Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021}; GN OrderedLocusNames=MPN_550; ORFNames=MP292; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA CC to produce 4-thiouridine in position 8 of tRNAs, which functions CC as a near-UV photosensor. Also catalyzes the transfer of sulfur to CC the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. CC This is a step in the synthesis of thiazole, in the thiamine CC biosynthesis pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260824, EBI-2260824; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95940.1; -; Genomic_DNA. DR PIR; S73618; S73618. DR RefSeq; NP_110239.1; NC_000912.1. DR RefSeq; WP_010874907.1; NC_000912.1. DR ProteinModelPortal; P75228; -. DR EnsemblBacteria; AAB95940; AAB95940; MPN_550. DR GeneID; 877210; -. DR KEGG; mpn:MPN550; -. DR PATRIC; 20022577; VBIMycPne110_0612. DR KO; K03151; -. DR OMA; PDEDCCT; -. DR OrthoDB; EOG6TBHGR; -. DR BioCyc; MPNE272634:GJ6Z-595-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA 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 GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00021; ThiI; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR020536; ThiI_AANH. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR003720; tRNA_STrfase. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR TIGRFAMs; TIGR00342; TIGR00342; 1. DR PROSITE; PS51165; THUMP; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase; KW tRNA-binding. FT CHAIN 1 387 Probable tRNA sulfurtransferase. FT /FTId=PRO_0000154851. FT DOMAIN 67 167 THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 185 186 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 210 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 269 269 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 287 287 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 296 296 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. SQ SEQUENCE 387 AA; 43341 MW; E418669E7A8F64DF CRC64; MGLHNEPNTI LICRYGELVL KGKNRLQFVK QLKKNVKQAF KKLSITNPVD YQFDMLVVGE VISTQRSLLK NLFTRLPGLS VCLFALQIPH DEAQLLALLQ QVVQSHPSFK IEVRRRDKLF ACNSSAFKKY LALQLWEKYQ LKGKLVDPAI TVHVEVTKEH FLIISESFNG IGGLPVFTSG TALALLSGGI DSPVAASLVL QRGFNVDFIT FINEPGHNAA TIGKIQRLAN LVSLNQTLCT GRLFVFDFTD LQKELSHISL EGYRIVLMRR CFYKIASLFK YDCLITGEAL GQVASQTIDN LKVIQAVVPN TFVIRPLIGL SKDKIIEWAK ALGTFETSIE HHMDTCTVFA PKKPTTKAKL AIVEKLESEL LFVRELIEAG VKKLQND // ID TIG_MYCPN Reviewed; 444 AA. AC P75454; Q50352; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=MPN_331; ORFNames=MP505; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-176. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by CC maintaining the newly synthesized protein in an open conformation. CC Functions as a peptidyl-prolyl cis-trans isomerase (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to CC the ribosome near the polypeptide exit tunnel while the other half CC is free in the cytoplasm. {ECO:0000250}. CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, CC the middle domain has PPIase activity, while the C-terminus has CC intrinsic chaperone activity on its own. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96153.1; -; Genomic_DNA. DR EMBL; Z32656; CAA83577.1; -; Genomic_DNA. DR PIR; S73831; S73831. DR RefSeq; NP_110019.1; NC_000912.1. DR RefSeq; WP_010874687.1; NC_000912.1. DR ProteinModelPortal; P75454; -. DR SMR; P75454; 167-250. DR IntAct; P75454; 4. DR EnsemblBacteria; AAB96153; AAB96153; MPN_331. DR GeneID; 876961; -. DR KEGG; mpn:MPN331; -. DR PATRIC; 20022016; VBIMycPne110_0355. DR KO; K03545; -. DR OMA; LVHEELM; -. DR OrthoDB; EOG63VBX3; -. DR BioCyc; MPNE272634:GJ6Z-348-MONOMER; -. DR Proteomes; UP000000808; 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; 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 1 444 Trigger factor. FT /FTId=PRO_0000179388. FT DOMAIN 170 255 PPIase FKBP-type. SQ SEQUENCE 444 AA; 51353 MW; 89475FDA4531FA82 CRC64; MKQYKLVNTT QKEKTLCLEI AIDTKLWKET QQKQTQDLTK NMKIKGFRKG KVPPTLAKDY LDRAELLQRS AQAVIDAIFQ PLQQEAVIAD NENVIEDFPT IDFKTINEND CVILFDFDLV PQFEPPDYKH IKDLSPIVPL KDEEFNKELH NIEKNKGKLV DVSDKALANN DIAVIDFVGK VDGKVLESAT AKQYELTIGS NSFIDGFESG LIGMKVGDKR QLKLKFPKDY HAEELKGKPV EFDIELKAIK QLEITPMDET NFKEYLPAQY QGFNSLKEFK TYFHKLVSAK KLEITLQENS VKIRQFFLAN TTLPYIPDSL IKLESDRLLR AQKDQAEQYK IPFERLLAAS KLSLEQLQQR NIKEARDNVT FALVMKRIAD VEKIKVDNKK IHSEIESIID VEYPFVNAEL KKQMFHNMEQ QKDFVESIIL NRLTTTKIIE YSTH // ID TILS_MYCPN Reviewed; 289 AA. AC P75549; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. 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=MPN_222; ORFNames=MP609; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96257.1; -; Genomic_DNA. DR PIR; S73935; S73935. DR RefSeq; NP_109910.1; NC_000912.1. DR RefSeq; WP_010874579.1; NC_000912.1. DR ProteinModelPortal; P75549; -. DR IntAct; P75549; 2. DR EnsemblBacteria; AAB96257; AAB96257; MPN_222. DR GeneID; 877151; -. DR KEGG; mpn:MPN222; -. DR PATRIC; 20021769; VBIMycPne110_0241. DR KO; K04075; -. DR OMA; ETNENTH; -. DR OrthoDB; EOG6NKR0V; -. DR BioCyc; MPNE272634:GJ6Z-229-MONOMER; -. DR Proteomes; UP000000808; 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; 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 PANTHER; PTHR11807:SF2; PTHR11807:SF2; 1. DR Pfam; PF01171; ATP_bind_3; 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 1 289 tRNA(Ile)-lysidine synthase. FT /FTId=PRO_0000181731. FT NP_BIND 11 16 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 289 AA; 34385 MW; 6A234642B8F6A0C2 CRC64; MPKTQYIAGV SGGPDSMLLL KLYHKKIACV VHVNYNKRTT ALRDQKMVEE YCKQLKVPLI VHTVPEDTVW KKNFQAQARK IRFEQFQKAA SLYKVDKLLL AHHRDDFIEQ AKMQLDARKR AMYYGIKTRG ELYGMKVYRP FIKYWKNEIL ALCEEHKVPY GIDETNAQPI YKRNQVRQEI ANWSKEEKEE FYIGVCAMNR VIGQKLFSLM KRAKQWLAHP DVRELKRYPL PDQRQLVYSF LITHHIDVTG DKIDAILDFI QPFQQKHYRL KDEIFLSIKD ERLTLLYKS // ID TKT_MYCPN Reviewed; 648 AA. AC P75611; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Transketolase; DE Short=TK; DE EC=2.2.1.1; GN Name=tkt; Synonyms=tktA; OrderedLocusNames=MPN_082; ORFNames=MP073; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from CC a ketose donor to an aldose acceptor, via a covalent intermediate CC with the cofactor thiamine pyrophosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; 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:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transketolase 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; U00089; AAB95721.1; -; Genomic_DNA. DR PIR; S73399; S73399. DR RefSeq; NP_109770.1; NC_000912.1. DR RefSeq; WP_010874439.1; NC_000912.1. DR ProteinModelPortal; P75611; -. DR EnsemblBacteria; AAB95721; AAB95721; MPN_082. DR GeneID; 877050; -. DR KEGG; mpn:MPN082; -. DR PATRIC; 20021447; VBIMycPne110_0084. DR KO; K00615; -. DR OMA; ESKDAKF; -. DR OrthoDB; EOG6N3CRG; -. DR BioCyc; MetaCyc:MONOMER-583; -. DR BioCyc; MPNE272634:GJ6Z-85-MONOMER; -. DR Proteomes; UP000000808; 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; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF02779; Transket_pyr; 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; PS00802; TRANSKETOLASE_2; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; Thiamine pyrophosphate; Transferase. FT CHAIN 1 648 Transketolase. FT /FTId=PRO_0000191862. FT NP_BIND 109 111 Thiamine pyrophosphate. {ECO:0000250}. FT ACT_SITE 397 397 Proton donor. {ECO:0000250}. FT METAL 150 150 Magnesium. {ECO:0000250}. FT METAL 180 180 Magnesium. {ECO:0000250}. FT METAL 182 182 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 22 22 Substrate. {ECO:0000250}. FT BINDING 62 62 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 151 151 Thiamine pyrophosphate; via amide FT nitrogen. {ECO:0000250}. FT BINDING 180 180 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 252 252 Substrate. {ECO:0000250}. FT BINDING 252 252 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 345 345 Substrate. {ECO:0000250}. FT BINDING 372 372 Substrate. {ECO:0000250}. FT BINDING 423 423 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 447 447 Substrate. {ECO:0000250}. FT BINDING 455 455 Substrate. {ECO:0000250}. FT BINDING 506 506 Substrate. {ECO:0000250}. FT SITE 22 22 Important for catalytic activity. FT {ECO:0000250}. FT SITE 252 252 Important for catalytic activity. FT {ECO:0000250}. SQ SEQUENCE 648 AA; 72378 MW; EFE8247D7F0837C9 CRC64; MKNLFACQHL ALSAIQHAKG GHVGMALGAS PILYTLWTKH IQFNPNCPKW INRDRLVMSA GHGSMALYPI LHFAGLITKQ EMLHHKYGQV NTSSHPEYAP NNFIDASTGP LGQGLGMAVG MALTQRVLAA EFKALSPKLF DHFTYVVVGD GDLQEGVSYE VAHLAGVYQL NKLIVLHDSN RVQMDSVVRD VSLENLQTRF TNMGWNYLET SDAVADIDAA IKQAKKSDKP TFIEVHTTIA KNTTLEDQPA GHWFIPTDKD FARFNSNTKT NFTPFEYPQT VYDFFHKQVI ARQAKPVQAY KELLEKLKDK PLYTKFINWT ENDYQALYLN QLDERKVAQA NAATRNYLKD FLGQINNSNS NLYCLNADVA RSCNIKLGDD NLHTNPHSRN IQVGIREFGM STIMNGMALH GGVKVMGGTF LAFADYSKPA IRLGALMNLP TFYVYTHDSY QVGGDGPTHQ PYDQLPMLRA IENVQVWRPC DEKETAAGVN YGLLSQDQTN VLILTRQALP SLEQSDSVQT LKGGYIISNR KQPDVIVAAS GSEVQLALQL EQALNEQQLK TRVVSVPNIN MLLSQPQSYL QQLFDPNSVL LTLEASASME WYALAKYVKK HTHLGAFSFG ESNDGQVVYE HKGFNVTNLL KLIKTLKS // ID TOP1_MYCPN Reviewed; 711 AA. AC P78032; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; GN OrderedLocusNames=MPN_261; ORFNames=MP572; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000255|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|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; U00089; AAB96220.1; -; Genomic_DNA. DR PIR; S73898; S73898. DR RefSeq; NP_109949.1; NC_000912.1. DR RefSeq; WP_010874618.1; NC_000912.1. DR ProteinModelPortal; P78032; -. DR IntAct; P78032; 4. DR EnsemblBacteria; AAB96220; AAB96220; MPN_261. DR GeneID; 877375; -. DR KEGG; mpn:MPN261; -. DR PATRIC; 20021847; VBIMycPne110_0280. DR KO; K03168; -. DR OMA; CSKFPKC; -. DR OrthoDB; EOG6S7XQ9; -. DR BioCyc; MPNE272634:GJ6Z-268-MONOMER; -. DR Proteomes; UP000000808; 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; 3. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Reference proteome; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 711 DNA topoisomerase 1. FT /FTId=PRO_0000145156. FT DOMAIN 3 134 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ZN_FING 624 652 C4-type 1. FT ZN_FING 673 702 C4-type 2. FT REGION 183 188 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 340 340 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 9 9 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 102 102 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 102 102 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 104 104 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 33 33 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 160 160 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 164 164 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 342 342 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 535 535 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 711 AA; 81965 MW; 16B863588B06582E CRC64; MSKNLVVIES PNKVKTLQKY LPNDFEIVST IGHIREMVHK NFGFNEADYS PVWEDWTKSK KKFSSLSFKG NLKGKKLLSK YDIIKSIKEK ASKATNIYLA TDPDREGEAI SWHVYDVLDE KDKSKCQRIT FNEITKNAVL DALKNPREID QSWVQSQFAR QILDRMIGFR LSRLLNNYLS AKSAGRVQSV ALRFLEEREQ EIRSFVPRFW WTLDVLLNPK AEGVREACAN RSIPIVLREI NPALRAGLKF EEEKSVSGID FLDEASAKKF GEQLKGVFEV YNIDETKHYS SSPNSAYTTA SLQKDAINKL GWSSKKVTLI AQHLYEGVSI NGEQTALISY PRTDSTRLSA QFQQSCKEYI LNHYGEKYLS NRIVSAKGKK GEKIIQDAHE AIHPTDINIT PEMVKNAIKK DEFLLYRLIW IRTVASLMAD CKKSHTHIRF INDGNKFYAS SKSLVFDGYR KIYEHFENKE SNDLYIDLDK IRVGDRFMAK DIKITARQTH PAARYTQASL IEALEKSNIG RPSTYNTMAS VNLDRGYASL NKHAFHVTQL GEQVNEELSK HFGKIINKEF TKNMEKSLDE IAENKKNYQE FLRDFWSNFK EEVKLAEGSI QRVKKEKEFV GRDCPSCASP LLYRYTKRGN EKFVGCSNFP NCKYNEFSQN KPNLTLEKLE ELCPECNSQL VKRRTKFNPN KTFVGCSNFP RCRYIKKDNA S // ID TPIS_MYCPN Reviewed; 244 AA. AC P78010; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; Synonyms=tim, tpi; GN OrderedLocusNames=MPN_629; ORFNames=MP213; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95861.1; -; Genomic_DNA. DR PIR; S73539; S73539. DR RefSeq; NP_110318.1; NC_000912.1. DR RefSeq; WP_010874986.1; NC_000912.1. DR ProteinModelPortal; P78010; -. DR IntAct; P78010; 2. DR EnsemblBacteria; AAB95861; AAB95861; MPN_629. DR GeneID; 877328; -. DR KEGG; mpn:MPN629; -. DR PATRIC; 20022741; VBIMycPne110_0693. DR KO; K01803; -. DR OMA; YHHESDE; -. DR OrthoDB; EOG66QM23; -. DR BioCyc; MetaCyc:MONOMER-547; -. DR BioCyc; MPNE272634:GJ6Z-675-MONOMER; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000000808; 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; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Pentose shunt; Reference proteome. FT CHAIN 1 244 Triosephosphate isomerase. FT /FTId=PRO_0000090254. FT REGION 9 11 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 93 93 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 160 160 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 166 166 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT BINDING 206 206 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00147}. SQ SEQUENCE 244 AA; 26958 MW; F127792746177533 CRC64; MRTKYLIGNW KTNKDLHQAL AFVEQFKQHP AKTKAVLGIA PVHVHLTEVN KVLPNNLLLL AQDANFIASG SYTGTVSYTQ LQDIKVNSVI IGHSERRKYF NETAQVINQK LKACLQAGML VVLCIGETEG QPISFLKEDL TQVLQGIDLS LLKQLVIAYE PIWAIGTGKT ATPEIANNTI AQIRVYLSEL YNKEIAQQTS ILYGGSVAKD NIKELAQTEQ IDGFLVGKAS LDVNDFLVMA QVYA // ID TRMB_MYCPN Reviewed; 210 AA. AC P75256; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. 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=MPN_522; ORFNames=G12_orf210V, MP320; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95968.1; -; Genomic_DNA. DR PIR; S73646; S73646. DR RefSeq; NP_110210.1; NC_000912.1. DR RefSeq; WP_010874878.1; NC_000912.1. DR ProteinModelPortal; P75256; -. DR EnsemblBacteria; AAB95968; AAB95968; MPN_522. DR GeneID; 876965; -. DR KEGG; mpn:MPN522; -. DR PATRIC; 20022504; VBIMycPne110_0579. DR KO; K03439; -. DR OMA; AHPEINY; -. DR OrthoDB; EOG6K6VBC; -. DR BioCyc; MPNE272634:GJ6Z-563-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000808; 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 1 210 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171359. FT REGION 188 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT ACT_SITE 112 112 {ECO:0000250}. FT BINDING 36 36 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 61 61 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 90 90 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 112 112 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 116 116 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 148 148 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. SQ SEQUENCE 210 AA; 24542 MW; 2A41D406B3C8B83C CRC64; MRLRKVKDAL VRVQDSPYFS NPEQLSTIES ESLFVEIGCG KSWFLSQQAQ QNPKCFFVGI EREPTIVLKA INKVNRLEVK PRNLLITCLD ANQLTEYLKP QSISKIFINF PDPWPKKRHT LRRLTAPHFL KQFHQLLKKQ GLIEFKTDND QLFEFTLEVL QKTVAHFKII EQTTDLHNSP LTSTNIMTEY EQRFVSLGVK IKKLTLEKLN // ID TRMD_MYCPN Reviewed; 231 AA. AC P75132; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 13-APR-2016, entry version 97. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase; DE EC=2.1.1.228; DE AltName: Full=M1G-methyltransferase; DE AltName: Full=tRNA [GM37] methyltransferase; GN Name=trmD; OrderedLocusNames=MPN_659; ORFNames=MP183; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA CC = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95831.1; 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; U00089; AAB95831.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_110348.1; NC_000912.1. DR RefSeq; WP_010875016.1; NC_000912.1. DR ProteinModelPortal; P75132; -. DR EnsemblBacteria; AAB95831; AAB95831; MPN_659. DR GeneID; 877016; -. DR KEGG; mpn:MPN659; -. DR PATRIC; 20022803; VBIMycPne110_0724. DR KO; K00554; -. DR OMA; NRYDLYL; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; MPNE272634:GJ6Z-705-MONOMER; -. DR Proteomes; UP000000808; 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 1 231 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060417. FT REGION 129 134 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 110 110 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 231 AA; 26340 MW; 3DE57E826D842C5A CRC64; MKITVLTLFE QVVWPYLNAS IMAQAQKAKL VEFEVINWRQ YCKDKHQTVD DMAYGGGGGM VLKAEPILKA LKACRTPQSK VVLLSPEGQQ FSQPMAQALT QTEHLILICG HYEGFDYRLY KHVDQIISLG DFVLSGGELV ALSVIDATVR LIKGVINDQS LIHESFNNYL LDFPAYTRPY DLDGDKVPEI LLSGDHKKIE AYRKEQQLLR TAQYRPDLYK QYLAKKDEKN K // ID TRML_MYCPN Reviewed; 166 AA. AC P75257; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885}; DE EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885}; DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885}; GN OrderedLocusNames=MPN_521; ORFNames=G12_orf166b, MP321; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble CC position in tRNA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01885}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|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; U00089; AAB95969.1; -; Genomic_DNA. DR PIR; S73647; S73647. DR RefSeq; NP_110209.1; NC_000912.1. DR RefSeq; WP_010874877.1; NC_000912.1. DR ProteinModelPortal; P75257; -. DR IntAct; P75257; 1. DR EnsemblBacteria; AAB95969; AAB95969; MPN_521. DR GeneID; 876885; -. DR KEGG; mpn:MPN521; -. DR PATRIC; 20022502; VBIMycPne110_0578. DR KO; K03216; -. DR OMA; AGLDYWH; -. DR OrthoDB; EOG6RG038; -. DR BioCyc; MPNE272634:GJ6Z-562-MONOMER; -. DR Proteomes; UP000000808; 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; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 166 Putative tRNA (cytidine(34)-2'-O)- FT methyltransferase. FT /FTId=PRO_0000159836. FT BINDING 83 83 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01885}. FT BINDING 109 109 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01885}. FT BINDING 130 130 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01885}. FT BINDING 138 138 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01885}. SQ SEQUENCE 166 AA; 19356 MW; 266F25FE37612F8E CRC64; MYKSAINIVL FCPEIPNNTG NIVRSCTAFK ANLHLIKPYG FFLNDKRMVR AGLNCWDKVQ MFEHKSWEHF IETTPPNKAI WLLTKSGTTT PDQINMQTDN REQLYFVFGQ ETKGLPQTLM EQYSQNQVRI PIWNPVRSIN LSNTVACVLY EYAKQNHYFN LDKQCA // ID TRXB_MYCPN Reviewed; 315 AA. AC P75531; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 109. DE RecName: Full=Thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9; GN Name=trxB; OrderedLocusNames=MPN_240; ORFNames=MP591; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9202470; RA Ben-Menachem G., Himmelreich R., Herrmann R., Aharonowitz Y., RA Rottem S.; RT "The thioredoxin reductase system of mycoplasmas."; RL Microbiology 143:1933-1940(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P0A9P4}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase 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; U51988; AAC45451.1; -; Genomic_DNA. DR EMBL; U00089; AAB96239.1; -; Genomic_DNA. DR PIR; S73917; S73917. DR RefSeq; NP_109928.1; NC_000912.1. DR RefSeq; WP_010874597.1; NC_000912.1. DR ProteinModelPortal; P75531; -. DR EnsemblBacteria; AAB96239; AAB96239; MPN_240. DR GeneID; 877259; -. DR KEGG; mpn:MPN240; -. DR PATRIC; 20021805; VBIMycPne110_0259. DR KO; K00384; -. DR OMA; RITLITN; -. DR OrthoDB; EOG65XN2W; -. DR BioCyc; MetaCyc:MONOMER-543; -. DR BioCyc; MPNE272634:GJ6Z-247-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; KW Oxidoreductase; Redox-active center; Reference proteome. FT CHAIN 1 315 Thioredoxin reductase. FT /FTId=PRO_0000166738. FT NP_BIND 45 52 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT NP_BIND 288 297 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT DISULFID 145 148 Redox-active. FT {ECO:0000250|UniProtKB:P0A9P4}. SQ SEQUENCE 315 AA; 34532 MW; 7155E4AF8D2A2EE7 CRC64; MLKVKSDFLT KDQVIYDVAI VGAGPAGIAA GIYGKRANLN LAIIEGSTPG GKVVKTNIVE NYPGYKSITG PDLGLEMYNH LIDLEPTFFY ANLIKLDKAA DTFILYLDDK TVVFAKTVIY ATGMLERKLG VAKEDHFYGK GISYCAICDG SLYKDQVVGV VGGGNSAIQE ALYLASMAKT VHLIHRREGF RADETALNKL RNLPNVVFHL NYTVKELLGN NTLNGIVLQN TLDHSTKQID LNCVFPYIGF ESITKPVEHL NLKLDPQGFL ITNEQMETSL KGLFAAGDCR SKHFRQIGTA INDGIIAVLT IRDVL // ID TYPH_MYCPN Reviewed; 421 AA. AC P75052; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Thymidine phosphorylase; DE EC=2.4.2.4; DE AltName: Full=TdRPase; GN Name=deoA; OrderedLocusNames=MPN_064; ORFNames=MP090; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis CC of pyrimidine nucleosides are involved in the degradation of these CC compounds and in their utilization as carbon and energy sources, CC or in the rescue of pyrimidine bases for nucleotide synthesis. CC -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy- CC alpha-D-ribose 1-phosphate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- INTERACTION: CC P75081:upp; NbExp=1; IntAct=EBI-2258997, EBI-2258987; CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase 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; U00089; AAB95738.1; -; Genomic_DNA. DR PIR; S73416; S73416. DR RefSeq; NP_109752.1; NC_000912.1. DR RefSeq; WP_010874421.1; NC_000912.1. DR ProteinModelPortal; P75052; -. DR IntAct; P75052; 1. DR EnsemblBacteria; AAB95738; AAB95738; MPN_064. DR GeneID; 876960; -. DR KEGG; mpn:MPN064; -. DR PATRIC; 20021407; VBIMycPne110_0065. DR KO; K00758; -. DR OMA; TETEINW; -. DR OrthoDB; EOG61ZTGG; -. DR BioCyc; MPNE272634:GJ6Z-66-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004645; F:phosphorylase activity; IEA:InterPro. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.1030.10; -; 1. DR Gene3D; 3.90.1170.30; -; 1. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR013102; PYNP_C. DR InterPro; IPR018090; Pyrmidine_PPas_bac/euk. DR InterPro; IPR017872; Pyrmidine_PPase_CS. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR PANTHER; PTHR10515; PTHR10515; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF07831; PYNP_C; 1. DR PIRSF; PIRSF000478; TP_PyNP; 1. DR SMART; SM00941; PYNP_C; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR SUPFAM; SSF54680; SSF54680; 1. DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1. DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 421 Thymidine phosphorylase. FT /FTId=PRO_0000059081. SQ SEQUENCE 421 AA; 46628 MW; E29DBF93C6D8549F CRC64; MNIVNLISKK QRGKALTETE INWFVHSVNN KSLADYQVSA FLMAVWFQGM NSKELFCLTK AMVKSGESLH FNHHSKLSVD KHSTGGIGDK VSIALIPILT ALDYSVAKLS GRGLGYTGGT IDKLEAVGVK TDFTPTEAQN LLDQNDCFII GQSEGIAPVD KVLYALRDTT ATVDSLPLIA SSVMSKKLAI NNDYIFIDLK YGKGAFCKTK TMAKELAQYM YSIAKQFKRK LYIKLSDMNQ VLGKTIGNAL EVLEVVHFLK RNWTEVGADF IQLMEQIVTE ILIETKRAPN KRAAVALYHA TLEGEKPWQR FLKFIELQGS SWERFLDLKE LFNPQYKAPV LASQSGTLSY TSPVDLAMVS ISLGAGRMVK TDLIDPMAGI KLVKQANEVV KAGDTVLELY SSKPITPAHI EAAQHTIIIK Q // ID TRUA_MYCPN Reviewed; 243 AA. AC Q50291; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 89. 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}; Synonyms=hisT; GN OrderedLocusNames=MPN_196; ORFNames=MP635; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U34795; AAC43685.1; -; Genomic_DNA. DR EMBL; U00089; AAB96283.1; -; Genomic_DNA. DR PIR; S62812; S62812. DR RefSeq; NP_109884.1; NC_000912.1. DR RefSeq; WP_010874553.1; NC_000912.1. DR ProteinModelPortal; Q50291; -. DR EnsemblBacteria; AAB96283; AAB96283; MPN_196. DR GeneID; 876925; -. DR KEGG; mpn:MPN196; -. DR PATRIC; 20021715; VBIMycPne110_0214. DR KO; K06173; -. DR OMA; NYCYEYL; -. DR OrthoDB; EOG6Z9B4R; -. DR BioCyc; MPNE272634:GJ6Z-203-MONOMER; -. DR Proteomes; UP000000808; 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; 1. 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 1 243 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057413. FT ACT_SITE 52 52 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00171}. FT BINDING 110 110 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00171}. SQ SEQUENCE 243 AA; 27717 MW; A5DE0B36E226FF12 CRC64; MPRYLAIVAY NGAPFRGWAK QPGYHTVQGQ IEQNLALIYQ TPINIYGSGR TDKGVHAINQ TFHVDLPDKL PLKQLIAKLN QLNYPDIFVK ALVPVAPRFH ARFAVKTKVY EYLINTRAFN PAQYHTVWQY NHPLDLAQLE ADTTLFLGRK DFWSFSTASQ KDTQRTISKI IVQQDHTGTV KLTFFGNGFL RNQIRMMVAS LVALNNRTLM RETVQQLFDQ PQKGGCKVKA PACGLYLKTV LYE // ID TSAD_MYCPN Reviewed; 319 AA. AC P75055; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. 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=MPN_059; ORFNames=MP095; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95743.1; -; Genomic_DNA. DR PIR; S73421; S73421. DR RefSeq; NP_109747.1; NC_000912.1. DR RefSeq; WP_010874416.1; NC_000912.1. DR ProteinModelPortal; P75055; -. DR IntAct; P75055; 2. DR EnsemblBacteria; AAB95743; AAB95743; MPN_059. DR GeneID; 876963; -. DR KEGG; mpn:MPN059; -. DR PATRIC; 20021395; VBIMycPne110_0059. DR KO; K01409; -. DR OMA; YTKEPGL; -. DR OrthoDB; EOG6K402S; -. DR BioCyc; MPNE272634:GJ6Z-61-MONOMER; -. DR Proteomes; UP000000808; 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; IPR017860; Peptidase_M22_CS. 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. DR PROSITE; PS01016; GLYCOPROTEASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 319 tRNA N6-adenosine FT threonylcarbamoyltransferase. FT /FTId=PRO_0000096968. FT REGION 135 139 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT METAL 110 110 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 114 114 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 301 301 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 168 168 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 181 181 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 185 185 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 277 277 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. SQ SEQUENCE 319 AA; 35210 MW; 39021A8BBC6A95CE CRC64; MEQPLCILGI ETTCDDTSIG VITESKVQAH IVLSSAKLHA QTGGVVPEVA ARSHEQNLLK ALQQSGVVLE QITHIAYAAN PGLPGCLHVG ATFARSLSFL LDKPLLPINH LYAHIFSALI DQDINQLKLP ALGLVVSGGH TAIYLIKSLF DLELIAETSD DAIGEVYDKV GRAMGFPYPA GPQLDSLFQP ELVKSHYFFR PSTKWTKFSY SGLKSQCFTK IKQLRERKGF NPQTHDWNEF ASNFQATIID HYINHVKDAI QQHQPQMLLL GGGVSANKYL REQVTQLQLP YLIAPLKYTS DNGAMIGFYA NLLINGKNN // ID ULAA_MYCPN Reviewed; 660 AA. AC P75291; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Ascorbate-specific permease IIC component UlaA; DE AltName: Full=Ascorbate-specific PTS system EIIC component; GN Name=ulaA; Synonyms=sgaT; OrderedLocusNames=MPN_496; ORFNames=MP347; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (PTS), a major carbohydrate active- CC transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitant with their translocation across the cell CC membrane. This system is involved in ascorbate transport (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- DOMAIN: In classical PTS systems, the EIIC domain forms the CC translocation channel and contains the specific substrate-binding CC site. UlaA does not exhibit the topological features of any CC recognized enzyme IIC. CC -!- SIMILARITY: Belongs to the UlaA 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; U00089; AAB95995.1; -; Genomic_DNA. DR PIR; S73673; S73673. DR RefSeq; NP_110184.1; NC_000912.1. DR RefSeq; WP_010874852.1; NC_000912.1. DR ProteinModelPortal; P75291; -. DR EnsemblBacteria; AAB95995; AAB95995; MPN_496. DR GeneID; 877364; -. DR KEGG; mpn:MPN496; -. DR PATRIC; 20022418; VBIMycPne110_0536. DR KO; K03475; -. DR OMA; TNVHSLM; -. DR OrthoDB; EOG64JFNM; -. DR BioCyc; MPNE272634:GJ6Z-537-MONOMER; -. DR Proteomes; UP000000808; 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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR InterPro; IPR004703; PTS_sugar-sp_permease. DR Pfam; PF03611; EIIC-GAT; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphotransferase system; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 660 Ascorbate-specific permease IIC component FT UlaA. FT /FTId=PRO_0000097715. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 307 327 Helical. {ECO:0000255}. FT TRANSMEM 362 382 Helical. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. FT TRANSMEM 422 442 Helical. {ECO:0000255}. FT TRANSMEM 450 470 Helical. {ECO:0000255}. FT TRANSMEM 480 500 Helical. {ECO:0000255}. FT TRANSMEM 592 612 Helical. {ECO:0000255}. FT TRANSMEM 615 635 Helical. {ECO:0000255}. SQ SEQUENCE 660 AA; 70859 MW; AA45EC672921BAA8 CRC64; MLNKIKLQQK RKLIIGWSVF ALINLVVILL TVLLRAGLPN LVSKGVTPFS AQAFGDAFIF LITRVYLDNF LRQPALLLGV ITLIGYLALG RGGVQSVVGA LKTVIGFILL SIGSGVLVST ARPVFDTIKG LGGTGVVLLD PYFSLASAND FFTNSFLNND YVSLIAFSLL VGFIVNIIFV GLKRWTNTNS IMVTGHVMLQ QAAVVTTLFY IVLFRQIPLL GTGIAYGAQA GLVIISGIFL GVYWSTASTG TYLVTNKVTN NAGFSIGHQQ MLGIMTVAKL GKYFGDKNDS AEHKKLPKAL KIFEDNIFTQ TIIILSLFVV LFIVILASYK GDKPLLINWD KFGAINGLEI WNTTFGGANF TLNIIGGALK MVASLIAIMT GVRMFITELQ QAFQGISEKV VPGAVVAVDI AAVYGFSINS VTFGFLSGVI GQFLAVAIMA GISYIPGNQF SFVAIPLFIT LFFNSGAFGV YANAEGGWKA ALLLPGIIGF LEIIVISFAL RTVSNAYQAS ALLDAKQSFD LKALMGNSLD NNNGSALKTA VEKVVNATGV NRITEAQSFV KSDSFNSLKA VNSTLAQAIE WISKSASPVD NGFIGMADWN LYFGLLVWIG AYNVIGGWIL VILATVGLIL LAQIIDNGKQ TKVTKLQQLL KINPQLDLNN // ID ULAB_MYCPN Reviewed; 95 AA. AC Q9EXD8; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Ascorbate-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.194; DE AltName: Full=Ascorbate-specific PTS system EIIB component; GN Name=ulaB; Synonyms=sgaB; OrderedLocusNames=MPN_495; ORFNames=MP347.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in ascorbate transport (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + L- CC ascorbate(Side 1) = [protein]-L-histidine + L-ascorbate 6- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00422}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34743.1; -; Genomic_DNA. DR RefSeq; NP_110183.1; NC_000912.1. DR RefSeq; WP_010874851.1; NC_000912.1. DR ProteinModelPortal; Q9EXD8; -. DR EnsemblBacteria; AAG34743; AAG34743; MPN_495. DR GeneID; 877366; -. DR KEGG; mpn:MPN495; -. DR PATRIC; 20022416; VBIMycPne110_0535. DR KO; K02822; -. DR OMA; MDVNEIK; -. DR OrthoDB; EOG6J48VN; -. DR BioCyc; MPNE272634:GJ6Z-536-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR InterPro; IPR013011; PTS_EIIB_2. DR InterPro; IPR003501; PTS_EIIB_2/3. DR Pfam; PF02302; PTS_IIB; 1. DR SUPFAM; SSF52794; SSF52794; 1. DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Kinase; Phosphotransferase system; KW Reference proteome; Transferase; Transport. FT CHAIN 1 95 Ascorbate-specific phosphotransferase FT enzyme IIB component. FT /FTId=PRO_0000186688. FT DOMAIN 1 95 PTS EIIB type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00422}. FT ACT_SITE 12 12 Phosphocysteine intermediate. FT {ECO:0000250}. SQ SEQUENCE 95 AA; 10327 MW; 486BF2F3E2E4AEA9 CRC64; MENKNLHIIA ACGNGMGTSM LIKIKVEKIM KELGYTAKVE ALSMGQTKGM EHSADIIISS IHLTSEFNPN AKAKIVGVLN LMDENEIKQA LSKVL // ID ULAC_MYCPN Reviewed; 159 AA. AC P75292; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Ascorbate-specific phosphotransferase enzyme IIA component; DE EC=2.7.1.-; DE AltName: Full=PTS system ascorbate-specific EIIA component; GN Name=ulaC; Synonyms=sgaA; OrderedLocusNames=MPN_494; ORFNames=MP348; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in ascorbate transport (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine + CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L- CC histidine/cysteine. {ECO:0000255|PROSITE-ProRule:PRU00417}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95996.1; -; Genomic_DNA. DR PIR; S73674; S73674. DR RefSeq; NP_110182.1; NC_000912.1. DR RefSeq; WP_010874850.1; NC_000912.1. DR ProteinModelPortal; P75292; -. DR EnsemblBacteria; AAB95996; AAB95996; MPN_494. DR GeneID; 877250; -. DR KEGG; mpn:MPN494; -. DR PATRIC; 20022414; VBIMycPne110_0534. DR KO; K02821; -. DR OMA; YKYGPYI; -. DR OrthoDB; EOG68DCVK; -. DR BioCyc; MPNE272634:GJ6Z-535-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR Pfam; PF00359; PTS_EIIA_2; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Phosphotransferase system; KW Reference proteome; Transferase; Transport. FT CHAIN 1 159 Ascorbate-specific phosphotransferase FT enzyme IIA component. FT /FTId=PRO_0000186685. FT DOMAIN 9 152 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT ACT_SITE 71 71 Tele-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00417}. SQ SEQUENCE 159 AA; 17808 MW; 85FEEAC315E735B6 CRC64; MTKLDFKAVL KQHHTVRLHQ TAQDWKQAIQ LCIHPLIAAK LVQPAYFDDI LKSVAQYGPY FIIAENVAMP HAQNNGTVQQ NCFSLVTLKE PVYFDNDPRP VRLLIGLAAT SAAIHTTEAL PQIAALVEDT QVVKDLLDCC DETSLFAVID RVNLHKYLT // ID ULAF_MYCPN Reviewed; 242 AA. AC P75289; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Probable L-ribulose-5-phosphate 4-epimerase UlaF; DE EC=5.1.3.4; DE AltName: Full=L-ascorbate utilization protein F; DE AltName: Full=Phosphoribulose isomerase; GN Name=ulaF; Synonyms=sgaE; OrderedLocusNames=MPN_498; ORFNames=MP345; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to CC D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate CC utilization (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = D-xylulose 5- CC phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose CC 5-phosphate from L-ascorbate: step 4/4. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95992.1; -; Genomic_DNA. DR PIR; S73671; S73671. DR RefSeq; NP_110186.1; NC_000912.1. DR RefSeq; WP_010874854.1; NC_000912.1. DR ProteinModelPortal; P75289; -. DR SMR; P75289; 5-228. DR EnsemblBacteria; AAB95992; AAB95992; MPN_498. DR GeneID; 877253; -. DR KEGG; mpn:MPN498; -. DR PATRIC; 20022428; VBIMycPne110_0541. DR KO; K03077; -. DR OMA; NPLHTPG; -. DR OrthoDB; EOG6358F1; -. DR BioCyc; MPNE272634:GJ6Z-539-MONOMER; -. DR UniPathway; UPA00263; UER00380. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 242 Probable L-ribulose-5-phosphate 4- FT epimerase UlaF. FT /FTId=PRO_0000162922. FT METAL 80 80 Zinc. {ECO:0000250}. FT METAL 99 99 Zinc. {ECO:0000250}. FT METAL 101 101 Zinc. {ECO:0000250}. FT METAL 175 175 Zinc. {ECO:0000250}. SQ SEQUENCE 242 AA; 27092 MW; 3F326B0F364CBB8B CRC64; MDQKMINDLK EQVFQTNLLL PKYGLVIHTW GNVSMIAPNR QFFVIKPSGV SYDKMRAQDM VVVDLDNNVL DTNGLKPSSD TPTHALMYKH CPDIKAIVHT HSTFATSFAQ ADKPIPCLGT THADNFFGPI PCTRALSDSE INGAYEHNTG LVILEHLKNN QVDVNACAAI LVKEHGSFVW SNKNGKDAVD RALTLEQVAQ MALYTQMINP HMKEANPALQ QKHYNRKHGK DAYYGQDTKQ ED // ID TYSY_MYCPN Reviewed; 287 AA. AC P78029; Q50354; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 101. 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=MPN_320; ORFNames=MP516; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-212. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). 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 -!- SEQUENCE CAUTION: CC Sequence=AAB96164.1; 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; U00089; AAB96164.1; ALT_INIT; Genomic_DNA. DR EMBL; Z32654; CAA83575.1; -; Genomic_DNA. DR PIR; S73842; S73842. DR RefSeq; NP_110008.2; NC_000912.1. DR RefSeq; WP_010874676.1; NC_000912.1. DR ProteinModelPortal; P78029; -. DR SMR; P78029; 2-287. DR IntAct; P78029; 3. DR EnsemblBacteria; AAB96164; AAB96164; MPN_320. DR GeneID; 876944; -. DR KEGG; mpn:MPN320; -. DR PATRIC; 20021994; VBIMycPne110_0344. DR KO; K00560; -. DR OMA; IVYELLW; -. DR OrthoDB; EOG6K6V53; -. DR BioCyc; MPNE272634:GJ6Z-337-MONOMER; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000808; 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; 1. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW Nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 287 Thymidylate synthase. FT /FTId=PRO_0000140987. FT ACT_SITE 170 170 {ECO:0000255|HAMAP-Rule:MF_00008}. FT CONFLICT 204 212 SYSLLVYLV -> FLLSYGA (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 287 AA; 33591 MW; DAD2E84FCD9C5EDE CRC64; MQQYLDLARY VLEHGKYRPN RTDTAGIGVF GYQMHFDISK HFPLLTTKKV HWKSIVHELL WFIKGDTNIK YLVDNKVNIW NEWPYESFKK SPHFNGESQK EFIERIRQDA KFAQQFGNLG PVYGKQWRDF NGVDQLKKVI AQIKVNPFSR RLIVSSWNPN EVDQMLLPPC HSLYQFYVQD GQLSCQLYQR SGDIFLGIPF NIASYSLLVY LVAKETNLKP GSFVHTIGDA HIYENHLEQI KLQLTRQPKP LPKVVLKSDK SIFDYQFDDI ELVDYDHHPT IKGEVAV // ID UNG_MYCPN Reviewed; 240 AA. AC P75536; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uracil-DNA glycosylase; DE Short=UDG; DE EC=3.2.2.27; GN Name=ung; OrderedLocusNames=MPN_235; ORFNames=MP596; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched CC double-stranded DNA and polynucleotides, releasing free uracil. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase 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; U00089; AAB96244.1; -; Genomic_DNA. DR PIR; S73922; S73922. DR RefSeq; NP_109923.1; NC_000912.1. DR RefSeq; WP_010874592.1; NC_000912.1. DR ProteinModelPortal; P75536; -. DR IntAct; P75536; 2. DR EnsemblBacteria; AAB96244; AAB96244; MPN_235. DR GeneID; 877251; -. DR KEGG; mpn:MPN235; -. DR PATRIC; 20021795; VBIMycPne110_0254. DR KO; K03648; -. DR OMA; SARYGFF; -. DR OrthoDB; EOG6MSS63; -. DR BioCyc; MPNE272634:GJ6Z-242-MONOMER; -. DR Proteomes; UP000000808; 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 1 240 Uracil-DNA glycosylase. FT /FTId=PRO_0000176116. FT ACT_SITE 70 70 Proton acceptor. {ECO:0000250}. SQ SEQUENCE 240 AA; 27819 MW; 8CF2B492009F4A2C CRC64; MEQLLDQFLS GVLSEWKAFI LQEAKQTYFQ ELLAKLKNVE QELTPKASQV FRPFSFFAPN NTKLIIYGQD PYPNPQHACG LSFASNAPKL PQSLKRMILR LQQEYPELAG QNHWTKQLLE GWAQQGILLL NGVFTTNAFQ TNAHRNWGWE QFNCHLLDFL LSQKLYVLLV FLGKQTENFV LKKIGGASQF ASLSYPHPSP LTGRKFFDHP DALFKQINQW LKHHNHTPID WTNGQVQYQF // ID ULAE_MYCPN Reviewed; 305 AA. AC P75294; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable L-ribulose-5-phosphate 3-epimerase UlaE; DE EC=5.1.3.22; DE AltName: Full=L-ascorbate utilization protein E; DE AltName: Full=L-xylulose-5-phosphate 3-epimerase; GN Name=ulaE; Synonyms=sgaU; OrderedLocusNames=MPN_492; ORFNames=MP350; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to CC L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate CC utilization (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = L-xylulose 5- CC phosphate. CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose CC 5-phosphate from L-ascorbate: step 3/4. CC -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95998.1; -; Genomic_DNA. DR PIR; S73676; S73676. DR RefSeq; NP_110180.1; NC_000912.1. DR RefSeq; WP_010874848.1; NC_000912.1. DR ProteinModelPortal; P75294; -. DR IntAct; P75294; 3. DR EnsemblBacteria; AAB95998; AAB95998; MPN_492. DR GeneID; 877214; -. DR KEGG; mpn:MPN492; -. DR PATRIC; 20022410; VBIMycPne110_0532. DR KO; K03079; -. DR OMA; SMCLSGH; -. DR OrthoDB; EOG6FFS58; -. DR BioCyc; MPNE272634:GJ6Z-533-MONOMER; -. DR UniPathway; UPA00263; UER00379. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro. DR GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR004560; L-Ru-5P_3-Epase. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR00542; hxl6Piso_put; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 305 Probable L-ribulose-5-phosphate 3- FT epimerase UlaE. FT /FTId=PRO_0000097717. SQ SEQUENCE 305 AA; 34888 MW; DCDB9D0709CBA51B CRC64; MLVIHFKPYN NLKMSFTSTE NKHLLGVYEK AINNKFAWKD KIAIAKQASF DFIELSIDES DARLQRLDWS DTEINQLHNE LQAQTFCLNS MCLSAHRRFP LGSKNKTTVQ QGLTIFEKAC VLARKLGIRI IQLAAYDVYY EPHDTETERN FITNMRKVAE LAQKYAVTIA FEVMDTPFAG TIVRCLNLIK RIGKANILLY PDIGNLSQFS TAVFDEIALG QDKIVGFHFK DTLPKQFKEV PFGTGTAQFE AALKAIHQYV PTVPILIEMW SKNDPAESTV QNVAQLKQAK QFYEQQWDLA LKRVK // ID UVRB_MYCPN Reviewed; 657 AA. AC P75558; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. 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=MPN_211; ORFNames=MP620; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96268.1; -; Genomic_DNA. DR PIR; S73946; S73946. DR RefSeq; NP_109899.1; NC_000912.1. DR RefSeq; WP_010874568.1; NC_000912.1. DR ProteinModelPortal; P75558; -. DR SMR; P75558; 9-598. DR IntAct; P75558; 1. DR EnsemblBacteria; AAB96268; AAB96268; MPN_211. DR GeneID; 877052; -. DR KEGG; mpn:MPN211; -. DR PATRIC; 20021747; VBIMycPne110_0230. DR KO; K03702; -. DR OMA; YQEFREF; -. DR OrthoDB; EOG6B360R; -. DR BioCyc; MPNE272634:GJ6Z-218-MONOMER; -. DR Proteomes; UP000000808; 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 1 657 UvrABC system protein B. FT /FTId=PRO_0000138409. FT DOMAIN 29 416 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 435 597 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 615 650 UVR. {ECO:0000255|HAMAP-Rule:MF_00204}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_00204}. FT MOTIF 95 118 Beta-hairpin. SQ SEQUENCE 657 AA; 75193 MW; 5D367BEFB3F04618 CRC64; MKSPTKDSKL FHLKSNFAPT GDQPAAIAKL AEFQTNEQVL LGATGTGKTF TIANVIQKVQ LPTVVIAHNK TLAGQLYQEL KELFPNNAVE YFISYFDFYQ PEAYLPAKGV YIEKSATVNE EIKRLRVSTL HSLSTRKDVI VVGSVASIYP TSSPADFAQY SLWLVVGKEY GLSELKTQLI HLNYVVNKQQ LTPGKFRFQG DVVEVFPGYA QDYVLRLSFF DQQLEQIARI DPLTNKVLET LNSFKLGPAD EYIVNQNDLG VALDTIKAEL KDRLKYFERL NFPERAQRLQ TITEHDLADL KAWGVCSGVE NYARHLEHRP PHSKPYNIFD YFTKGEWLLV VDESHQTLPQ IKGMYNTDIS RKQSLIEYGF RLPSALDNRP LSYEEFRQGI NKVIYVSATP REEEIQLSHN NVVEQLVRPT YLLDPEVIVK PKDNQVEDLV SEIINQRKHN GRTFVTVLTI KMAENLTDFL KERNIKVAYI HKDIKALERL ILLTDLRKGE YECLVGINLL REGLDVPEVS LVAIFDADIP GLPRDERSLI QIIGRAARNV HGRVIMYANT ISEQMDKAIK ETQRRRTIQM AYNEQHHKTP MTVQKPITLN QPIKLKTKSS EQQKAALIKQ LTKEMKQAAA NQNYELAIEI RDSIFELEKQ FRGKIKS // ID ULAD_MYCPN Reviewed; 218 AA. AC P75293; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable 3-keto-L-gulonate-6-phosphate decarboxylase; DE Short=KGPDC; DE EC=4.1.1.85; DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase; DE AltName: Full=L-ascorbate utilization protein D; GN Name=ulaD; Synonyms=sgaH; OrderedLocusNames=MPN_493; ORFNames=MP349; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9274005; RA Reizer J., Reizer A., Saier M.H. Jr.; RT "Is the ribulose monophosphate pathway widely distributed in RT bacteria?"; RL Microbiology 143:2519-2520(1997). CC -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P CC into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate CC utilization (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 3-dehydro-L-gulonate 6-phosphate = L-xylulose CC 5-phosphate + CO(2). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose CC 5-phosphate from L-ascorbate: step 2/4. CC -!- INTERACTION: CC Q50333:MPN_596; NbExp=1; IntAct=EBI-2260297, EBI-2260294; CC -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95997.1; -; Genomic_DNA. DR PIR; S73675; S73675. DR RefSeq; NP_110181.1; NC_000912.1. DR RefSeq; WP_010874849.1; NC_000912.1. DR ProteinModelPortal; P75293; -. DR SMR; P75293; 3-217. DR IntAct; P75293; 1. DR EnsemblBacteria; AAB95997; AAB95997; MPN_493. DR GeneID; 877220; -. DR KEGG; mpn:MPN493; -. DR PATRIC; 20022412; VBIMycPne110_0533. DR KO; K03078; -. DR OMA; TIPTMKA; -. DR OrthoDB; EOG66B435; -. DR BioCyc; MPNE272634:GJ6Z-534-MONOMER; -. DR UniPathway; UPA00263; UER00378. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. 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. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Decarboxylase; Lyase; KW Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 218 Probable 3-keto-L-gulonate-6-phosphate FT decarboxylase. FT /FTId=PRO_0000212104. FT METAL 33 33 Magnesium. {ECO:0000250}. FT METAL 62 62 Magnesium. {ECO:0000250}. FT BINDING 11 11 Substrate. {ECO:0000250}. FT BINDING 194 194 Substrate. {ECO:0000250}. FT SITE 64 64 Transition state stabilizer. FT {ECO:0000250}. FT SITE 67 67 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 218 AA; 24133 MW; 5285E03888F1CBA4 CRC64; MALPLIQIAL DNLSLASALN DLAKVGDAVD VIEVGTILLT AEGVNAVKEI AKRYPHKLIV ADGKIADTGK VFNQMFFDAG AHFTTVICAA ELPTVKDVVT VGNSYTPIKE TQVEMTSNFT WEQVTQWKQV GVQQVVWHRS RDAQAAGVNW SDKDLQAVKR LADLGFKVTV TGGITLNDIQ LFKDIPIYIF IAGRTIRDAS DPLQTVQQFK DEFHKYWK // ID URK_MYCPN Reviewed; 213 AA. AC P75217; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uridine kinase; DE EC=2.7.1.48; DE AltName: Full=Cytidine monophosphokinase; DE AltName: Full=Uridine monophosphokinase; GN Name=udk; OrderedLocusNames=MPN_561; ORFNames=MP281; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP. CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage CC pathway; CTP from cytidine: step 1/3. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uridine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95929.1; -; Genomic_DNA. DR PIR; S73607; S73607. DR RefSeq; NP_110250.1; NC_000912.1. DR RefSeq; WP_010874918.1; NC_000912.1. DR ProteinModelPortal; P75217; -. DR EnsemblBacteria; AAB95929; AAB95929; MPN_561. DR GeneID; 876884; -. DR KEGG; mpn:MPN561; -. DR PATRIC; 20022601; VBIMycPne110_0623. DR KO; K00876; -. DR OMA; FNEELMF; -. DR OrthoDB; EOG6KMBCH; -. DR BioCyc; MPNE272634:GJ6Z-607-MONOMER; -. DR UniPathway; UPA00574; UER00637. DR UniPathway; UPA00579; UER00640. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00551; Uridine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006083; PRK/URK. DR InterPro; IPR000764; Uridine_kinase-like. DR InterPro; IPR026008; Uridine_kinase_. DR Pfam; PF00485; PRK; 1. DR PRINTS; PR00988; URIDINKINASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00235; udk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 213 Uridine kinase. FT /FTId=PRO_0000164481. FT NP_BIND 13 20 ATP. {ECO:0000255}. SQ SEQUENCE 213 AA; 24912 MW; 1FBD5843609068A9 CRC64; MDSKKGILVA IGGGSCSGKT TIADMIYQLL RKKLKVAILP QDNYYKPYKN KSMAQRKAIN FDHPDAFDWK LLWSHLDNLL MGKTVAVPMY DYVNYTRKKE TIEIGPLNVV ILEGLMPWFD ERIAKLCKLK IFVEATGEER LIRRIERDWE RGRDVASIIK QWREAVSPMY EIFVEKMKQK ADLIIPWSER HEVSTNVLDF AIEHLFRKHV DPN // ID UVRC_MYCPN Reviewed; 586 AA. AC P75350; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. 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=MPN_125; ORFNames=MP029; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrC both incises the 5' and 3' sides CC of the lesion. The N-terminal half is responsible for the 3' CC incision and the C-terminal half is responsible for the 5' CC incision. {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBUNIT: Interacts with UvrB in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95677.1; -; Genomic_DNA. DR PIR; S73355; S73355. DR RefSeq; NP_109813.1; NC_000912.1. DR RefSeq; WP_010874482.1; NC_000912.1. DR ProteinModelPortal; P75350; -. DR IntAct; P75350; 1. DR EnsemblBacteria; AAB95677; AAB95677; MPN_125. DR GeneID; 877114; -. DR KEGG; mpn:MPN125; -. DR PATRIC; 20021551; VBIMycPne110_0132. DR KO; K03703; -. DR OMA; GAINSYK; -. DR OrthoDB; EOG6K13R9; -. DR BioCyc; MPNE272634:GJ6Z-132-MONOMER; -. DR Proteomes; UP000000808; 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 HAMAP; MF_00203; UvrC; 1. DR InterPro; IPR027299; GIY-YIG_dom. DR InterPro; IPR000305; GIY-YIG_SF. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004791; UvrC. DR InterPro; IPR001162; UvrC_homol_region. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF08459; UvrC_HhH_N; 1. DR SMART; SM00465; GIYc; 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 1 586 UvrABC system protein C. FT /FTId=PRO_0000138318. FT DOMAIN 17 94 GIY-YIG. {ECO:0000255|HAMAP- FT Rule:MF_00203}. FT DOMAIN 201 236 UVR. {ECO:0000255|HAMAP-Rule:MF_00203}. SQ SEQUENCE 586 AA; 67771 MW; 6A495512C3447C81 CRC64; MIIVNNTLAF KLKNAPHKPG CYLWKDDAGQ VLYVGKAKDI FKRVHHYFNP NRSFKTRALV ERIADVEYVI LKNENDALNL EAKLIKQYKP RFNLVLKENN GYLYFFITAS VKPTLELGRR YEFSKNKYFG PFASSKFRLR DIYDLLLKLF PLRKCAPHER GHPCFYYQLK MCMGQCMGED TPERYQTTVK GIEQFFNHGP EQVLNHLQQQ EIKASEQQNF EAARHFLDLQ KAVLELVNMQ QTAFIKAKQS HDFIGYVFEK NVLAITVFAY VDNQLIGKNQ QVFELPQDDE KEVESALVTF IYHYYSTNKI PKTLTVSLSE ENLSLLANSL KINVTQPKNG EQKSILQTVI DNARYALNTK WTGFINNLNR AEVHQQLAQL LQVPSIQSLE IIDISFYDKD HVVGAMLRYE NGKRMKALSR RYNINIDHKG DTNYMADVVY RRIISSIQTH KQLPLSDLLI VDGGIAQINT VTKVFASFPN VTQPIIIGLA KNTRHQTDHI VLTDNTTINI DKNTPLFAYL TTIQEEVDSF AKHNAFKRVS RARFQNPLLQ IEGVGRKTVQ ILLDNFQTNA KHWSCFFERI ITVYSC // ID UVRD_MYCPN Reviewed; 715 AA. AC P75437; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Probable DNA helicase II homolog; DE EC=3.6.4.12; GN Name=uvrD; OrderedLocusNames=MPN_341; ORFNames=MP495; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA CC duplexes with 3' to 5' polarity with respect to the bound strand CC and initiates unwinding most effectively when a single-stranded CC region is present. Involved in the post-incision events of CC nucleotide excision repair and methyl-directed mismatch repair (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00560}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00617}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96143.1; -; Genomic_DNA. DR PIR; S73821; S73821. DR RefSeq; NP_110029.1; NC_000912.1. DR RefSeq; WP_010874697.1; NC_000912.1. DR ProteinModelPortal; P75437; -. DR IntAct; P75437; 2. DR EnsemblBacteria; AAB96143; AAB96143; MPN_341. DR GeneID; 876740; -. DR KEGG; mpn:MPN341; -. DR PATRIC; 20022036; VBIMycPne110_0365. DR KO; K03657; -. DR OMA; FAICDAG; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; MPNE272634:GJ6Z-358-MONOMER; -. DR Proteomes; UP000000808; 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:0003677; F:DNA 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; 3.40.50.300; -; 4. 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; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 715 Probable DNA helicase II homolog. FT /FTId=PRO_0000102077. FT DOMAIN 7 295 UvrD-like helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00560}. FT DOMAIN 296 554 UvrD-like helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00617}. FT NP_BIND 31 36 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00560}. FT BINDING 293 293 ATP. {ECO:0000250}. SQ SEQUENCE 715 AA; 83497 MW; D68896507E933181 CRC64; MAFNISTQLN KEQRAAVTCG KGVNIVYSGA GTGKTTIISQ RFAYLFNQKR INPSNILALT YTRKAASEMK QRILELLPEK YHKDVNIYTF HSFCSRFLRE EGQKNFVIDD DLSNFLKDFL KESELKSQKV LQIIDGFKNA YFDFDTNSLK DDERLVELCE FHLDPQERNF QLFKETAIAA FVEYEKGKQQ NNKIDFADLL IKTCTLLSKD HKLLRKWSKK FQYILGDEFQ DTNQIQYELI KMLASHHQNL FLVGDNNQMI YRWRGAVSDI IDSLKSDFKV RPENEFYITQ NYRCDQNILT VANSILGTIY AKENQPDSTK GFLFSAIKSN RLPVYFQASS VEGQHSWIIN KIKNLHKNHG IQYKDMAILF RTNRNMDSMT EALEADGSIP LKQNKGFFKQ LETFKKVLVA LITRSNYDIK LALKSLRVWP NVLNKSLTVN EQVNLDKILQ NLEQAIFLDE HTRGELTEAA KVFTRLIKFV EEQQFEALLA FTFEALNTDQ FVCNFIFRTL QKLQTENKNF TITDFINELR FQQDELKQSK DNVINLITVH SAKGLEFEAV FIYGINQDNF PLKSKNQIID LQRELDELRL FYVALTRAKK YLFLLSVYQM SGEIIYPSKF IRFINKEDRL EIATINHKVH QDDEFFDSSK TEDYQKKYLT ENTDFVNGDS VSHRTYGKGV VVEVREDAVC VAFKNSKYGQ RWIVKNHRDL VKAVY // ID UPP_MYCPN Reviewed; 206 AA. AC P75081; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 20-JAN-2016, entry version 96. 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=MPN_033; GN ORFNames=MP121; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAG34738.1; -; Genomic_DNA. DR PIR; S73447; S73447. DR RefSeq; NP_109721.1; NC_000912.1. DR RefSeq; WP_010874390.1; NC_000912.1. DR ProteinModelPortal; P75081; -. DR SMR; P75081; 4-206. DR IntAct; P75081; 8. DR EnsemblBacteria; AAG34738; AAG34738; MPN_033. DR GeneID; 877341; -. DR KEGG; mpn:MPN033; -. DR PATRIC; 20021341; VBIMycPne110_0032. DR KO; K00761; -. DR OMA; TIEGWCG; -. DR OrthoDB; EOG6HF5WX; -. DR BioCyc; MPNE272634:GJ6Z-35-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000808; 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 1 206 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120856. FT REGION 128 136 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT REGION 196 198 Uracil binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT BINDING 76 76 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 101 101 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 191 191 Uracil; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 197 197 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. SQ SEQUENCE 206 AA; 22750 MW; 681506D3C62CC884 CRC64; MIKKVHHALI ENELTKLRDK SSSSSQFRMA LSQITSLLFF EVTKESPLEE IVVKTPFTKT KGYKLKNEIV LVPIMRAGLG MVDPIVRYSE KIRVGHLGIY REHEGTNVIS YYKKMPENIG NSHVIILDPM LATGTTLATA ISSIKKNHPI KISVVAIVAA PEGIKAVEAA HPDVDIYLAA IDEKLNKDNY IIPGLGDAGD RLFGTK // ID UVRA_MYCPN Reviewed; 948 AA. AC P75176; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205}; DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; GN OrderedLocusNames=MPN_619; ORFNames=MP223; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding CC protein. A damage recognition complex composed of 2 UvrA and 2 CC UvrB subunits scans DNA for abnormalities. When the presence of a CC lesion has been verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95871.1; -; Genomic_DNA. DR PIR; S73549; S73549. DR RefSeq; NP_110308.1; NC_000912.1. DR RefSeq; WP_010874976.1; NC_000912.1. DR ProteinModelPortal; P75176; -. DR SMR; P75176; 9-948. DR IntAct; P75176; 3. DR EnsemblBacteria; AAB95871; AAB95871; MPN_619. DR GeneID; 876802; -. DR KEGG; mpn:MPN619; -. DR PATRIC; 20022721; VBIMycPne110_0683. DR KO; K03701; -. DR OMA; GAIKGWD; -. DR OrthoDB; EOG6QK4PS; -. DR BioCyc; MPNE272634:GJ6Z-665-MONOMER; -. DR Proteomes; UP000000808; 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 Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; SSF52540; 5. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; DNA-binding; Excision nuclease; Metal-binding; KW Nucleotide-binding; Reference proteome; Repeat; SOS response; Zinc; KW Zinc-finger. FT CHAIN 1 948 UvrABC system protein A. FT /FTId=PRO_0000093066. FT DOMAIN 316 595 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT DOMAIN 615 944 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 38 45 ATP 1. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 259 286 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 647 654 ATP 2. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 746 772 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. SQ SEQUENCE 948 AA; 105426 MW; 4466DE773D3B370C CRC64; MKPELKTNDF IRVKGARENN LKNVNIDIPK NQFVVITGLS GSGKSSLAFN TIYAEGRRRY LESLSSYARQ FLGNSDKPDV DSIEGLSPAI SIDQKTTSHN PRSTVGTVTE IYDYLRLLWA RIGIPFCPNG HGAIQTQTVN QIANQIFNLP VKSRIQILAP TIKNQRGTFA NEFAKYQQLG FLRVWVDGQV YTLDEEIKLD KNTKHNLSVV VDRIVINQDK QTLGRIVDAI EGVIKLTEGR IEVLLEDGKI LSFNKNHGCD QCGFSISELE PRLFSFNSPL GSCEYCKGLG FSYEPDVEKI IPNPLLSINE GGIDIFKNIV HGTSLDWQRF LSLINHYQIP LDQPLGQMDT DLVRMILEGS DEPIEIKTVS NSGAKNVRFE HYEGVAHLIK RRHLETSSQA SREWYSAYMS EITCKKCQGK KLTTNSLSVK LGGLDIISFT ELSIDKAIEF LLQIELNQEQ KKIGELALKE IINRLSFLKN VGLEYLNLAR RASTLSGGEA QRIRLATQIG SQLTGVLYVL DEPSIGLHQK DNDRLINTMM VMRDLGNTLL VVEHDSETML AADYLIDIGP KAGNQGGEVV AAGTPLEVME NPDSLTGQYL SGKKQIEVPK TRHAGNGRTL TLKGAKGNNL KNINVTIPLN KLVLVTGVSG SGKSTLINQT LVPILERLVN YKNVKPAPYK EIIGVNHIDK VVVVSQDPIG RTPRSNPATY VSVFDDIREL FANTKEAKAR GYTNSRFSFN VAGGRCDKCF GDGVIRIEMH FLPDVYVTCE MCDGKKYNPQ TLEVKYLGKS IFDVLQMSCQ EAYDFFKAIP NIARKLKLLC DVGLEYLQLG LNVTFLSGGE AQRIKLAKFL QKKATGKTLY VLDEPSTGLH IEDINKLLTV IQRIIKNGDS VIIIEHNLDI IKMADYIIDL GPEGGEKGGQ IIAQGTPEQL LNQVDKSYTA QYLAKILK // ID Y009_MYCPN Reviewed; 261 AA. AC P78005; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Uncharacterized metal-dependent hydrolase MPN_009 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=MPN_009; ORFNames=D12_orf261, MP145; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P0AFQ7}; CC Note=Binds 2 divalent metal cations per subunit. CC {ECO:0000250|UniProtKB:P0AFQ7}; CC -!- SIMILARITY: Belongs to the TatD-type hydrolase 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; U00089; AAB95793.1; -; Genomic_DNA. DR PIR; S73471; S73471. DR RefSeq; NP_109697.1; NC_000912.1. DR RefSeq; WP_010874366.1; NC_000912.1. DR ProteinModelPortal; P78005; -. DR IntAct; P78005; 5. DR EnsemblBacteria; AAB95793; AAB95793; MPN_009. DR GeneID; 877360; -. DR KEGG; mpn:MPN009; -. DR PATRIC; 20021291; VBIMycPne110_0009. DR KO; K03424; -. DR OMA; GNWEKVR; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; MPNE272634:GJ6Z-9-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome. FT CHAIN 1 261 Uncharacterized metal-dependent hydrolase FT MPN_009. FT /FTId=PRO_0000202007. FT METAL 7 7 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 9 9 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 96 96 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 96 96 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 132 132 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 156 156 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 211 211 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 261 AA; 29820 MW; D2F2EA805864C3EB CRC64; MEYFDAHCHL NCEPLLEQHE KSLANFRLIG LKANVVGTNL TNSQIAVNLA KQHPDLLKAG VGIHPNDVQL FDLKAAQATL KKLVSTHRSF ISCIGEYGFD YHYTKDYITQ QEQFFLMQFQ LAEQYQLVHM LHVRDVHERI YEVLKRLKPK QPVVFHCFSE DTNTALKLLT LREVGLKVYF SIPGIVTFKN AKNLQAALSV IPTELLLSET DSPYLAPVPF RGKTNWPECV VHTVQTIADI KQVPLAEIKQ AIVHNAKKLF W // ID Y027_MYCPN Reviewed; 274 AA. AC P75087; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MPN_027; GN OrderedLocusNames=MPN_027; ORFNames=B01_orf274, MP127; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95775.1; -; Genomic_DNA. DR PIR; S73453; S73453. DR RefSeq; NP_109715.1; NC_000912.1. DR RefSeq; WP_010874384.1; NC_000912.1. DR ProteinModelPortal; P75087; -. DR IntAct; P75087; 2. DR EnsemblBacteria; AAB95775; AAB95775; MPN_027. DR GeneID; 876919; -. DR KEGG; mpn:MPN027; -. DR PATRIC; 20021329; VBIMycPne110_0026. DR OMA; AQIVENF; -. DR BioCyc; MPNE272634:GJ6Z-29-MONOMER; -. DR Proteomes; UP000000808; 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 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 274 Uncharacterized protein MPN_027. FT /FTId=PRO_0000210633. FT DOMAIN 39 179 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 274 AA; 32143 MW; EFB93EB7C004D18D CRC64; MDKNTILEFC FFGDRYQLMA LKNPNKLVKN KQVKAAFNVF MKHRTTLSAT NYMAQIVENF EQFLEYIHDK LQPGKLLALL FKNKQFLGWF CVGQWGNMPV LSFWIDPSQQ QSGVALETIS FFLKYYQRTL QPRELVWSFY ESNQRSRHLA NKLGFPSLFY FKKAEPNAPK VYFGTKDFKG ESVIETKPYL GWGSGWKVNQ MLKPTKNLTV NLINIGFDAY ADSQKALLAW FKTHKLTKGQ VEVFFNYELC CLCISYNHKQ SWVVYSFQQL LAKR // ID Y032_MYCPN Reviewed; 108 AA. AC P75082; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MG029 homolog; GN OrderedLocusNames=MPN_032; ORFNames=B01_orf108, MP122; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95770.1; -; Genomic_DNA. DR PIR; S73448; S73448. DR RefSeq; NP_109720.1; NC_000912.1. DR RefSeq; WP_010874389.1; NC_000912.1. DR ProteinModelPortal; P75082; -. DR IntAct; P75082; 3. DR EnsemblBacteria; AAB95770; AAB95770; MPN_032. DR GeneID; 876894; -. DR KEGG; mpn:MPN032; -. DR PATRIC; 20021339; VBIMycPne110_0031. DR OrthoDB; EOG65XN5N; -. DR BioCyc; MPNE272634:GJ6Z-34-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002818; DJ-1/PfpI. DR Pfam; PF01965; DJ-1_PfpI; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 108 Uncharacterized protein MG029 homolog. FT /FTId=PRO_0000210394. SQ SEQUENCE 108 AA; 12200 MW; 6C0D6FDA546E8B2C CRC64; MKKLLVIVYP DMNDVEYTNT MVVFGFVKEL QTVIYHPNLS TVKGSNGVTL VNQITSKVNL EEFDGVFIPG GMGATKVLDH DQQLLDTIRY FKDHDKYVFA ICDTPNVL // ID Y037_MYCPN Reviewed; 147 AA. AC P75077; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 04-FEB-2015, entry version 54. DE RecName: Full=Uncharacterized protein MPN_037; GN OrderedLocusNames=MPN_037; ORFNames=B01_orf147, MP117; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_465. {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; U00089; AAB95765.1; -; Genomic_DNA. DR PIR; S73443; S73443. DR RefSeq; NP_109725.1; NC_000912.1. DR RefSeq; WP_010874394.1; NC_000912.1. DR EnsemblBacteria; AAB95765; AAB95765; MPN_037. DR GeneID; 877333; -. DR KEGG; mpn:MPN037; -. DR BioCyc; MPNE272634:GJ6Z-39-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MPN_037. FT /FTId=PRO_0000210634. SQ SEQUENCE 147 AA; 17030 MW; 2080A27AD0DA625F CRC64; MPSSAFKINL SVSPWFFCST WSSLICWPWT ITTSVSRSTL SSTTWILWTW LFNSVSIFVS RWSFDFLYSL NSLRVTYSVF TGITGLLSLN CLLKLPENST LLLSLSIIYQ PEKVPFWSFS PCHEILFRYK TEFSLSLSHT SFLFSEI // ID Y051_MYCPN Reviewed; 384 AA. AC P75063; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MG039 homolog; GN OrderedLocusNames=MPN_051; ORFNames=D09_orf384, MP103; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95751.1; -; Genomic_DNA. DR PIR; S73429; S73429. DR RefSeq; NP_109739.1; NC_000912.1. DR RefSeq; WP_010874408.1; NC_000912.1. DR PDB; 4X9M; X-ray; 2.40 A; A=1-384. DR PDB; 4X9N; X-ray; 2.50 A; A=1-384. DR PDBsum; 4X9M; -. DR PDBsum; 4X9N; -. DR ProteinModelPortal; P75063; -. DR IntAct; P75063; 1. DR EnsemblBacteria; AAB95751; AAB95751; MPN_051. DR GeneID; 877174; -. DR KEGG; mpn:MPN051; -. DR PATRIC; 20021379; VBIMycPne110_0051. DR KO; K00111; -. DR OMA; WGVSKAN; -. DR OrthoDB; EOG6X9MHV; -. DR BioCyc; MPNE272634:GJ6Z-53-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 384 Uncharacterized protein MG039 homolog. FT /FTId=PRO_0000210396. FT STRAND 2 9 {ECO:0000244|PDB:4X9M}. FT HELIX 13 22 {ECO:0000244|PDB:4X9M}. FT STRAND 25 27 {ECO:0000244|PDB:4X9M}. FT STRAND 29 32 {ECO:0000244|PDB:4X9M}. FT STRAND 34 39 {ECO:0000244|PDB:4X9M}. FT TURN 42 44 {ECO:0000244|PDB:4X9M}. FT STRAND 53 56 {ECO:0000244|PDB:4X9M}. FT HELIX 61 75 {ECO:0000244|PDB:4X9M}. FT HELIX 77 80 {ECO:0000244|PDB:4X9M}. FT STRAND 85 87 {ECO:0000244|PDB:4X9M}. FT STRAND 90 96 {ECO:0000244|PDB:4X9M}. FT HELIX 97 112 {ECO:0000244|PDB:4X9M}. FT HELIX 117 119 {ECO:0000244|PDB:4X9M}. FT STRAND 120 124 {ECO:0000244|PDB:4X9M}. FT HELIX 125 131 {ECO:0000244|PDB:4X9M}. FT STRAND 141 145 {ECO:0000244|PDB:4X9M}. FT STRAND 149 151 {ECO:0000244|PDB:4X9M}. FT HELIX 153 166 {ECO:0000244|PDB:4X9M}. FT STRAND 170 172 {ECO:0000244|PDB:4X9M}. FT STRAND 177 182 {ECO:0000244|PDB:4X9M}. FT STRAND 188 192 {ECO:0000244|PDB:4X9M}. FT STRAND 199 207 {ECO:0000244|PDB:4X9M}. FT HELIX 210 212 {ECO:0000244|PDB:4X9M}. FT HELIX 213 219 {ECO:0000244|PDB:4X9M}. FT STRAND 227 237 {ECO:0000244|PDB:4X9M}. FT STRAND 246 251 {ECO:0000244|PDB:4X9M}. FT HELIX 253 256 {ECO:0000244|PDB:4X9M}. FT STRAND 261 264 {ECO:0000244|PDB:4X9M}. FT STRAND 270 273 {ECO:0000244|PDB:4X9M}. FT HELIX 282 284 {ECO:0000244|PDB:4X9M}. FT HELIX 292 303 {ECO:0000244|PDB:4X9M}. FT STRAND 311 323 {ECO:0000244|PDB:4X9M}. FT TURN 324 326 {ECO:0000244|PDB:4X9M}. FT STRAND 330 334 {ECO:0000244|PDB:4X9M}. FT STRAND 337 344 {ECO:0000244|PDB:4X9M}. FT HELIX 350 364 {ECO:0000244|PDB:4X9M}. SQ SEQUENCE 384 AA; 42724 MW; DA3E128719EE1BCD CRC64; METRDVLIVG GGVIGCATAY ELSQYKLKVT LVEKHHYLAQ ETSHANSGVI HTGIDPNPHK LTAKYNILGK KLWLNTYFKR LGFPRQKIRT LIVAFNEMER EQLEVLKQRG IANQINLEDI QMLSKEETLK LEPYVNPEIV AGLKIEGSWA IDPVLASKCL ALAAQQNKVQ ICTNTEVTNI SKQVDGTYLV WTNNETTPSF KVKKIIDAAG HYADYLAHLA KADDFEQTTR RGQYVVVTNQ GELHLNSMVF MVPTIHGKGV IVSPMLDGNF LVGPTALDGV DKEATRYITK DAPCMLTKIG KHMVPSLNIN NALISFAGSR PIDKATNDFI IRVAHNDPDF VILGGMKSPG LTAAPAIVRE AVRLLNWKLT KKPNWNGKYN LPWI // ID Y052_MYCPN Reviewed; 657 AA. AC P75062; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Uncharacterized lipoprotein MG040 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_052; ORFNames=D09_orf657, MP102; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: To T.pallidum TmpC. {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; U00089; AAB95750.1; -; Genomic_DNA. DR PIR; S73428; S73428. DR RefSeq; NP_109740.1; NC_000912.1. DR RefSeq; WP_010874409.1; NC_000912.1. DR ProteinModelPortal; P75062; -. DR EnsemblBacteria; AAB95750; AAB95750; MPN_052. DR GeneID; 876850; -. DR KEGG; mpn:MPN052; -. DR PATRIC; 20021381; VBIMycPne110_0052. DR OMA; NGLWKRP; -. DR OrthoDB; EOG6H7FCZ; -. DR BioCyc; MPNE272634:GJ6Z-54-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR003760; Bmp. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 657 Uncharacterized lipoprotein MG040 FT homolog. FT /FTId=PRO_0000014023. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 657 AA; 71672 MW; 6147B1A5673606A9 CRC64; MFGKGLVKKS LLFFSGVSTM AVFLVSCGAT RIWESSIQLL VSNDEATLAD KSFSEMSYEG IRRYFRSQKH IELPSPNSSL LQDGNGLWKR PGRTLSDRIA TFKNIKNDGS DVIVATGFNQ QEALQAISSD DRRYLADKND LAKVGFIFVD GQIEKEYNVI NKTPQFRSTP LNISSVAFRS DDGSFLTGVA TAVYLNLNQD YFLKKNGATN NSSQDLTVSG FVGVPIPSTL SFLNGFRLGI AYFNEVIYTH LSDAETTSDN KSNSSSASNS VLVQLKQMQG NDKKIKKIKW ISPKQGSDNN SNLSIDDHKS GSFSSTEPRA TTIINNLLDK GVSAIIPVAG PQVNLAVNEV ARRKAHTAII GVDSAQELLD INQDAPDKDQ LIKGNKKIIP FSSIKALDVA IENMLIAIQK GSDNNGYKGF GYNNIGTVGT SSVGISEAGY EFLIDPVFWK TTQSQGKSMA TNMTNLKRLS SDDTNTKKAL KEVSTHKNGS DKDGIIGKYS NLLTKKSTTV TAVAQKSMTD NNSGTEQKKN LSEVDTKKKE KESKGKTQSN GQDSGQQNGK ETNDIISKYS KLLTMTTMNN KVMSSKKQSS DDNSFKKTSE NGDWVIKGDE LTKKKSTELP AFAKGADYPT FPTEAVSVIN GSTALDGKGF KWSFKQI // ID Y077_MYCPN Reviewed; 546 AA. AC P75040; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 2. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MG061 homolog 2; GN OrderedLocusNames=MPN_077; ORFNames=MP078, R02_orf469; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP SEQUENCE REVISION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34737.1; -; Genomic_DNA. DR PIR; S73404; S73404. DR RefSeq; NP_109765.1; NC_000912.1. DR RefSeq; WP_010874434.1; NC_000912.1. DR ProteinModelPortal; P75040; -. DR EnsemblBacteria; AAG34737; AAG34737; MPN_077. DR GeneID; 876753; -. DR KEGG; mpn:MPN077; -. DR PATRIC; 20021433; VBIMycPne110_0078. DR OMA; WSISYLI; -. DR OrthoDB; EOG6TTVJZ; -. DR BioCyc; MPNE272634:GJ6Z-79-MONOMER; -. DR Proteomes; UP000000808; 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; IPR020846; MFS_dom. DR InterPro; IPR011699; MFS_Mycoplasma. DR Pfam; PF07672; MFS_Mycoplasma; 1. DR SUPFAM; SSF103473; SSF103473; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 546 Uncharacterized protein MG061 homolog 2. FT /FTId=PRO_0000210406. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 248 268 Helical. {ECO:0000255}. FT TRANSMEM 305 325 Helical. {ECO:0000255}. FT TRANSMEM 344 364 Helical. {ECO:0000255}. FT TRANSMEM 377 397 Helical. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. FT TRANSMEM 442 462 Helical. {ECO:0000255}. FT TRANSMEM 485 505 Helical. {ECO:0000255}. SQ SEQUENCE 546 AA; 60148 MW; 7238E3F1E51468D3 CRC64; MWGLVLLGYV LFVIEWFVID FIRGSAASLL TEQTSAVPQY GGWFSSFFVA DAGFIPGQAT NWTITLLRAV GSILCGVMVV KFGYRHAVMI MMGLMCVCFP FLIIGSPLGG HNELTLLRPA SSEVISKLTK ISSSLQQGQL LGPVQVGSQT MLADGTPVSL IKGINGNEIG TSASMTGYAF FIIFRSTIAI GGTTLIAYAQ PIIASLSSNR KKSILSNANF WGFNVGLVIV AAPFLIPGVG RFATANWVWV VTFMILLVFA MLLVFAWFEK KVDHMLPQKQ SKTNQSLSVR PSALSILKRK TTWKLLAIAG VGTILLINPL TQTWFNSLLA ISGAKKAIIP TARPILLILW VMGYLLGYFL LSPFNKTIYD KKRWLHFIFT ANAVLVLLIV IFAATLGLNT VVGFTFVGIF TFIAGGFGWS LGSSILILPY EYKEYKRNEV SIIFGYVWGF AYVFYSIFDI ITSVFLDAPR IATGNTSANI LPGAIAAIVL FVSLLLVINW VIIYLPSSWI KNGDECVSEM TKKWRITQWQ FLIANKAKNR YADLLK // ID Y012_MYCPN Reviewed; 235 AA. AC P75101; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 69. DE RecName: Full=Uncharacterized protein MPN_012; DE Flags: Precursor; GN OrderedLocusNames=MPN_012; ORFNames=D12_orf235, MP142; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95790.1; -; Genomic_DNA. DR PIR; S73468; S73468. DR RefSeq; NP_109700.1; NC_000912.1. DR RefSeq; WP_010874369.1; NC_000912.1. DR EnsemblBacteria; AAB95790; AAB95790; MPN_012. DR GeneID; 877415; -. DR KEGG; mpn:MPN012; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-12-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 235 Uncharacterized protein MPN_012. FT /FTId=PRO_0000014054. SQ SEQUENCE 235 AA; 26907 MW; C3B547E002DF4851 CRC64; MKFKYLSIPF LSSTLLFSAY ASIQSDLRNL IQETTKQDVD VYKVIKTSEG RKNLITSLKK SYEVNPDKTT KLLLDAWKQS AEKGEIDIEK INFPDVGIYA TGNDPLKIEL KVEYFDMEYQ DLNNFSINAK LNYNFNWHGN YSSNGFAAKK GDKHVFDLPL AIKPSSKNQS KTISFITKTG EGVDTEWIEF PVSLSWSLQG KINKVKEILR KSFWKAMILE QILNTQLISL DTCFS // ID Y014_MYCPN Reviewed; 212 AA. AC P75099; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MG010 homolog; GN OrderedLocusNames=MPN_014; ORFNames=D12_orf212, MP140; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|PROSITE- CC ProRule:PRU00995}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95788.1; -; Genomic_DNA. DR PIR; S73466; S73466. DR RefSeq; NP_109702.1; NC_000912.1. DR RefSeq; WP_010874371.1; NC_000912.1. DR ProteinModelPortal; P75099; -. DR IntAct; P75099; 2. DR EnsemblBacteria; AAB95788; AAB95788; MPN_014. DR GeneID; 876726; -. DR KEGG; mpn:MPN014; -. DR PATRIC; 20021299; VBIMycPne110_0013. DR KO; K02316; -. DR OMA; YLVEGDF; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; MPNE272634:GJ6Z-14-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004611; DNA_primase-rel. DR InterPro; IPR006171; Toprim_domain. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR00646; MG010; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 212 Uncharacterized protein MG010 homolog. FT /FTId=PRO_0000180535. FT DOMAIN 105 187 Toprim. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. SQ SEQUENCE 212 AA; 24497 MW; 24F971B162DEC2C3 CRC64; MELRNTKLEQ LFYIYHRNLK YRCPMQYLTK RGFNLQDLLS VGGGLAYLGE KQWLNLSLYN FNNQLVGFLS RKVGFEKKFL YLPINKPPSK SESFLGLKHL PTETNTIYLV EGDFDWLAFR KGGILNCLPL CGLTLSDKQM KFFQQSKIEK VVLCLDNDFA GKVAAANLER ILKNAGFQVK VVQLKGKVKD WNELLLLYPK NWAKALRDHL AL // ID Y015_MYCPN Reviewed; 285 AA. AC P75098; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG011 homolog; GN OrderedLocusNames=MPN_015; ORFNames=D12_orf285, MP139; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95787.1; -; Genomic_DNA. DR PIR; S73465; S73465. DR RefSeq; NP_109703.1; NC_000912.1. DR RefSeq; WP_010874372.1; NC_000912.1. DR ProteinModelPortal; P75098; -. DR EnsemblBacteria; AAB95787; AAB95787; MPN_015. DR GeneID; 876734; -. DR KEGG; mpn:MPN015; -. DR PATRIC; 20021301; VBIMycPne110_0014. DR OMA; VEYRAYI; -. DR OrthoDB; EOG6N9493; -. DR BioCyc; MPNE272634:GJ6Z-15-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003824; F:catalytic 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 InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR Pfam; PF08443; RimK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 285 Uncharacterized protein MG011 homolog. FT /FTId=PRO_0000210386. FT DOMAIN 107 285 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. SQ SEQUENCE 285 AA; 33446 MW; 1D0F653B3EA5049F CRC64; MAKIKLKNRK ALVVYNKTDF DKNKHFAQAL VDELNKKKLV GHILLLDDET ADHKHIKNVE LIINRSRRID FLTKHNFLNS FLINPQNIVL VANDKYETYR WLKQHKFLTV DTTIFDPKKI KTFPIVIKKR DSYGGEDVHL IQNAEEIKQL PIQNPNEWIV QPFLSIGKVE YRAYILFGKV LKTIRRTASG DDFRANYSQN AAVDLFKLKW YIKHKIKRIA KKLGHGYYAI DFFLNKYNRI VVNEIEDAAG ARALTKMCPD LNLPRVIIKS SLTHFKHHLK RQMIP // ID Y019_MYCPN Reviewed; 634 AA. AC P75094; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Putative ABC transporter ATP-binding protein MG015 homolog; GN OrderedLocusNames=MPN_019; ORFNames=D12_orf634, MP135; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95783.1; -; Genomic_DNA. DR PIR; S73461; S73461. DR RefSeq; NP_109707.1; NC_000912.1. DR RefSeq; WP_010874376.1; NC_000912.1. DR ProteinModelPortal; P75094; -. DR EnsemblBacteria; AAB95783; AAB95783; MPN_019. DR GeneID; 877382; -. DR KEGG; mpn:MPN019; -. DR PATRIC; 20021313; VBIMycPne110_0018. DR KO; K06147; -. DR OMA; ANANNDM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-21-MONOMER; -. DR Proteomes; UP000000808; 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: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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 634 Putative ABC transporter ATP-binding FT protein MG015 homolog. FT /FTId=PRO_0000093238. FT TRANSMEM 54 74 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 111 131 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 189 209 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 213 233 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 296 316 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 325 345 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 54 364 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 397 631 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 430 437 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 634 AA; 71147 MW; E10CE07E0EB8D406 CRC64; MLSSCRAVTS MSRWSKHKKT KEVISMLSHN QKPNSWKILW RLIKSVQGRT SSKVLYVMVC AIFGILTGVT NSILLAQGLG FIFPTTNTET DGIQSVYLLV FAHNLPVMER LTIVCVTVVV AYILIFSFNV AQNYLGLKLY QEICALLRWK AYLKIQSMST SFFDTQNNGD LMSRLTNDVY NINNLYAQVG GQTIQSLFIL MTTATILFVL SPVIALISLT VLIALIALSF LFLKKARAAY AKVQNNLGDM SGYIEEVLSN HKVVHVLKLQ EVMIDNFDKY NRPMVNPTIK ANTYAVFIYS WFGFISNITY LASISIATAF SVNNIPSFGV SAINYSFMLS YIAALRQTAL PLNQIFSLWN LIQLGIVSGE RVFKILDLES PQKQATITKL PNIKGNIRFE KVVFGYSADK PILTGIDFSV KHGDIVAIVG PTGAGKSTII NLLMKFYKPF AGKIYMDNFE ISEVSETAWR EKISIVLQDP FLFSGTIKEN IRMGRQDATD EEIIEACKVA NAHDFIMRLP QGYNTFISNK TDYLSVGERQ LLTIARAVIR NAPVLLLDEA TSSIDVHSEK LIQQSIGRLM KDKTSFIISH RLSIIRNATL IIVINDGKVL EMGNHEQLMR QNGFYARLKR SAVK // ID Y031_MYCPN Reviewed; 203 AA. AC P75083; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MG028 homolog; GN OrderedLocusNames=MPN_031; ORFNames=B01_orf203, MP123; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95771.1; -; Genomic_DNA. DR PIR; S73449; S73449. DR RefSeq; NP_109719.1; NC_000912.1. DR RefSeq; WP_010874388.1; NC_000912.1. DR EnsemblBacteria; AAB95771; AAB95771; MPN_031. DR GeneID; 876900; -. DR KEGG; mpn:MPN031; -. DR PATRIC; 20021337; VBIMycPne110_0030. DR OMA; ISIGMSK; -. DR OrthoDB; EOG62RSFG; -. DR BioCyc; MPNE272634:GJ6Z-33-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 203 Uncharacterized protein MG028 homolog. FT /FTId=PRO_0000210392. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. SQ SEQUENCE 203 AA; 23002 MW; 944D12A6529B1115 CRC64; MRRNWREHYN VFVANLALVL GFMLNIVVAR YTLTGATPQA RFLFLTPFLG IVAASIFYFF DVKWFLADYP YKKFHFQKKW TWTYLSGVFV FFANILVNVI LLALLVNQMT NQILSEKYTG LLDNAYPLLW SAVGVSIFLS LISIGLSKTA HFKIDVEMLK AKKGEPTAAD KTDSRPVVVD LDQTKSKKDG DNPPQASGDM TSL // ID Y058_MYCPN Reviewed; 485 AA. AC P75056; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized lipoprotein MG045 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_058; ORFNames=D09_orf485, MP096; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95744.1; -; Genomic_DNA. DR PIR; S73422; S73422. DR RefSeq; NP_109746.1; NC_000912.1. DR RefSeq; WP_010874415.1; NC_000912.1. DR ProteinModelPortal; P75056; -. DR EnsemblBacteria; AAB95744; AAB95744; MPN_058. DR GeneID; 877332; -. DR KEGG; mpn:MPN058; -. DR PATRIC; 20021393; VBIMycPne110_0058. DR KO; K11069; -. DR OMA; HEVEISD; -. DR OrthoDB; EOG6S7XQ8; -. DR BioCyc; MPNE272634:GJ6Z-60-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR000044; Uncharacterised_lipoprot_MG045. DR PRINTS; PR00905; MG045FAMILY. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 485 Uncharacterized lipoprotein MG045 FT homolog. FT /FTId=PRO_0000014025. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 485 AA; 55020 MW; 1AD4E0AB211B64F8 CRC64; MKKQLKYWFS LMGLTMSVGL TACSSNQFVF ANFESYVSPL LLERAEAKQP MTFLTYPTNE KLINGFANNT YTVAVASSYA VSELQQQGHL LPIDWAKFNL KKTQNGSNQA TIQNKEDAKE LFTKEIGDIS GELLNWGVPY FLQDLVFVYR GEKIQELEGQ DVTWSTIIKA IVNHKDRFNN NRLALIDDAR TIFSLANVVH HEVKNTTVDV NPTGSTLNYF GNVYESFANL GLKRDNLNTL FVNSDSNIII NELANGRRQG GIVYNGDAVY AALGGDLRDE INENNLPNGD NFHIVQPKHS PVALDFLIIN QQQTHFRDAA HQLIYQLALE GADQTAEELL KTDEEKGTSD EDYYTYGAMQ NFSYVNYVSP LKNISDETTG IVFKENKQAD TKQVVKQQSQ SEQQSESAEK EETEQDDFYT ATLKSLLKAD SLDDKAKKLV DTIKKTYKIK KADNINWANL IEKPITPLQR SNLTLSWLDF KQRFW // ID Y086_MYCPN Reviewed; 105 AA. AC P75607; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 65. DE RecName: Full=Uncharacterized protein MPN_086; GN OrderedLocusNames=MPN_086; ORFNames=MP069, R02_orf105; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95717.1; -; Genomic_DNA. DR PIR; S73395; S73395. DR RefSeq; NP_109774.1; NC_000912.1. DR RefSeq; WP_010874443.1; NC_000912.1. DR EnsemblBacteria; AAB95717; AAB95717; MPN_086. DR GeneID; 877123; -. DR KEGG; mpn:MPN086; -. DR BioCyc; MPNE272634:GJ6Z-89-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 105 Uncharacterized protein MPN_086. FT /FTId=PRO_0000210637. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. SQ SEQUENCE 105 AA; 12074 MW; 66E0FFB6823D3405 CRC64; MESALNQEFQ IDFCVKNKKL LKILANVLIA SWLSFVVFLI LGCIAIDLFR FDLYSQFFFN HLSTLSALAW TFFVLAILFG AATLAINGFF YKEIRKKSAF KEDSK // ID Y095_MYCPN Reviewed; 254 AA. AC P75597; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein MPN_095; GN OrderedLocusNames=MPN_095; ORFNames=MP059, R02_orf254; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_308 N-terminal region. 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; U00089; AAB95707.1; -; Genomic_DNA. DR PIR; S73385; S73385. DR RefSeq; NP_109783.1; NC_000912.1. DR RefSeq; WP_010874452.1; NC_000912.1. DR ProteinModelPortal; P75597; -. DR IntAct; P75597; 2. DR EnsemblBacteria; AAB95707; AAB95707; MPN_095. DR GeneID; 876790; -. DR KEGG; mpn:MPN095; -. DR PATRIC; 20021477; VBIMycPne110_0096. DR OrthoDB; EOG6G4VVV; -. DR BioCyc; MPNE272634:GJ6Z-101-MONOMER; -. DR Proteomes; UP000000808; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR Pfam; PF13520; AA_permease_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 254 Uncharacterized protein MPN_095. FT /FTId=PRO_0000210642. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. SQ SEQUENCE 254 AA; 28425 MW; F92126629ED0D3AF CRC64; MNQQLNTTRK STAARGRMGL VGGILLVIGT CIGAGIFFKS ERVLQNMGGN TTLALLVWLM AGITVILMGL ALVEITAKAA FDDLALLSWT QKFTNNTFYK ACKRFLIWIY LPTTFFFMPL YLVQSLQDGL RGFGVANHFN TPHDWAIWMV IVLLINLWFF FTSGLSVKWT SVQNVVLLLL KVIPLIAVVI LALWLGASAE QMERQPVVPV KDFTAISPFF GWFSAMGAIF FAFDGFYVSA AAKTQLKKQK NYRK // ID Y099_MYCPN Reviewed; 347 AA. AC P75593; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Putative adhesin P1-like protein MPN_099; GN OrderedLocusNames=MPN_099; ORFNames=MP055, R02_orf347L; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95703.1; -; Genomic_DNA. DR PIR; S73381; S73381. DR IntAct; P75593; 1. DR EnsemblBacteria; AAB95703; AAB95703; MPN_099. DR PATRIC; 20021489; VBIMycPne110_0102. DR BioCyc; MPNE272634:GJ6Z-105-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 347 Putative adhesin P1-like protein MPN_099. FT /FTId=PRO_0000210706. SQ SEQUENCE 347 AA; 37101 MW; 55CBC03BCAFA98D2 CRC64; MLGSIPVLVN RSGSDSNKFQ ATDQKWSYTD LQSDQTKLNL SAYGEVNGLL NPALVETYFG TTRTSSTANQ NSTTVPGIGF KIPEQNNDSK ATLITPGLAW TPQDVGNLVV SGTTVSFQLG GWLVTFTDFV KPRAGYLGLQ LSGLNASDSD QRELIWAPRP WAAFRGSWVN RLGRVESVWD LKGVWADQAQ LAAQAATSST TTTATGATLP EHPNALAYQI SYTDKDSYKA STQGSGQTNS QNNSLYLHLI KPKKVESTTQ LDQGLKNLLD PNQVRTKLRQ SFGTDHSTQP QPQSLKTTTP VFGAMSGNLG SVLSGGGAGG AGSTNSVDLS PVERVSGSLT INRNFSY // ID Y113_MYCPN Reviewed; 223 AA. AC P75449; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MPN_113; GN OrderedLocusNames=MPN_113; ORFNames=C09_orf223, MP041; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95689.1; -; Genomic_DNA. DR PIR; S73367; S73367. DR ProteinModelPortal; P75449; -. DR EnsemblBacteria; AAB95689; AAB95689; MPN_113. DR PATRIC; 20021525; VBIMycPne110_0120. DR OrthoDB; EOG6W71WS; -. DR BioCyc; MPNE272634:GJ6Z-119-MONOMER; -. DR Proteomes; UP000000808; 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; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 223 Uncharacterized protein MPN_113. FT /FTId=PRO_0000210650. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. SQ SEQUENCE 223 AA; 24406 MW; 4066156893CE018C CRC64; MNVYQTIANF GTNILESLGL EAALSPTLSN TYIYGIPVLG AIFSGLITKK LTKSTAKSLI VQALFVILGT LAFLVITLAS PAKPETGAFN QATLWIAFVV ICFIMFFIGA NRSIFWSTIT ELKVNKEIVG LAVGFISIIG FSKDVWLSPL LTGTTNQFIV KNSQGTSFYS QQALVAWAIF ALINACLALL VTYMIVRKVK YGKVWVNPKF KKVFALGEQQ YGH // ID Y013_MYCPN Reviewed; 257 AA. AC P75100; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=UPF0134 protein MPN_013; GN OrderedLocusNames=MPN_013; ORFNames=D12_orf257, MP141; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2261205, EBI-2261205; CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95789.1; -; Genomic_DNA. DR PIR; S73467; S73467. DR RefSeq; NP_109701.1; NC_000912.1. DR RefSeq; WP_010874370.1; NC_000912.1. DR ProteinModelPortal; P75100; -. DR EnsemblBacteria; AAB95789; AAB95789; MPN_013. DR GeneID; 876722; -. DR KEGG; mpn:MPN013; -. DR PATRIC; 20021297; VBIMycPne110_0012. DR OMA; VSEGPKE; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; MPNE272634:GJ6Z-13-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 2. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 257 UPF0134 protein MPN_013. FT /FTId=PRO_0000221591. SQ SEQUENCE 257 AA; 29144 MW; 1DDFEAA5626B093F CRC64; MPKVISQKEF NILSRTKERV NFQIVYTKQR NGLHKAAKEY FFKDKDFTII EDTPDTPDQP DGPCITKGPK EPGGPEEPNG PDKPEDPKDP DTPDVSEGPK EQGGQKDPGG PDDPSEGKQK VSKPDKYVTH RELDEKLKDF ATKADFKRVE DKVDVLFELQ KTQGEQIKVQ GEQIKAQGKQ IEQLTETVKV QGEQIRAQGE QIKAQSEEIK EIKVEQKAQG EQIKELQVEQ KAQGKTLQLI LKTLEKMNER LEKLESK // ID Y018_MYCPN Reviewed; 623 AA. AC P75095; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Putative ABC transporter ATP-binding protein MG014 homolog; GN OrderedLocusNames=MPN_018; ORFNames=D12_orf623, MP136; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95784.1; -; Genomic_DNA. DR PIR; S73462; S73462. DR RefSeq; NP_109706.1; NC_000912.1. DR RefSeq; WP_010874375.1; NC_000912.1. DR ProteinModelPortal; P75095; -. DR EnsemblBacteria; AAB95784; AAB95784; MPN_018. DR GeneID; 876861; -. DR KEGG; mpn:MPN018; -. DR PATRIC; 20021311; VBIMycPne110_0017. DR KO; K06147; -. DR OMA; SYMAIYL; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-20-MONOMER; -. DR Proteomes; UP000000808; 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: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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 623 Putative ABC transporter ATP-binding FT protein MG014 homolog. FT /FTId=PRO_0000093236. FT TRANSMEM 27 47 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 86 106 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 157 177 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 180 200 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 266 286 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 307 327 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 16 325 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 365 611 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 400 407 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 623 AA; 68928 MW; AB0D481D8AEF736B CRC64; MGLVLKQFNR KIRTALILAP LFTFAQIIID LIIPSFLASA IAVVFSIVTL KQKEASGEGV AVDFIAESKL SFQSVQEAQI VLATSVILLA LFGLVFGLIS IFCASIVAGN TSYFLRRKIF RKIMHITAPS HDQYGSSTLL VRLTNDVYLM EIMTFDFLRL IVRAPFLFIG GLAFAIATNS DMSISLAITF PLTFLVIGIL NKKSTPLFKN NQKSVDQINE RVEEDVSGYK VVQSFNLKDT ECLKFKAANA RWTKSSTNSL FVNTLNIPFT FFFSSMTIII ALLLVFQLDN SVRVDPLPDN AAIRPSIFAF FQYNFYIVLG LILTSLTMVN FTRSRVALGR IKDVLNKPEI QQHVVPDQTV LAPSLEFKNV AFGLGNKENR DFLQDLNFKF EAGKTYGIVG PTGSGKSLIA NIIGGLYEPN QGEIFVGGQS IKTIDSDYLA KMIGIVFQQN ILFKGTIASN IKIGLETRED WKHEPDSKKD AAMKRAAAIA CADTFIEKFS DTYDHTVEQL GKNLSGGQKQ RVAIARTVIT KPQILVLDDS MSALDALTEK KVRENIANEL PGTTKIIISQ NINSIKYAHK IMVIDNGRIA GFDSDAKLMQ SCDIYVKMKQ AQKDQGGDFD AVA // ID Y039_MYCPN Reviewed; 338 AA. AC P75075; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MPN_039; GN OrderedLocusNames=MPN_039; ORFNames=B01_orf338, MP115; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95763.1; -; Genomic_DNA. DR PIR; S73441; S73441. DR EnsemblBacteria; AAB95763; AAB95763; MPN_039. DR PATRIC; 20021355; VBIMycPne110_0039. DR OMA; AIHEGSF; -. DR BioCyc; MPNE272634:GJ6Z-41-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 338 Uncharacterized protein MPN_039. FT /FTId=PRO_0000215249. SQ SEQUENCE 338 AA; 38899 MW; D9D1ABD51BBC67B1 CRC64; MTKLPKLLLG LTFSVSLIPF SSLLITSTDV NKQPVPTALQ RTGASAIHEG SFQTITLGQS LMEQIEQLQQ FTPAQRFTQF KKKFPNQKLL SQSELSPVDV YNFLSGWQDA LVSFLDRVIK LQGKVKEANE IFNPNVGDQI VLPKKENPNV LEVLGEYNGF GFFPTLGKNG LNLPQQIFEN FTDFKVESYQ INDFKVSLVG ERDIIKNDKV RFSYAVQIPL NLELLVNNQK VTFNITVDLR TNNFSTQETF NDLFNNGTAP TNWQFFSRIK VNKLHYDQTD ATHLANTLLQ DQFNALNLDL QKSIYDLNLD DLEERFEEEY AKPLREKRTQ QKKEWEEE // ID Y080_MYCPN Reviewed; 1386 AA. AC P75613; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized ABC transporter permease MG064 homolog; GN OrderedLocusNames=MPN_080; ORFNames=MP075, R02_orf1386; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95723.1; -; Genomic_DNA. DR PIR; S73401; S73401. DR RefSeq; NP_109768.1; NC_000912.1. DR RefSeq; WP_010874437.1; NC_000912.1. DR ProteinModelPortal; P75613; -. DR EnsemblBacteria; AAB95723; AAB95723; MPN_080. DR GeneID; 877100; -. DR KEGG; mpn:MPN080; -. DR PATRIC; 20021443; VBIMycPne110_0082. DR KO; K02004; -. DR OMA; ITPDFMY; -. DR OrthoDB; EOG6NWBKC; -. DR BioCyc; MPNE272634:GJ6Z-83-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR Pfam; PF02687; FtsX; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1386 Uncharacterized ABC transporter permease FT MG064 homolog. FT /FTId=PRO_0000210408. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 402 422 Helical. {ECO:0000255}. FT TRANSMEM 494 514 Helical. {ECO:0000255}. FT TRANSMEM 518 538 Helical. {ECO:0000255}. FT TRANSMEM 563 583 Helical. {ECO:0000255}. FT TRANSMEM 592 612 Helical. {ECO:0000255}. FT TRANSMEM 613 633 Helical. {ECO:0000255}. FT TRANSMEM 682 702 Helical. {ECO:0000255}. FT TRANSMEM 1261 1281 Helical. {ECO:0000255}. FT TRANSMEM 1310 1330 Helical. {ECO:0000255}. FT TRANSMEM 1349 1369 Helical. {ECO:0000255}. SQ SEQUENCE 1386 AA; 154871 MW; 2460EFA53137433A CRC64; MRNLIKNVFR SFRTAKIALI ALTFLIFVAV GSFVLLNNTV NNFNASFQHV TEQGQLSNAI INERYDFGKL EFQKTSNDAT SSAQPSVSTR STLTAQKANG ANSSFTLTLT PDSRTSFINN ALQLKPDVYN SLVTVTFSYG SESDQTKKTQ IEEQSKLIAA NNLSRALQTD KELLVTGQLE QLKATFRTYK AINITDQGVF KKLIASEPTD QVNRLVLFDG HQLARSRQVE FNELFSQFTQ VQAKGKDQLS TTLKNGNYEQ LLQAIANNFG SSETELLKEI QDALKQTNSS TTLAQTQSSQ QFSKLKNLFD SGSTFTNIAG KLTLQWMEGT NKKQLVIFDP SSYETVVAPG NWSYEQQQGK AVYQDINHWN RIKRLPFNEF EREFQKIDKR YKMLVDKIEY LILGVGITPD FVYPVFSESL LIPNTANEQL YYVNQTGYER TASSFLTNPT ETGIVARLPN LNHDLDVINQ WAVKNMSWPP NLKAAYSNTD TTNILNLLAA RTVFIPNLIN TISLVSSFLT IAILLVAIFV TILILVSYLK KNTEQIGILK ANGVSGRKIN LSLLIFSLIP GIVGSFIGYT LGISMQNVAI NLFSNYWFIP TQTSSFSVLG LLFFALLVVL MMSGISLFVG WLILRQDVVK ILKHDSEFKV SHLGLWAKWL FAKFGIMTRF RVALAFNAPW KLVFLTLMSA LTMMILNLSF ATKDAFQVAQ TKTTLTQSNH QYEFELASPT EQSGLLKWQL FAELGATDDR TTDAVKLANR RMEIQSVDES KKWKNQQVIN FVTDATGFSN DINYLENIVQ SKIGLDYSLG FGNVSSNPWK LSETLMPANQ ASASNTAFQN FLKAIIVIDP NEGGKYIKQT KDEVTVRFLY EIDSSKALKN GNTKSVNKIQ KSTAAPQAQQ GQSNQLMLDN DFAKFLYKQF NLIKEGGKAD PVDLNNFDFA NQNQIKRFYS KYNALPPVDY KLAFNVIGLP KETIANQKDA PLFGFLTLQA QLGNDAIKIK GIKDWKLDNT NLGPVLRTNE DEIINQRLFS KPNGIIINSS AAKKYRLKEG SQLHVKIHNG YKRVNAKLVN QDPTLTATFN IVGINNSVHE PEFYTSYKTA ATLLQYPNEW IEKQLPFNSF YANSILPFTQ STSLFSESGL FPGTSSFAAN NTVLTEVIKK TIEGGKTNSK TDVQKRAAQA TANGKYNSSQ NNKMNYERLQ KALGITSDLD SSKAGEYATI LERVYDGLPY NSTISFISNV QANDALFANI ANTTQQIQTA AIGIIIPIIM LIVLLVSTTL IQELKKIAIR LKALGYSNPK ILLSFLSIYL PLFIFGLLIS IPISIYLIAL HNQVIFSSAA ILLEATLNFP TVILSMLVLS GVLSITFVLN WLELNKIKIA KEIKNS // ID Y109_MYCPN Reviewed; 165 AA. AC P75453; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 56. DE RecName: Full=Uncharacterized protein MPN_109; GN OrderedLocusNames=MPN_109; ORFNames=C09_orf165, MP045; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95693.1; -; Genomic_DNA. DR PIR; S73371; S73371. DR RefSeq; NP_109797.1; NC_000912.1. DR RefSeq; WP_010874466.1; NC_000912.1. DR EnsemblBacteria; AAB95693; AAB95693; MPN_109. DR GeneID; 877222; -. DR KEGG; mpn:MPN109; -. DR PATRIC; 20021515; VBIMycPne110_0115. DR BioCyc; MPNE272634:GJ6Z-115-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 165 Uncharacterized protein MPN_109. FT /FTId=PRO_0000210647. SQ SEQUENCE 165 AA; 19820 MW; 4B8DB2142A13C1A9 CRC64; MKFKLNFHEK INQKDCWQSL IDHKERSYSL DFVNNTEKEL PLIYGYEVKD FENHGVKIGY TTCKPSDKIQ SAIEERILSQ EKEFRFLDEN IEKIEEVKVI FWAIAINEKD ESFKDYSLHS FIKEKNLLKE SQAGGEWFIV DENKDKFEYL SQIFRQFRAP SLFKK // ID Y110_MYCPN Reviewed; 718 AA. AC P75452; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 68. DE RecName: Full=Uncharacterized protein MPN_110; GN OrderedLocusNames=MPN_110; ORFNames=C09_orf718, MP044; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95692.1; -; Genomic_DNA. DR PIR; S73370; S73370. DR RefSeq; NP_109798.1; NC_000912.1. DR RefSeq; WP_010874467.1; NC_000912.1. DR EnsemblBacteria; AAB95692; AAB95692; MPN_110. DR GeneID; 877363; -. DR KEGG; mpn:MPN110; -. DR PATRIC; 20021517; VBIMycPne110_0116. DR OrthoDB; EOG6RC3KH; -. DR BioCyc; MPNE272634:GJ6Z-116-MONOMER; -. DR Proteomes; UP000000808; Chromosome. 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; IPR027417; P-loop_NTPase. DR Pfam; PF04851; ResIII; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 718 Uncharacterized protein MPN_110. FT /FTId=PRO_0000210648. SQ SEQUENCE 718 AA; 84850 MW; 3201D642E00E0754 CRC64; MKIRISLNIL AKFLDSFAHL LFLKNKEIYT PRKEQAACVE VLERYFQANP ENGRFLMNCK MRFGKCFTLY SYAQKNNINK ILILTFVPAV EESLKDDLNH IEKNYKFYTD DDLQKSNFDL KNQNEPYVVF LSLQNVLGKQ RIDGAKTDFD KERISKLQEI DFDLIVFDEY HYGANKKRTQ IKVEKVNKKI DNPEQQDNQD DAEEELASTF KLKDIKSKFQ FSYKQLVCLS GTPFSSLRNN EFSSKDQVFT YSYFDEQKAK SAENHPLKLG QYGIFPEMNI YCFELAEIFT AQEQEIFITP GKGKNKLPEI SFRKLFQTEN VSKESSKPVY RFVNENLVEK LIDSLIDKRK GFSHTPLSWE NIDKHKHSLL ILPTRVACFA LANLLKNHWY FENNDFQIIN MSESQFGNGK KALIELNKHL DEAKKTNKNT LTITVAKLTI GITVKEWSTV FFLKDLKGAE SYFQTIFRIQ TPYIKNCKNL KEICYVYDFN MYRCLEVTNE YSKQTQTDPK FSASWFQNLD KFLPIYLVRG DEIQKTDPEI LQKYEYFIMD KRAFSTRWMD ESNIIDIDVL CNVGQDEDAQ KILKKILAHK KFKSSKKKRE FEDVHLEKSP KSEAFSEGVR SGKDYAAEQG NVLEELENFW NFNQALEQKA KAEFQQKNFD DNEWNNYKKG FNFGVNKHFE DKVSIKKIVQ NKIKDFKKRK GRTTSTFKKW KWLYFWWE // ID Y111_MYCPN Reviewed; 422 AA. AC P75451; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized adenine-specific methylase MPN_111; DE EC=2.1.1.72; GN OrderedLocusNames=MPN_111; ORFNames=C09_orf422, MP043; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase 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; U00089; AAB95691.1; -; Genomic_DNA. DR PIR; S73369; S73369. DR RefSeq; NP_109799.1; NC_000912.1. DR RefSeq; WP_010874468.1; NC_000912.1. DR EnsemblBacteria; AAB95691; AAB95691; MPN_111. DR GeneID; 877256; -. DR KEGG; mpn:MPN111; -. DR PATRIC; 20021521; VBIMycPne110_0118. DR KO; K00571; -. DR OMA; THTEREQ; -. DR OrthoDB; EOG6HQSKB; -. DR BioCyc; MPNE272634:GJ6Z-117-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; RM_methylase_Eco57I. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF07669; Eco57I; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 422 Uncharacterized adenine-specific FT methylase MPN_111. FT /FTId=PRO_0000088017. SQ SEQUENCE 422 AA; 49062 MW; C0AB9D9E4230BA81 CRC64; MNKNSGKDYE SIQGKIKSKA EIEDSVILDQ DTFQGKGEEK TKLDELIRWE AEKNDLLKLI DNVGNDEVFT PVETCQRMLD ELFPEDHEVW SNPDLKWLNP CDKNGVFFRE IALRLDKGLT KIIPDEYARK KHIMTKMLFS IGLTKFTSLM VRRTLYYCIK ANKRKTSEDE GCAIANGARF NNEFGNVVTP YKEHYFGKES KSKNCHFCGT NKNSKYVNSM TEEKYAYDFI HLNSDEYENY FKTNFGVMKF DVIIGNPPYQ LSNGSGSDGN GAKAIFQDFV LKAIDLEPKY LAMIIPAKWM ISAENIFLNL RDKLKKNKDI KEINIFFDSK DCFPKREIKG GICYFIWQNN YQGKTLINTK FSKKGKSTEI DSSKRNLFVS VLNNTEQIIF RKRIWQDIYT KIDSISASEM KNTHTEREQF RS // ID Y114_MYCPN Reviewed; 600 AA. AC P75448; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative acetyltransferase MPN_114; DE EC=2.3.1.-; GN OrderedLocusNames=MPN_114; ORFNames=C09_orf600, MP040; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase 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; U00089; AAB95688.1; -; Genomic_DNA. DR PIR; S73366; S73366. DR RefSeq; NP_109802.1; NC_000912.1. DR RefSeq; WP_010874471.1; NC_000912.1. DR ProteinModelPortal; P75448; -. DR IntAct; P75448; 1. DR EnsemblBacteria; AAB95688; AAB95688; MPN_114. DR GeneID; 877261; -. DR KEGG; mpn:MPN114; -. DR PATRIC; 20021527; VBIMycPne110_0121. DR KO; K00624; -. DR OMA; RTECIRP; -. DR OrthoDB; EOG6TXQVQ; -. DR BioCyc; MPNE272634:GJ6Z-120-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR000542; Carn_acyl_trans. DR PANTHER; PTHR22589; PTHR22589; 1. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 600 Putative acetyltransferase MPN_114. FT /FTId=PRO_0000210177. FT REGION 396 409 Coenzyme A binding. {ECO:0000255}. FT ACT_SITE 323 323 Proton acceptor. {ECO:0000255}. SQ SEQUENCE 600 AA; 68887 MW; 4791591966AE1E4D CRC64; MDTKLTPPWL RQENNLLNPE VTQRLFINQD NIPNLPTEAP QVYLARFLEW VEPLVSKVKF VKAQAAVQDY LNSKACAQIE TIIAERAQNT HSSWLANWWV QYAYLTSTGP VSPEVNAPYY LELPTVGWSQ AELAAALSAQ LWHIYQQVQK RQLTSFSVKD KLFSLDTLQS IFASCQIHRA DGDVYFVNDQ PANFIVVIKN NVFYKLVIDN SGSLEQLQAQ LQLSFVQILD NELSHPPHWN LLTATTTKAE SQSLLDQLWA QNPEMLLDIY NSAFIVNLDN VELTTPLQLL RNSTWTPNFN RWHAKGIQLV ITKNAQLVIL ADHTSFDGSS VATLANIFVS KLQKVNTEGA SALTPTMLSF PTVDQDKQKY FKQLSKNFKD YVYNAVMFEL KWDWFTKPLI KAKGIKNSEA FIHLCYQIAQ YQTNKKLQNT YVAVDMRQYF RGRTECLRPL SKQSVAFVKR YCKDPKGTLK QFRKYYPAIE SLHFEKTRLA QKGSGVNRHL LGAYLAWNEH QDTIAKPALF ETKAWKTIAA NPLSTSSIVD KYLRNFSFDP VEPNGIGIAY AIDDTNFRAI LSVYQHNLQY LKDWMKHFEQ TVKTILKTLK // ID Y130_MYCPN Reviewed; 140 AA. AC P75345; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 64. DE RecName: Full=UPF0134 protein MPN_130; GN OrderedLocusNames=MPN_130; ORFNames=C09_orf140o, MP024; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95672.1; -; Genomic_DNA. DR PIR; S73350; S73350. DR RefSeq; NP_109818.1; NC_000912.1. DR RefSeq; WP_010874487.1; NC_000912.1. DR ProteinModelPortal; P75345; -. DR EnsemblBacteria; AAB95672; AAB95672; MPN_130. DR GeneID; 877291; -. DR KEGG; mpn:MPN130; -. DR PATRIC; 20021569; VBIMycPne110_0141. DR OrthoDB; EOG6FBWTD; -. DR BioCyc; MPNE272634:GJ6Z-137-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 UPF0134 protein MPN_130. FT /FTId=PRO_0000221597. SQ SEQUENCE 140 AA; 16543 MW; 5708B67CF2DAD3B8 CRC64; MKEKTPFKNE KEFHDMVKKT KKGTFSGWYI VNPENNSVEF SGNFNRQFKL NKPVIPVNTE YVTRKEFNEY KDSNDQRLIK IETTLAAQGE QIRIQGEQIK ELQIEQKAQS ETLKLILQTL QKMSDRLDKM DVRLDKLESK // ID Y134_MYCPN Reviewed; 586 AA. AC P75264; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Putative ABC transporter ATP-binding protein MG187 homolog; GN OrderedLocusNames=MPN_134; ORFNames=E07_orf586, MP020; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95668.1; -; Genomic_DNA. DR PIR; S73346; S73346. DR RefSeq; NP_109822.1; NC_000912.1. DR RefSeq; WP_010874491.1; NC_000912.1. DR ProteinModelPortal; P75264; -. DR IntAct; P75264; 1. DR EnsemblBacteria; AAB95668; AAB95668; MPN_134. DR GeneID; 877300; -. DR KEGG; mpn:MPN134; -. DR PATRIC; 20021583; VBIMycPne110_0148. DR KO; K10112; -. DR OMA; LANIKTE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-141-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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 Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 586 Putative ABC transporter ATP-binding FT protein MG187 homolog. FT /FTId=PRO_0000093242. FT DOMAIN 13 464 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 45 52 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 586 AA; 66464 MW; 8BAD0293B1A6A876 CRC64; MEKIQAEKSQ SAIEFKNIVV DFGESIAIDN INLTVKKKEL VTLLGPSGCG KTTSLSVIAG LIAPTSGQVL FNGYDVTKKP PQQRKLGLVF QNYALYPHMS VFENIVFPLY SDTSWREAIF EKNTWAQHDI NCLILKANGA TSEELAELNR LMQQRIDEPK RMAYQINDLM VSVFQKQSEL EANLKLIPRK KQFAIISLSK ETLSQIRDVE TKAKAALETA DSAEVEQTIK SELKQKLSEI KANYHDEKAN IKAYWWEMLA NIKTELKTEK TAIKQTNDYA KLKELKWKIH FEPLNLKKQY RSYFKQLKAK YSLKDGNLTE SELSQIEELQ KRIVSLKDFI NRTAKEVAEK LEITKILHKR PANISGGQQQ RVAIARAIVR RPKVLLMDEP LSNLDAKLRV QTRQWIRKFQ QDLQITTVFV THDQEEAMSI SDTIVCMSTG KVQQIGSPSE LYLKPANEFV ATFLGSPEMN IVNATVKAGQ LLWNENPLVK TKFDLPDGAI RVGFRYDEVT APKNDGSPVF SGTLISVENL GKHMVGVVES NGVQLNVRLE LSHQFEVGNA VKFTIKPNGL HFFDPQTTQR VEVKHV // ID Y143_MYCPN Reviewed; 175 AA. AC P75143; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=Uncharacterized protein MPN_143; GN OrderedLocusNames=MPN_143; ORFNames=E07_orf175, MP011; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95659.1; -; Genomic_DNA. DR PIR; S73337; S73337. DR RefSeq; NP_109831.1; NC_000912.1. DR RefSeq; WP_010874500.1; NC_000912.1. DR EnsemblBacteria; AAB95659; AAB95659; MPN_143. DR GeneID; 877205; -. DR KEGG; mpn:MPN143; -. DR PATRIC; 20021601; VBIMycPne110_0157. DR OMA; ELHEDNQ; -. DR BioCyc; MPNE272634:GJ6Z-150-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 175 Uncharacterized protein MPN_143. FT /FTId=PRO_0000210653. SQ SEQUENCE 175 AA; 20516 MW; 50DC773EF76335C0 CRC64; MSHKDFNGLQ APQLLSSSSP VAKKQSSHKL RHALKHARYL NHSSKRTLKH ALELHEDNQV LLEKEGSPNF QDWLSKQPGV NKTSLKYNKS LGSWISKESK PKKRFPPYFT YKGSKTTPEE AKALQQMKQS QKRFFHENMH SFLNEVAHNP MIQRFKQKQA KRAANTRQRT YKYRQ // ID Y011_MYCPN Reviewed; 231 AA. AC P75102; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 73. DE RecName: Full=Uncharacterized lipoprotein MPN_011; DE Flags: Precursor; GN OrderedLocusNames=MPN_011; ORFNames=D12_orf231, MP143; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95791.1; -; Genomic_DNA. DR PIR; S73469; S73469. DR RefSeq; NP_109699.1; NC_000912.1. DR RefSeq; WP_010874368.1; NC_000912.1. DR IntAct; P75102; 1. DR EnsemblBacteria; AAB95791; AAB95791; MPN_011. DR GeneID; 877413; -. DR KEGG; mpn:MPN011; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-11-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 231 Uncharacterized lipoprotein MPN_011. FT /FTId=PRO_0000014053. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 231 AA; 26923 MW; 400D5F2D3D2A9191 CRC64; MKFKFLLTPL LSSVLFLSAC SATFEADLKN LIKETDGKDL DVSKLIITSE GKQILIGYLK KSYEVNSEKT TELLLNAWKQ SAEKNEIGID LFNWTKSIFS GVNTFNKKQK VEYFNMTYKG ISDVSVKAKL NHTLTWNENY SYRGFNIHKG DKHYFNSFLT LKANSYLPFT SKNFDVYSKR IRLSVSFHWI LKGKDELSQK ILDKTVLNGY IEYIVDNYQI NLFRYLVYLI E // ID Y028_MYCPN Reviewed; 299 AA. AC P75086; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized glycosyltransferase MG025 homolog; DE EC=2.4.-.-; GN OrderedLocusNames=MPN_028; ORFNames=B01_orf299V, MP126; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; U00089; AAB95774.1; -; Genomic_DNA. DR PIR; S73452; S73452. DR RefSeq; NP_109716.1; NC_000912.1. DR RefSeq; WP_010874385.1; NC_000912.1. DR ProteinModelPortal; P75086; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB95774; AAB95774; MPN_028. DR GeneID; 877179; -. DR KEGG; mpn:MPN028; -. DR PATRIC; 20021331; VBIMycPne110_0027. DR OMA; PAYTWLP; -. DR OrthoDB; EOG6HXJ6D; -. DR BioCyc; MPNE272634:GJ6Z-30-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; 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 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 299 Uncharacterized glycosyltransferase MG025 FT homolog. FT /FTId=PRO_0000059242. SQ SEQUENCE 299 AA; 34936 MW; 9A3AF2F099283565 CRC64; MQFKYLFTVI IPTYNCGQYI PKALDSLLLQ GEYFTKTQVL IVNDGSTDNT KQIVEPYTQQ YSNIEYLEKP NGNWGSVVNF VKQNQLAKGQ YITVLDSDDY FLANAFQRVA AHFGHDMIVS AFYCYISPKR RRFLKPYFGK TGVIEQKTKL RTPHSQPLAK FYRHEIFHLL DPLKEKLFYQ DCLLYHNAIN KVQSVFYICE PLAVWYATRP GNSTTMPWNN ADKFQAWCDL LKQMNLYGAG IVIYIYTMLP GFLKELKRQQ LVLDLAKKPA YTWLPQPLAF LFGGLMALRT RKYIRYPKN // ID Y041_MYCPN Reviewed; 186 AA. AC P75073; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 52. DE RecName: Full=Uncharacterized protein MPN_041; GN OrderedLocusNames=MPN_041; ORFNames=B01_orf186L, MP113; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95761.1; -; Genomic_DNA. DR PIR; S73439; S73439. DR IntAct; P75073; 1. DR EnsemblBacteria; AAB95761; AAB95761; MPN_041. DR PATRIC; 20021357; VBIMycPne110_0040. DR OMA; REWGNGA; -. DR BioCyc; MPNE272634:GJ6Z-43-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR Pfam; PF03072; DUF237; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein MPN_041. FT /FTId=PRO_0000215250. SQ SEQUENCE 186 AA; 21895 MW; BCD4B226980E4CF1 CRC64; MRDAIDKYAT YSVSRLNNVT TYLPGKVDGS GKDQIWISPN NFQVNREWGN GAHFKDKAYR FNFDVKVEYD VEVKAAWWTA LFRGSIPGYW KGKFKVTYSF NGEVPSWNYG DKQVRPPQYS FKEQEKQLLF VPRHVQKIEA EGKHLEIINP FLKDQHLDFF EHYHPDLTQP LDMVSYLMYA IADKVK // ID Y091_MYCPN Reviewed; 138 AA. AC P75602; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 59. DE RecName: Full=Uncharacterized protein MPN_091; GN OrderedLocusNames=MPN_091; ORFNames=MP064, R02_orf138; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_413 and MPN_463. {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; U00089; AAB95711.1; -; Genomic_DNA. DR PIR; S73390; S73390. DR IntAct; P75602; 1. DR EnsemblBacteria; AAB95711; AAB95711; MPN_091. DR BioCyc; MPNE272634:GJ6Z-94-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Uncharacterized protein MPN_091. FT /FTId=PRO_0000210641. SQ SEQUENCE 138 AA; 15763 MW; F52380D428F42709 CRC64; MGGWMLCAPP IYTPHTNSWT ERWDRTSWWR WSAQRWSGWS FKIVRANKAL RVMAKTKMPL VLIPPSPNKP YSKLAINQEL HLIPPKKTSP ATSSSLKPRP GPRGCLNARL SWRCPTLSRK VRVPTIKVPM VRAPSTPP // ID Y092_MYCPN Reviewed; 173 AA. AC P75600; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 52. DE RecName: Full=Putative MgpC-like protein MPN_092; GN OrderedLocusNames=MPN_092; ORFNames=MP062, R02_orf173; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95710.1; -; Genomic_DNA. DR PIR; S73388; S73388. DR EnsemblBacteria; AAB95710; AAB95710; MPN_092. DR BioCyc; MPNE272634:GJ6Z-95-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 173 Putative MgpC-like protein MPN_092. FT /FTId=PRO_0000210717. SQ SEQUENCE 173 AA; 18777 MW; B31F701A125F86A4 CRC64; MVSKWGAGSA FGLQGNGSNS SGLRPLLKRT AQINLRQTQD NAQTGKFSKY LNTAQALHQM GVIVPSLETW PGKPSTGIAT RAVGGVSVQA ATRLDFYKWR SAECNNKVIP HLHVPTRLLK WPDRCDGFKR GTEFVVLGCR GGPGIGSRNL MSPHRAQLGH RQAEAVCRKP VGF // ID Y126_MYCPN Reviewed; 159 AA. AC P75349; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative metallophosphoesterase MG207 homolog; DE EC=3.1.4.-; GN OrderedLocusNames=MPN_126; ORFNames=C09_orf159, MP028; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2260422, EBI-2260422; CC P75200:MPN_580; NbExp=1; IntAct=EBI-2260422, EBI-2260425; CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE 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; U00089; AAB95676.1; -; Genomic_DNA. DR PIR; S73354; S73354. DR RefSeq; NP_109814.1; NC_000912.1. DR RefSeq; WP_010874483.1; NC_000912.1. DR ProteinModelPortal; P75349; -. DR IntAct; P75349; 1. DR EnsemblBacteria; AAB95676; AAB95676; MPN_126. DR GeneID; 877208; -. DR KEGG; mpn:MPN126; -. DR PATRIC; 20021553; VBIMycPne110_0133. DR KO; K07095; -. DR OMA; TIANNKM; -. DR OrthoDB; EOG6D2M09; -. DR BioCyc; MPNE272634:GJ6Z-133-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR020935; PdiEstase_YfcE_CS. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. DR PROSITE; PS01269; UPF0025; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 159 Putative metallophosphoesterase MG207 FT homolog. FT /FTId=PRO_0000155610. SQ SEQUENCE 159 AA; 18339 MW; 0AE5E3D046560B3D CRC64; MTKVLVLSDT HGYNDRWLAV MKLHNPDVVI HAGDHLTTKK FMDQNATFWV AGNHDVVGEE IQMFELEGIQ FVLMHGHQAP RHDLKQWYKM LVDQAKSYLC DVLIVGHSHI EHYETIDGIQ VINPGSLEIP RNPRKLPTYC NLNLSQGRIS DLTFHFPRD // ID Y136_MYCPN Reviewed; 319 AA. AC P75262; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable ABC transporter permease protein MG189 homolog; GN OrderedLocusNames=MPN_136; ORFNames=E07_orf319, MP018; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. MalFG subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95666.1; -; Genomic_DNA. DR PIR; S73344; S73344. DR RefSeq; NP_109824.1; NC_000912.1. DR RefSeq; WP_010874493.1; NC_000912.1. DR ProteinModelPortal; P75262; -. DR EnsemblBacteria; AAB95666; AAB95666; MPN_136. DR GeneID; 877322; -. DR KEGG; mpn:MPN136; -. DR PATRIC; 20021587; VBIMycPne110_0150. DR KO; K02026; -. DR OMA; FMQRLFV; -. DR OrthoDB; EOG6GR3D7; -. DR BioCyc; MPNE272634:GJ6Z-143-MONOMER; -. DR Proteomes; UP000000808; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 319 Probable ABC transporter permease protein FT MG189 homolog. FT /FTId=PRO_0000060288. FT TRANSMEM 41 61 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 98 118 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 134 154 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 169 189 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 229 249 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 282 302 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 99 302 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 319 AA; 36677 MW; 4E63938BA6DB3D9F CRC64; MFKQSLIWYN RYVQKRKKGL DLTIKDRSWS NVLLGLIFKT VVLCFFGLMV IFPFYLMLVV ALTSDEVVLN IREPILKSDG WHFENFRRVL EDGKYLNAIW INSLVTILSI ILRLFFTVSM GYAFSLKKWK LKKLFWFIFL AVLILPESAL LIGQYRVVVV ANWNQPEKPA IILGLTMPFV ASVFSGFMFR TAFEAIPPRI KESAFVDGCT GLRYFLKIAF PMVRSTTWTV SILTAFAAWN SYLWPLLLLT NRPDLNINLW VLAQGTDGNA GQSDEQIRVL LNLKMAAAIL AILPMFIVYF LFRKRIMKAV GSRANTIKG // ID Y138_MYCPN Reviewed; 166 AA. AC P75260; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=UPF0134 protein MPN_138; GN OrderedLocusNames=MPN_138; ORFNames=E07_orf166, MP016; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95664.1; -; Genomic_DNA. DR PIR; S73342; S73342. DR RefSeq; NP_109826.1; NC_000912.1. DR RefSeq; WP_010874495.1; NC_000912.1. DR ProteinModelPortal; P75260; -. DR EnsemblBacteria; AAB95664; AAB95664; MPN_138. DR GeneID; 877272; -. DR KEGG; mpn:MPN138; -. DR PATRIC; 20021591; VBIMycPne110_0152. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-145-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 166 UPF0134 protein MPN_138. FT /FTId=PRO_0000221599. SQ SEQUENCE 166 AA; 19519 MW; BE44F5377B2FA709 CRC64; MKEKIPFYNE KEFNEMMKKT KKGTFSGWYI INPENKSVEF SGNFNRQFKL NKPVIPVNTE YVTRKEFNEY KDSNDQRLTK IENKVDKLEV KVDKLEEKVD KLEAKVDKLE EKVDKLEAKV DKLEEKVDKL EAKVDSGFEM LAKILAAINK RLDSIEGRLD KIEPPK // ID Y149_MYCPN Reviewed; 434 AA. AC P75037; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 01-APR-2015, entry version 53. DE RecName: Full=Putative MgpC-like protein MPN_149; GN OrderedLocusNames=MPN_149; ORFNames=E07_orf434, MP005; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95653.1; -; Genomic_DNA. DR PIR; S73331; S73331. DR RefSeq; NP_109837.1; NC_000912.1. DR RefSeq; WP_010874506.1; NC_000912.1. DR EnsemblBacteria; AAB95653; AAB95653; MPN_149. DR GeneID; 877331; -. DR KEGG; mpn:MPN149; -. DR PATRIC; 20021617; VBIMycPne110_0165. DR BioCyc; MPNE272634:GJ6Z-156-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 434 Putative MgpC-like protein MPN_149. FT /FTId=PRO_0000210720. SQ SEQUENCE 434 AA; 47970 MW; DE66C156B01EE11E CRC64; MAVGIFILSL NPSYELVDWK RVGDTKLVAL VRSALVRVKF NDGTSSDSNN QDTNQNALSF DTQESQKALN GSQSGSSDTS GSNSQDFASY ILIFQAAPRA TWVFERKIKL ELPYVKNESG AGDSTTTNSG SLYTTLQDLL VEQPVTPYTP NAGLARVNGA AQDTVHFGSG QESSWNSQRS QKVLKNNPGP KAVTGFKLDK GRAYRKLNEA WPVYEPLDST KDGKGKDESS WNSSEKTTAE SDAPLVGSTG SQMAAVTDSQ QSGDNNGLVS LAQRSTTVAV QKSDSSGSQG QGTTDNKFQK YLNTTQALHQ MGVIVPSLET WAGENKYWNR YPCCWWCFSP SSDPAIVFHK WRSTECNHPV IPYFNRPTRL LKWPDRCDGF ERGTEFVVLG RGWANHVRKG YLMSPHRVEL GHRQAEGVCG ESAWFQWNQR HRLA // ID Y035_MYCPN Reviewed; 666 AA. AC P75079; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MPN_035; GN OrderedLocusNames=MPN_035; ORFNames=B01_orf666, MP119; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95767.1; -; Genomic_DNA. DR PIR; S73445; S73445. DR RefSeq; NP_109723.1; NC_000912.1. DR RefSeq; WP_010874392.1; NC_000912.1. DR EnsemblBacteria; AAB95767; AAB95767; MPN_035. DR GeneID; 876857; -. DR KEGG; mpn:MPN035; -. DR PATRIC; 20021345; VBIMycPne110_0034. DR OrthoDB; EOG6Z0QJK; -. DR BioCyc; MPNE272634:GJ6Z-37-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 666 Uncharacterized protein MPN_035. FT /FTId=PRO_0000215247. SQ SEQUENCE 666 AA; 76898 MW; DF096AA4B475402D CRC64; MKAFRKLLLG LALPTTIGPL LGLLLTNTDT VKNESLTTVR HRSSINQDFD GIFHTVKLLE PIQQSNADPA ASFALFQQKF PNLKRVANST LNTFDVYNLL SGWKSSLTAY LNQVLALQQR IKAADQIFPN QKETLPKDEN PNIFEVLGAY GGKGFFPTLG SNGLHLPPQL FQFFRDFQLS SFTIKDFEVA LVSEPDIVQH DKVRYAFQVQ FNLVLQLQIN RNPVLFDFNL QLKTNNFANQ TSFDELFNEK TNPLNWQFFS KLKVNHLVYE GNDITQLANT LLQSQFNVLQ LDLNKSIYRL NLNAMAQRFE HDWVQPLYAK RTQAKIAYEA EQARIAAENK RKELERQKLL AELKAKAEHY QKIKQARENM LKGLKSITDF VKFWKSPDRL LVGFNKQDDI TTRAGVYKAL QIAYANYPQW TFYLTLQGWK NGSELLLKRP SWTNLLSDIH FQKAFNLKNT VSEQTLGAAT LPGYGYYGLR MSDWLRWALG YYSYIHMGVP QNVQTKFTGT PDNEQQVWIA NEPFEWNKHY GVGPKYKDKA YRFNMEISFE LEGWIAVKWW AWAFKGSIPG NWKGKLKVTH LFDGMVPVWE LGPVNTHLPQ YSFTDQQQLL FVPHSIQKIE AIGADKGIND LLKTQNLHNL ERLSYESTNP IDLISYLLYA IQYIKV // ID Y038_MYCPN Reviewed; 116 AA. AC P75076; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=UPF0134 protein MPN_038; GN OrderedLocusNames=MPN_038; ORFNames=B01_orf116L, MP116; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95764.1; -; Genomic_DNA. DR PIR; S73442; S73442. DR RefSeq; NP_109726.1; NC_000912.1. DR RefSeq; WP_010874395.1; NC_000912.1. DR ProteinModelPortal; P75076; -. DR SMR; P75076; 44-115. DR EnsemblBacteria; AAB95764; AAB95764; MPN_038. DR GeneID; 876755; -. DR KEGG; mpn:MPN038; -. DR PATRIC; 20021351; VBIMycPne110_0037. DR OMA; YTWEEEL; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-40-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 116 UPF0134 protein MPN_038. FT /FTId=PRO_0000221592. SQ SEQUENCE 116 AA; 13629 MW; 15A7715768B51AD9 CRC64; MFKKRLNKDK INDCYTWEEE LPDGSYDMGF HGNLNHMEKG KSGYVTHKQL DKKLEVFKQD LLVELSEKFV TKEEFRAQGK QIKELQIEQK AQGKTLQLIL EALQGINKRL DKLESK // ID Y040_MYCPN Reviewed; 103 AA. AC P75074; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 52. DE RecName: Full=Uncharacterized protein MPN_040; GN OrderedLocusNames=MPN_040; ORFNames=B01_orf103b, MP114; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95762.1; -; Genomic_DNA. DR PIR; S73440; S73440. DR IntAct; P75074; 2. DR EnsemblBacteria; AAB95762; AAB95762; MPN_040. DR BioCyc; MPNE272634:GJ6Z-42-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 103 Uncharacterized protein MPN_040. FT /FTId=PRO_0000210635. SQ SEQUENCE 103 AA; 11291 MW; 62E96884733993C6 CRC64; MSSVFSKPNL KRPSFDVKNL TKPSRLLSAT LRSSCAFLSS ASFFACSLCF FCCSSISFCS LASSSARLRY SSSHSFFCWV LFSRSGLAYS SSNLSSKSSR LRS // ID Y042_MYCPN Reviewed; 672 AA. AC P75072; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MPN_042; GN OrderedLocusNames=MPN_042; ORFNames=B01_orf672, MP112; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95760.1; -; Genomic_DNA. DR PIR; S73438; S73438. DR RefSeq; NP_109730.1; NC_000912.1. DR RefSeq; WP_010874399.1; NC_000912.1. DR ProteinModelPortal; P75072; -. DR IntAct; P75072; 4. DR EnsemblBacteria; AAB95760; AAB95760; MPN_042. DR GeneID; 877359; -. DR KEGG; mpn:MPN042; -. DR PATRIC; 20021359; VBIMycPne110_0041. DR OMA; KIWIASH; -. DR OrthoDB; EOG6Z0QJK; -. DR BioCyc; MPNE272634:GJ6Z-44-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 672 Uncharacterized protein MPN_042. FT /FTId=PRO_0000215251. SQ SEQUENCE 672 AA; 77589 MW; 1A7A593003ADB866 CRC64; MKKLHKILLG LSLPASLAPL SGFISTDADN SQFSLKKSST EIKGTQSIHL LNLGESLTEE IKEAQKRTPE TSFASFKQKF PNKESFVKGF QPIDVYNLLS GWKDAISSFL DKVVELQKKI EEANKIFNTN IGNQIDLPED ENPNVLNVLG SYGGEGFFPT LGKNGLNLPQ QIFENFTDFK VVSHKIHDFQ VSLVGERDII KNDKVRFSYA VQIPLNLELL VNNQKVTFNI TVDLRTNNFS TQETFNELFN KCIGPVNWQF FSRVKVDKLH YDQTDATHLA NTLLQDQFNA LNLDLEKSIY DLELPRLEAE FQQKYVDPLI EKKQRQKAEW EEAERIRKEE EEKHQKELEE QQRIQAEKAK NDEQLQKPQT ELKKALGGID SFVEFFTNND LRLKLGYTKE DNVRTRAGLF RALEVSFGNY RAWTFYITLL GWKDTTEKIF KKAKWQDIRD DEKFRKAFGL SPKATEKDVG KVTNPGYGYQ GIYIKDSLRD GIAKYSDSTV SEPKNVKVSL PGTVGDNEEG KIWIASHNFR QNHEWGAGEK FKYSAYRFKF DVTVDYDVEV SAKWWTWAFR GSIPGYWRGK FKVTYSFDGV VPSWKYGHIQ VRTPQYSFNK QEQKILFVPH AIQKIAAEGS NLDLINPFLK DQKLDEFEHY HPDLTKPLDL VAYLLYAITT RS // ID Y054_MYCPN Reviewed; 123 AA. AC P75060; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MPN_054; DE Flags: Precursor; GN OrderedLocusNames=MPN_054; ORFNames=D09_orf123, MP100; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95748.1; -; Genomic_DNA. DR PIR; S73426; S73426. DR RefSeq; NP_109742.1; NC_000912.1. DR RefSeq; WP_010874411.1; NC_000912.1. DR EnsemblBacteria; AAB95748; AAB95748; MPN_054. DR GeneID; 876890; -. DR KEGG; mpn:MPN054; -. DR PATRIC; 20021385; VBIMycPne110_0054. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-56-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 123 Uncharacterized lipoprotein MPN_054. FT /FTId=PRO_0000014055. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 123 AA; 14170 MW; 2780F8C46C5E1404 CRC64; MKIKYFFIPL FSSAILFSAC SSIQSDLRNL IKETTGKDFD VSKLIKTSEG RKNLINSLKK SYESKPDETA SLLLIAWKQS AEMGEIGFDD IKEGGIYTRD NDPFKLEQKV EYFNMEYKIL VMF // ID Y070_MYCPN Reviewed; 127 AA. AC P75047; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG055.2 homolog; GN OrderedLocusNames=MPN_070; ORFNames=D09_orf127a, MP085; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95733.1; -; Genomic_DNA. DR PIR; S73411; S73411. DR RefSeq; NP_109758.1; NC_000912.1. DR RefSeq; WP_010874427.1; NC_000912.1. DR EnsemblBacteria; AAB95733; AAB95733; MPN_070. DR GeneID; 877167; -. DR KEGG; mpn:MPN070; -. DR PATRIC; 20021419; VBIMycPne110_0071. DR OMA; INTACEN; -. DR OrthoDB; EOG6RZBD3; -. DR BioCyc; MPNE272634:GJ6Z-72-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 127 Uncharacterized protein MG055.2 homolog. FT /FTId=PRO_0000210400. FT TRANSMEM 13 35 Helical. {ECO:0000255}. FT TRANSMEM 57 75 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 14519 MW; EFCDC8D6A0E9AD9B CRC64; MKVIKKLNLL NELTMLVCIF FFVCTISLIG IGIMYDLINR TSLSAPRRDP IFRNLNTVLI VLGVLEILLM VAQLVMSNMA ANIINEVAEN VEQKFAKALK WSRFLPFGLL QLYCYHKIKL VTQTDNI // ID Y076_MYCPN Reviewed; 564 AA. AC P75041; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MG061 homolog 1; GN OrderedLocusNames=MPN_076; ORFNames=MP079, R02_orf564o; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95727.1; -; Genomic_DNA. DR PIR; S73405; S73405. DR RefSeq; NP_109764.1; NC_000912.1. DR RefSeq; WP_010874433.1; NC_000912.1. DR ProteinModelPortal; P75041; -. DR IntAct; P75041; 1. DR EnsemblBacteria; AAB95727; AAB95727; MPN_076. DR GeneID; 877154; -. DR KEGG; mpn:MPN076; -. DR PATRIC; 20021431; VBIMycPne110_0077. DR OMA; PHEYKGS; -. DR OrthoDB; EOG6TTVJZ; -. DR BioCyc; MPNE272634:GJ6Z-78-MONOMER; -. DR Proteomes; UP000000808; 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; IPR020846; MFS_dom. DR InterPro; IPR011699; MFS_Mycoplasma. DR Pfam; PF07672; MFS_Mycoplasma; 1. DR SUPFAM; SSF103473; SSF103473; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 564 Uncharacterized protein MG061 homolog 1. FT /FTId=PRO_0000210405. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. FT TRANSMEM 404 424 Helical. {ECO:0000255}. FT TRANSMEM 425 445 Helical. {ECO:0000255}. FT TRANSMEM 457 477 Helical. {ECO:0000255}. FT TRANSMEM 501 521 Helical. {ECO:0000255}. SQ SEQUENCE 564 AA; 61632 MW; EE65E57D11C8F953 CRC64; MLWAIVLLGY LLFVVEWFVI DRIAGKPAGI LDSNTKVLPN YDGWVNSFFA NSAGSIAGSA TNWSITLLRA VGSVLCGIVV LKFGYRYAVM IMMGLMCLCF PFLIIGDPLG GNNQLTLLRP LSKEVMGKLS SLSSQLHEGQ LLGPVMAEGK TMLADGQTID LVQGLDKNLI GTSSSIAGYA LFIIFRSTIA IGGTTLVTYS QPLIASLSTQ RRKSVLSNAN LWGFNSGIVV AFVPFLFQSV QQAGTKYWVF ILTALILIGF GILCVFAWFE KQMDPFMPQK QTKEQMQLGN QPSAGDILKR KATWKMIGMY GICLVVLVNP LTGGWWNILQ AVSPASSFNV KDGVKTLKPL EGAGGYFAGL PTLAILWVLG YGMGYMVFSP FNKTVYDRKR WLSFMFFMNA LMVIVIVLFA ATLGVGTAVG FAFVAIATFI GGSFAWSMQS TILILPHEFK EYKRSEVSVL FGYIWGFGYV IYTAFDITNS MFLEAPKLAN PGMKGVSILP GAIAGVALFA GLLLAAIAIV VTLPSSYLKN GDELVSEMTK KWKLNQWQFL VASKEKNRYA DLLK // ID Y084_MYCPN Reviewed; 524 AA. AC P75609; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized lipoprotein MPN_084; DE Flags: Precursor; GN OrderedLocusNames=MPN_084; ORFNames=MP071, R02_orf524; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95719.1; -; Genomic_DNA. DR PIR; S73397; S73397. DR RefSeq; NP_109772.1; NC_000912.1. DR RefSeq; WP_010874441.1; NC_000912.1. DR EnsemblBacteria; AAB95719; AAB95719; MPN_084. DR GeneID; 877129; -. DR KEGG; mpn:MPN084; -. DR PATRIC; 20021451; VBIMycPne110_0086. DR OMA; PAIETYK; -. DR OrthoDB; EOG6N9469; -. DR BioCyc; MPNE272634:GJ6Z-87-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 3. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 524 Uncharacterized lipoprotein MPN_084. FT /FTId=PRO_0000018739. FT LIPID 22 22 N-palmitoyl cysteine. {ECO:0000255}. FT LIPID 22 22 S-diacylglycerol cysteine. {ECO:0000255}. SQ SEQUENCE 524 AA; 59553 MW; F4E7138D8092E74F CRC64; MLLRSVWYKL GSLLIILPLT GCGYVRLKRA NFQTDFTINR IPTQGDVYHD NYDLTFSLNF ATSSKDSYGT GWLIDWKGDE NKPSNTDPFL IYLATNLHVV DALRNPQDYE PYNKDSNGQD YGNRDITHFF ALGKYTDPGL LGVETKEQSA FISIQTSAIP KTAYTANDFV DYQYDSLTKQ WNKKSDQKDQ TQEQTVIGQS WSYKPAYADF AVIEVPLFLD NVRDKQVFDY FVKPAIETYK KLGDTAQLFT EQNLKELEKE TYIMLGYPVV ESNIYAHILG QGKELRVTQQ VNNQPVKKNY VLQTITKEQH TLDITREIPT LIQNKSLSGD FVGSKLLSQE EQQQEHAFLG NLNQGIIDFA RLSNFNLQYH NREYQQYGKG LALANTNFSG GSSGTLVLNQ QKQISGVYFG VLEFGGTNGT NRESSIGVGQ ILRVKDDAQL QQHSHNNLLS QLGSSHNSIT YDIIFGNKDT KNYYAQFAKK HQTHLYSQIS SSNQQELKYV DNDPNLKIKE EAAKSTVQNL TVYS // ID Y085_MYCPN Reviewed; 440 AA. AC P75608; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MPN_085; GN OrderedLocusNames=MPN_085; ORFNames=MP070, R02_orf440; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_087. {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; U00089; AAB95718.1; -; Genomic_DNA. DR PIR; S73396; S73396. DR RefSeq; NP_109773.1; NC_000912.1. DR RefSeq; WP_010874442.1; NC_000912.1. DR EnsemblBacteria; AAB95718; AAB95718; MPN_085. DR GeneID; 877131; -. DR KEGG; mpn:MPN085; -. DR PATRIC; 20021453; VBIMycPne110_0087. DR OMA; FENHESN; -. DR BioCyc; MPNE272634:GJ6Z-88-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 440 Uncharacterized protein MPN_085. FT /FTId=PRO_0000210636. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 284 304 Helical. {ECO:0000255}. FT TRANSMEM 394 414 Helical. {ECO:0000255}. FT TRANSMEM 418 438 Helical. {ECO:0000255}. SQ SEQUENCE 440 AA; 50936 MW; F96291EBAB4A048F CRC64; MQLTTSQQMQ TNFLTTNKHH LLKYTNGLIW CWWLFVISLV LASSTFRGFF LGTINIVNFV FWILALIFGV AVAFINGVLS SELKENSVFQ EEQKRFFLGF FFPQMAFCNA LWLKLKLSYL NSERENLLEK IKQKLKKLTL SVFVVWGIYC VLATSIYLPN ALRILNIYQI PNLIALINNR LSEILPDGNR YFLGHSSFAF HYYEIVSRIP FLVFFIIPTI TLITLGCYLF AYLRFINSNK LRKPLSTLSI VIMLTDVVGI IQWIIIDILL IWLNVPFVIF VIFWVIKLVL PLAMIGTFVS SLTIYKKVTS KEWLAIKEEQ INLTTMNINI NMGEQSSKNM NSFENHESNE RNSLQIYQQH SSMMSETKRK QSSLSYDARI LLPKSPYNTK KTLFLIIFFS IISLILATIG SVFISFAIVQ ISIPFYVIGG VIWFFTFISL // ID Y096_MYCPN Reviewed; 264 AA. AC P75596; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MPN_096; GN OrderedLocusNames=MPN_096; ORFNames=MP058, R02_orf264; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_308 C-terminal region. 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; U00089; AAB95706.1; -; Genomic_DNA. DR PIR; S73384; S73384. DR RefSeq; NP_109784.1; NC_000912.1. DR RefSeq; WP_010874453.1; NC_000912.1. DR EnsemblBacteria; AAB95706; AAB95706; MPN_096. DR GeneID; 876789; -. DR KEGG; mpn:MPN096; -. DR PATRIC; 20021479; VBIMycPne110_0097. DR OrthoDB; EOG6G4VVV; -. DR BioCyc; MPNE272634:GJ6Z-102-MONOMER; -. DR Proteomes; UP000000808; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR Pfam; PF13520; AA_permease_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 264 Uncharacterized protein MPN_096. FT /FTId=PRO_0000210643. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. FT TRANSMEM 181 201 Helical. {ECO:0000255}. FT TRANSMEM 215 235 Helical. {ECO:0000255}. SQ SEQUENCE 264 AA; 28961 MW; 84F1B7716ACB928F CRC64; MLLGLGIVVL IYSLIALSVS LTTPNGAFSG LGDWLKHKKL GWFFGVLNLL IALGVAGIIN GFVMWTGKLT QSLIKSGELW VPDKCKLCLN KPKPVVGLIH AGILMVLTTV ALSSLGGLLY LPKVNASYDG KGFKSMGCLL EFADLIATWT SVGIFWFLGL VLLGGLLQIK KPKRWYFRTT GWLAVVVIGL TTLVVMVQPF VDLGIAVFNR SYERIVANTI LIAILVIIVL VMFFPTEPIK LRLWRKRIQA MEACGEDCDA CVEY // ID Y103_MYCPN Reviewed; 172 AA. AC P75566; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MPN_103; GN OrderedLocusNames=MPN_103; ORFNames=C09_orf172, MP051; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95699.1; -; Genomic_DNA. DR PIR; S73377; S73377. DR RefSeq; NP_109791.1; NC_000912.1. DR RefSeq; WP_010874460.1; NC_000912.1. DR IntAct; P75566; 2. DR EnsemblBacteria; AAB95699; AAB95699; MPN_103. DR GeneID; 876989; -. DR KEGG; mpn:MPN103; -. DR BioCyc; MPNE272634:GJ6Z-109-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 172 Uncharacterized protein MPN_103. FT /FTId=PRO_0000210645. SQ SEQUENCE 172 AA; 21221 MW; E48E8C70D84FBF8E CRC64; MKLSKFLIKL AMCYILIWFR HFLLSSIRII GTTWTFWTAW FFGAFRNIWC IRIIGNRWLF RSFWSTGTLR SIFNTRILWF FRSLRFLFNY FNWWFWFILD LLKYFEPTFT LFLFGALDLK KKFNFIACKL PVLFFSNGKE FIFTHHFLNK ARQQLISSKR PFVALLINEL HK // ID Y104_MYCPN Reviewed; 104 AA. AC P75565; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 14-OCT-2015, entry version 66. DE RecName: Full=UPF0134 protein MPN_104; GN OrderedLocusNames=MPN_104; ORFNames=C09_orf104, MP050; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95698.1; -; Genomic_DNA. DR PIR; S73376; S73376. DR RefSeq; NP_109792.1; NC_000912.1. DR RefSeq; WP_010874461.1; NC_000912.1. DR ProteinModelPortal; P75565; -. DR SMR; P75565; 46-103. DR EnsemblBacteria; AAB95698; AAB95698; MPN_104. DR GeneID; 877156; -. DR KEGG; mpn:MPN104; -. DR PATRIC; 20021505; VBIMycPne110_0110. DR OrthoDB; EOG6SV5BV; -. DR BioCyc; MPNE272634:GJ6Z-110-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 104 UPF0134 protein MPN_104. FT /FTId=PRO_0000221595. SQ SEQUENCE 104 AA; 11858 MW; F3884D7EC102BDAD CRC64; MVELDGKFAT KADLKRVEDK VDVLFELQKT QGEQIKVQGK QIEQLTETVQ KQGEQIKELQ VQVKAQGEEI KEIKVEQKAQ GQTLQLILKA LEGINKRLDN LESK // ID Y121_MYCPN Reviewed; 121 AA. AC P75353; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MG202 homolog; GN OrderedLocusNames=MPN_121; ORFNames=C09_orf121, MP033; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95681.1; -; Genomic_DNA. DR PIR; S73359; S73359. DR RefSeq; NP_109809.1; NC_000912.1. DR RefSeq; WP_010874478.1; NC_000912.1. DR IntAct; P75353; 2. DR EnsemblBacteria; AAB95681; AAB95681; MPN_121. DR GeneID; 877246; -. DR KEGG; mpn:MPN121; -. DR PATRIC; 20021541; VBIMycPne110_0128. DR OMA; AISEDHY; -. DR OrthoDB; EOG66QM68; -. DR BioCyc; MPNE272634:GJ6Z-127-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Uncharacterized protein MG202 homolog. FT /FTId=PRO_0000210453. SQ SEQUENCE 121 AA; 13321 MW; 7F72B749F2219E17 CRC64; MSTNKRRTIQ IEITEEHFKD LEKALEALKG TQLPFSTTVE QFVELILSNY VATSNKISNL AESGFDVASI QQELEKIGSA AGADDALKSF LDELLKTSQK SFSNTKDGKK NDDDNNSSSK S // ID Y129_MYCPN Reviewed; 149 AA. AC P75346; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MPN_129; GN OrderedLocusNames=MPN_129; ORFNames=C09_orf149b, MP025; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_090. {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; U00089; AAB95673.1; -; Genomic_DNA. DR PIR; S73351; S73351. DR RefSeq; NP_109817.1; NC_000912.1. DR RefSeq; WP_010874486.1; NC_000912.1. DR ProteinModelPortal; P75346; -. DR EnsemblBacteria; AAB95673; AAB95673; MPN_129. DR GeneID; 877286; -. DR KEGG; mpn:MPN129; -. DR PATRIC; 20021565; VBIMycPne110_0139. DR OMA; RENTQQY; -. DR BioCyc; MPNE272634:GJ6Z-136-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 149 Uncharacterized protein MPN_129. FT /FTId=PRO_0000210652. FT TRANSMEM 39 61 Helical. {ECO:0000255}. FT TRANSMEM 82 104 Helical. {ECO:0000255}. FT TRANSMEM 119 141 Helical. {ECO:0000255}. SQ SEQUENCE 149 AA; 16669 MW; BE82494CCCE2CAED CRC64; MVSFFDIYTK ASIVEAVRFS FLNTFQLKEL GLPIKEIAVP LGTLVFLFVV IITLIPLLII GNLIWTNLRL IERENTQQYQ LVFGYSLIVS DIVGFAIVFF GAILGTNLKS VELFIALGWM MMLGSLIALG TTANLVSSIY LYIKLALKR // ID Y137_MYCPN Reviewed; 228 AA. AC P75261; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=UPF0134 protein MPN_137; GN OrderedLocusNames=MPN_137; ORFNames=E07_orf228, MP017; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95665.1; -; Genomic_DNA. DR PIR; S73343; S73343. DR RefSeq; NP_109825.1; NC_000912.1. DR RefSeq; WP_010874494.1; NC_000912.1. DR ProteinModelPortal; P75261; -. DR IntAct; P75261; 1. DR EnsemblBacteria; AAB95665; AAB95665; MPN_137. DR GeneID; 877336; -. DR KEGG; mpn:MPN137; -. DR OMA; PWEEDIS; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-144-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 228 UPF0134 protein MPN_137. FT /FTId=PRO_0000221598. SQ SEQUENCE 228 AA; 26777 MW; 95A74DE7A54DC524 CRC64; MEKKPWEEDI SIEEFKKSLN KDKITNLIIK RRWNKGKSTY HLSFNGDFEV VTKKPSTKYV THKQLDQKLK EFKQDLMVEL HDTFATKADL RDSEARINQK LEALVQVVLL HGEQINKLTQ IVEKQGEQIR ELQVEQKAQR QEFNARMDRL ENLLVESIES TNKRFDSIEG RLDSMDSRLD SMENRLDSIE GRLDSVEGRL DSVEGRLDSM ENRLDSMETR LDKIDPPK // ID Y144_MYCPN Reviewed; 413 AA. AC P75142; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Putative adhesin P1-like protein MPN_144; GN OrderedLocusNames=MPN_144; ORFNames=E07_orf413, MP010; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95658.1; -; Genomic_DNA. DR PIR; S73336; S73336. DR RefSeq; NP_109832.1; NC_000912.1. DR RefSeq; WP_010874501.1; NC_000912.1. DR EnsemblBacteria; AAB95658; AAB95658; MPN_144. DR GeneID; 877183; -. DR KEGG; mpn:MPN144; -. DR PATRIC; 20021605; VBIMycPne110_0159. DR OMA; NNAHRAQ; -. DR BioCyc; MPNE272634:GJ6Z-151-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 413 Putative adhesin P1-like protein MPN_144. FT /FTId=PRO_0000210709. SQ SEQUENCE 413 AA; 43250 MW; 594375273CD5E6E5 CRC64; MGQQGQSGTS AGNPDSLKQD KISKSGDSLT TQDGNATGQQ EATNYTNLPP NLTPTADWPN ALSFTNKNNA HRAQLFLRGL LGSIPVLVNR SGSDSNKFQA TDQKWSYTDL QSDQTKLNLP AYGEVNGLLN PALVETYFGN TRAGGSGSNT TSSPGIGFKI PEQNNDSKAT LITPGLAWTP QDVGNLVVSG TSLSFQLGGW LVSFTDFIKP RAGYLGLQLS GLDASDSDQR ELIWAKRPWA AFRGSWVNRL GRVESVWDLK GVWADQAQLA AQAATSEASG SALAPHPNAL AFQVSVVEAS AYSSSTSSSG SGSSSNTSPY LHLIKPKKVE STTQLDQGLK NLLDPNQVRT KLRQSFGTDH STQPQSLKTT TPVFGTSSGN IGSVLSGGGA GGGSSGSGQS GVDLSPVERV SGH // ID Y145_MYCPN Reviewed; 179 AA. AC P75141; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=UPF0134 protein MPN_145; GN OrderedLocusNames=MPN_145; ORFNames=E07_orf179, MP009; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95657.1; -; Genomic_DNA. DR PIR; S73335; S73335. DR RefSeq; NP_109833.1; NC_000912.1. DR RefSeq; WP_010874502.1; NC_000912.1. DR ProteinModelPortal; P75141; -. DR EnsemblBacteria; AAB95657; AAB95657; MPN_145. DR GeneID; 877163; -. DR KEGG; mpn:MPN145; -. DR PATRIC; 20021609; VBIMycPne110_0161. DR OMA; KTRYVTH; -. DR OrthoDB; EOG6QCD98; -. DR BioCyc; MPNE272634:GJ6Z-152-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 179 UPF0134 protein MPN_145. FT /FTId=PRO_0000221601. SQ SEQUENCE 179 AA; 20533 MW; 7BBD7C0875FCF1B1 CRC64; MSYSPSLKEI IAILQKYTSK NYQSNCKTRP DGKLELSLNG VFEEIVKTPG KTRYVTHKQL DQKLKDFKQD LMVELHDTFA TKTDLKESEA RINQKLEALI QIVMVQGEQI KVHGEQINKL TQAVEKQGEK IEAQGQQIQK VNETLNFVVE SLGSIHKRLD SMEGRLDSME NRLDKLESK // ID Y157_MYCPN Reviewed; 402 AA. AC P75588; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG144 homolog; GN OrderedLocusNames=MPN_157; ORFNames=MP674, VXpSPT7_orf402; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96322.1; -; Genomic_DNA. DR PIR; S74000; S74000. DR RefSeq; NP_109845.1; NC_000912.1. DR RefSeq; WP_010874514.1; NC_000912.1. DR EnsemblBacteria; AAB96322; AAB96322; MPN_157. DR GeneID; 877330; -. DR KEGG; mpn:MPN157; -. DR PATRIC; 20021637; VBIMycPne110_0175. DR OrthoDB; EOG6W724W; -. DR BioCyc; MPNE272634:GJ6Z-164-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 402 Uncharacterized protein MG144 homolog. FT /FTId=PRO_0000210441. FT TRANSMEM 279 299 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. FT TRANSMEM 360 380 Helical. {ECO:0000255}. SQ SEQUENCE 402 AA; 44296 MW; 0882860660BF82D0 CRC64; MKPPKKPVNP PFGKLTDSKA GVVKATSSQE TKKVADTKPK NKGGLFSFFK KDKTEKPAKA AKPKDAFKSA IAELNPKANP KTVKADVAPA KIPHSDKGTV TPVELKPQTE APLPPGVKQP DPKKDKPKGG LFGFFKKDKN KDVKKEPAKP ATPVKTEPTS PKVEPTKVKP PGGVPTKPVV EKPVSAQPTV PLQPEPTFPV KAAPLPPGVK AEPESKKRFG LFKAFQKDDA KQPKQKLNLQ DQQDRFIDDP TAKKHFSAFN QKVGNLLKDK KTRNRDWKIV GWIHGLILLF FIPLLAIMNK FVTLPAQSYP AVSLQVSINN ALWGIAIFVI ANIALPFITM FVLFLTGVRD VHASRPVHYF IWVLMLLNLT FLVISCCLLA AAYANLDLYN IWRNLQALDP NN // ID Y206_MYCPN Reviewed; 113 AA. AC P75570; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein MPN_206; GN OrderedLocusNames=MPN_206; ORFNames=GT9_orf113, MP625; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96273.1; -; Genomic_DNA. DR PIR; S73951; S73951. DR EnsemblBacteria; AAB96273; AAB96273; MPN_206. DR BioCyc; MPNE272634:GJ6Z-213-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 113 Uncharacterized protein MPN_206. FT /FTId=PRO_0000210656. SQ SEQUENCE 113 AA; 13237 MW; F757C47E8391BA73 CRC64; MEERPPIPNI KNTVAKRKST SWLLRCHQLG RPKFFKAGSL VVKLVVASPP FWRLSVILNA QNKKPIPTKI STIPKTIKRT RAFSMRIQPF RTFSVWIWFE KTPYYNSIQF SAF // ID Y212_MYCPN Reviewed; 135 AA. AC P0CJ80; P75557; DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 1. DT 11-NOV-2015, entry version 16. DE RecName: Full=Uncharacterized protein MG074 homolog; GN OrderedLocusNames=MPN_212; ORFNames=G07_orf135, MP619; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96267.1; -; Genomic_DNA. DR PIR; S73945; S73945. DR RefSeq; NP_109900.1; NC_000912.1. DR RefSeq; WP_010874569.1; NC_000912.1. DR EnsemblBacteria; AAB96267; AAB96267; MPN_212. DR GeneID; 877072; -. DR KEGG; mpn:MPN212; -. DR PATRIC; 20021749; VBIMycPne110_0231. DR OMA; WFELINN; -. DR OrthoDB; EOG6130M4; -. DR BioCyc; MPNE272634:GJ6Z-219-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 135 Uncharacterized protein MG074 homolog. FT /FTId=PRO_0000210410. SQ SEQUENCE 135 AA; 16104 MW; C07CD5273A17E088 CRC64; MRKLIKLNVI VFVLLYLGEL FASLSFKLIS CLKTRNQYSL NGYYALFVFV NIIQKMANSF QKLASSVVLF ETEINEFLVL FTDTKNKREE SEPVRQVSTT QEYHQVTLDQ QHYFNHKLSD YFRLFKDKTF FFEII // ID Y214_MYCPN Reviewed; 138 AA. AC P75555; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG076 homolog; GN OrderedLocusNames=MPN_214; ORFNames=G07_orf138, MP617; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96265.1; -; Genomic_DNA. DR PIR; S73943; S73943. DR RefSeq; NP_109902.1; NC_000912.1. DR RefSeq; WP_010874571.1; NC_000912.1. DR EnsemblBacteria; AAB96265; AAB96265; MPN_214. DR GeneID; 877082; -. DR KEGG; mpn:MPN214; -. DR PATRIC; 20021753; VBIMycPne110_0233. DR OMA; RYEISKF; -. DR OrthoDB; EOG654PCW; -. DR BioCyc; MPNE272634:GJ6Z-221-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 138 Uncharacterized protein MG076 homolog. FT /FTId=PRO_0000210414. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. SQ SEQUENCE 138 AA; 15773 MW; 7763801331012BED CRC64; MLGTQTTNSK PREYGGLIVS TIYIVLFFAI LNLTVFFNKT NNINLILKNS CVVSFVVVWL LVCLQGIVRL KTCDGARYEI SKFNQYLKLG SIYAKPNISF DEYKAKSSSY RKQTRGFWWM NFSLYLLGSL ISIVVSLL // ID Y007_MYCPN Reviewed; 253 AA. AC P75105; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MG007 homolog; GN OrderedLocusNames=MPN_007; ORFNames=D12_orf253, MP147; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75177:dnaX; NbExp=3; IntAct=EBI-2258613, EBI-2258609; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95795.1; -; Genomic_DNA. DR PIR; S73473; S73473. DR RefSeq; NP_109695.1; NC_000912.1. DR RefSeq; WP_010874364.1; NC_000912.1. DR ProteinModelPortal; P75105; -. DR IntAct; P75105; 4. DR EnsemblBacteria; AAB95795; AAB95795; MPN_007. DR GeneID; 877315; -. DR KEGG; mpn:MPN007; -. DR PATRIC; 20021287; VBIMycPne110_0007. DR KO; K02341; -. DR OMA; INIVCTE; -. DR OrthoDB; EOG6D2KS0; -. DR BioCyc; MPNE272634:GJ6Z-7-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 253 Uncharacterized protein MG007 homolog. FT /FTId=PRO_0000210384. SQ SEQUENCE 253 AA; 29056 MW; 90650B20802C8787 CRC64; MFNPTHALLI IQRRGSYLQP VLTEYLTRVV CEQQTGCQTC PSCLEILHGT YNNFYSFDQA NPFKREHALH LSEVLNRQSE SNQKQLYLIK NLETLTATAM NSLLRLIEEH PVNTYGVFTT KNENMILPTI LSRVQKVVLK KATQLPFQVD SKDQAILKSF FSVDEQLQAL DNGSFTRLKT IITTLTNKKN TASTVHEAWV LFKQLNQTET AQVLNFMVDY TKDLTKKDRL LNMVQNLVFN PPKAALFANL INW // ID Y016_MYCPN Reviewed; 288 AA. AC P75097; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MG012 homolog; GN OrderedLocusNames=MPN_016; ORFNames=D12_orf288, MP138; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95786.1; -; Genomic_DNA. DR PIR; S73464; S73464. DR RefSeq; NP_109704.1; NC_000912.1. DR RefSeq; WP_010874373.1; NC_000912.1. DR ProteinModelPortal; P75097; -. DR IntAct; P75097; 1. DR EnsemblBacteria; AAB95786; AAB95786; MPN_016. DR GeneID; 876841; -. DR KEGG; mpn:MPN016; -. DR PATRIC; 20021303; VBIMycPne110_0015. DR KO; K05844; -. DR OMA; WKTNTAL; -. DR OrthoDB; EOG6DZDX8; -. DR BioCyc; MPNE272634:GJ6Z-16-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification 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 InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX. DR Pfam; PF08443; RimK; 1. DR TIGRFAMs; TIGR00768; rimK_fam; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 288 Uncharacterized protein MG012 homolog. FT /FTId=PRO_0000205507. FT DOMAIN 107 288 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 178 188 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT METAL 248 248 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 261 261 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 261 261 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 263 263 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT BINDING 145 145 ATP. {ECO:0000255}. SQ SEQUENCE 288 AA; 32435 MW; D0215C770C9BDF58 CRC64; MKHISAVYNP AFTNIASKLN QTELLKDAAQ SLNIQLDFFT CFDINTNQDK TKLPFKSNTI LFLDKNIALA QWLESVGLRV INSSIAINNA DNKALSHAVL AQHPTIKQIP TLIGPQNFRL AWYPEKLEQF IEQIKRCFQF PVIVKSIYGS FGDYVFLCKD EQKLRQTLSG LTEQIIVQQY IATSNSEAVR VIVVNNQVVG ALHTQNEGDF RSNLNKGAVG EPYQLSQEET KLAITISQAM QLFYCGIDFL FDQDRSLIFC EVNSNVQLTK SSMYLKTNLA IQLLASIA // ID Y083_MYCPN Reviewed; 533 AA. AC P75610; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized lipoprotein MPN_083; DE Flags: Precursor; GN OrderedLocusNames=MPN_083; ORFNames=MP072, R02_orf533; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95720.1; -; Genomic_DNA. DR PIR; S73398; S73398. DR RefSeq; NP_109771.1; NC_000912.1. DR RefSeq; WP_010874440.1; NC_000912.1. DR IntAct; P75610; 1. DR EnsemblBacteria; AAB95720; AAB95720; MPN_083. DR GeneID; 877109; -. DR KEGG; mpn:MPN083; -. DR PATRIC; 20021449; VBIMycPne110_0085. DR OMA; QEWIRPA; -. DR OrthoDB; EOG61S2V3; -. DR BioCyc; MPNE272634:GJ6Z-86-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 4. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 22 533 Uncharacterized lipoprotein MPN_083. FT /FTId=PRO_0000018738. FT LIPID 22 22 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 22 22 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 533 AA; 59972 MW; 5E096DE3E8E054EB CRC64; MVKVWKIGFG VFLPTALLFS ACSFKDYIPT PSFRKDFSTE NNFVKNKVPG KDDIYSKFYD LTFSLNFVNN QAQEFGTGWL IDWKGDENKN LSKNKEGQTA SQTRSSSEQT TDQDANLFTA YIATNLHVAD GLKNDQDYAP YNKDGWGQPY PYQQKTQSFL LGKYTKPNVQ LVKTNYEKPE DAVIEQKLKE DSLLFIQTST LPKTAYAAID PVNFSYNPTR TNGFWTAGKY NVYNGGNSIG NYADFAVIEV PLVLSNPNDA KIYQEWIRPA TQAYKYLGDV EGLFAKKGYR SYIQDFYHLL GYPVTKNTKS EFILGQSQGT VNHMSFSNDE SNTTNTITKA SLTQQPHKEQ SAYVVRESGL PTLTMNVDKY TGAKGTHLVN VDQITDLSLG DGLIDFGGLS RFILQYHNVN YKQFGYGTIL WDTNFGGGSS GSAIFNQNKQ INSIYFGALV NVTTDRNENV GLGLGQILRA PNTFNSSHEV PYSYDLIFGD VNTTNFYAQF AKKHNTHMWS KIQSTQNGEI GFHKNSKTGQ QRH // ID Y094_MYCPN Reviewed; 140 AA. AC P75598; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=UPF0134 protein MPN_094; GN OrderedLocusNames=MPN_094; ORFNames=MP060, R02_orf140; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95708.1; -; Genomic_DNA. DR PIR; S73386; S73386. DR RefSeq; NP_109782.1; NC_000912.1. DR RefSeq; WP_010874451.1; NC_000912.1. DR ProteinModelPortal; P75598; -. DR IntAct; P75598; 2. DR EnsemblBacteria; AAB95708; AAB95708; MPN_094. DR GeneID; 876767; -. DR KEGG; mpn:MPN094; -. DR PATRIC; 20021463; VBIMycPne110_0092. DR OMA; KEFHDMM; -. DR OrthoDB; EOG6FBWTD; -. DR BioCyc; MPNE272634:GJ6Z-97-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 UPF0134 protein MPN_094. FT /FTId=PRO_0000221593. SQ SEQUENCE 140 AA; 16625 MW; 91D07DF689F869D3 CRC64; MKEKIPFYNE KEFHDMMKKT KKGTFSGWYI IDKDNKSVEF SGNFNRQFKL NKPVIPVNTE YVTRKEFNEY KDSNDQRLTK IETTLAAQGE QIRIQGEQIK ELQIEQKAQG ETLKLILQTL QKMSDRLNKM DVRLDKLESK // ID Y101_MYCPN Reviewed; 428 AA. AC P75568; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MPN_101; GN OrderedLocusNames=MPN_101; ORFNames=C09_orf428V, MP053; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAB95701.1; -; Genomic_DNA. DR PIR; S73379; S73379. DR RefSeq; NP_109789.1; NC_000912.1. DR RefSeq; WP_010874458.1; NC_000912.1. DR EnsemblBacteria; AAB95701; AAB95701; MPN_101. DR GeneID; 877387; -. DR KEGG; mpn:MPN101; -. DR PATRIC; 20021495; VBIMycPne110_0105. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-107-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF12378; CytadhesinP1; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 428 Uncharacterized protein MPN_101. FT /FTId=PRO_0000210644. SQ SEQUENCE 428 AA; 46909 MW; 991143BEF683A261 CRC64; MRDNSAKGIT AGSESQQTTY DPTRTEAALT ASTTFALRRY DLAGRALYDL DFSRLNPQTP TRDQTGQITF NPFGGFGLSG AAPQQWNEVK NKVPVEVAQD PSNPYRFAVL LVPRSVVYYE QLQRGLALPN QGSSSGSGQQ NTTIGAYGLK VKNAEADTAK SNEKLQGDES KSSNGSSSTS TTTQRGGSSG DTKVKALQVA VKKKSGSQGN SGEQGTEQVE LESNDLANAP IKRGEESGQS VQLKAADFGT TPSSSGSGGN SNPGSPTPWR PWLATEQIHK DLPKWSASIL ILYDAPYARN RTAIDRVDHL DPKVMTANYP PSWRTPKWNH HGLWDWKARD VLLQTTGFFN SRRHPEWFDQ GQAVADNTQT GFDTDDTDNK KTRLSKGSWL RQAGPDRPPV WSVLRQHWQP HLVRASAFGV WDLFVLIN // ID Y108_MYCPN Reviewed; 404 AA. AC P75561; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized adenine-specific methylase MPN_108; DE EC=2.1.1.72; GN OrderedLocusNames=MPN_108; ORFNames=C09_orf404, MP046; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase 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; U00089; AAB95694.1; -; Genomic_DNA. DR PIR; S73372; S73372. DR RefSeq; NP_109796.1; NC_000912.1. DR RefSeq; WP_010874465.1; NC_000912.1. DR ProteinModelPortal; P75561; -. DR IntAct; P75561; 1. DR EnsemblBacteria; AAB95694; AAB95694; MPN_108. DR GeneID; 877203; -. DR KEGG; mpn:MPN108; -. DR PATRIC; 20021513; VBIMycPne110_0114. DR KO; K00571; -. DR OrthoDB; EOG6HQSKB; -. DR BioCyc; MPNE272634:GJ6Z-114-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 3. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; RM_methylase_Eco57I. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF07669; Eco57I; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 404 Uncharacterized adenine-specific FT methylase MPN_108. FT /FTId=PRO_0000088016. SQ SEQUENCE 404 AA; 47115 MW; D096EEF4E1CD6895 CRC64; MSQNGDKDHE LIQGKVKSKT EIEDSVILDQ DTLQGKGEEK TKLDELIRWE AEKNDLLKLI DNVGNDEVFT TVETCQRMLD DLFPQDHEVW SNPDLKWLNP CDKNGVFFRE IALRLDKGLA KVIPDEYERK KHIMTKMLFS IDLTKFTSLM VRRTLYYCIK ANKRKTSEDE GCAIANGAWF NNECGNVVKP YKEHYFDKQG KNKKCKFCRT DEKFKYQQSS SNEKYAYDFI HLNPNEYESY FKTNFGVMKF DVIIGNPPYQ LANNRGGDAG DGNGANPIFQ EFILRALELQ PKYLAMIVPA RWINSSEKVF LKFRAKLQKS NGFKGINIFF DSKHCFPNRQ IKGGVCYFNW QNGYEGQTLI TTKSSKKGKQ EEIETYKRDF FAPVLNNTEQ VIFRKKFDTT FIKR // ID Y131_MYCPN Reviewed; 221 AA. AC P75267; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Putative adhesin P1-like protein MPN_131; GN OrderedLocusNames=MPN_131; ORFNames=E07_orf221V, MP023; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95671.1; -; Genomic_DNA. DR PIR; S73349; S73349. DR RefSeq; NP_109819.1; NC_000912.1. DR RefSeq; WP_010874488.1; NC_000912.1. DR EnsemblBacteria; AAB95671; AAB95671; MPN_131. DR GeneID; 877230; -. DR KEGG; mpn:MPN131; -. DR PATRIC; 20021573; VBIMycPne110_0143. DR OMA; TNFASAK; -. DR BioCyc; MPNE272634:GJ6Z-138-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 221 Putative adhesin P1-like protein MPN_131. FT /FTId=PRO_0000210707. SQ SEQUENCE 221 AA; 23200 MW; AA586FA39C5A5C00 CRC64; MLDYVPWIGN GYRYGNNHRG SNSSTSGVTT QGQSQNASSN EPAPTFSNVG VGLKANVNGT LSGSRTTPNQ QGTPWLTLDQ ANLQLWTGAG WRNDKNGQSD ENYTNFASAK GSTNQQGSTT GGSAGNPDSL KQDKADKSGD SVTVAEATSG DNLTNYTNLP PTSPPHPTDR TRCHSPTRTT PSGCSCSCAA CWAASRCWSI RVGKMITVSL IPPTKNGLTP N // ID Y148_MYCPN Reviewed; 140 AA. AC P75138; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_148; GN OrderedLocusNames=MPN_148; ORFNames=E07_orf140, MP006; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95654.1; -; Genomic_DNA. DR PIR; S73332; S73332. DR EnsemblBacteria; AAB95654; AAB95654; MPN_148. DR PATRIC; 20021615; VBIMycPne110_0164. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-155-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MPN_148. FT /FTId=PRO_0000210654. SQ SEQUENCE 140 AA; 16187 MW; 8097D116EA510325 CRC64; MERKVDHFQM TYQSFKDLSI KAKLSYTFNW FGDYSSGGFT AKKGDKHYFD LFLKIKPDPN KSFKAANFKT EEKNSTAIDG QETTRNLEWI EFGASISWSL KGKDDASEKS VKQFLDSYAN NTSGYSSDIN LFSYLEYLIR // ID Y160_MYCPN Reviewed; 377 AA. AC P75585; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG147 homolog; GN OrderedLocusNames=MPN_160; ORFNames=MP671, VXpSPT7_orf377; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96319.1; -; Genomic_DNA. DR PIR; S73997; S73997. DR RefSeq; NP_109848.1; NC_000912.1. DR RefSeq; WP_010874517.1; NC_000912.1. DR EnsemblBacteria; AAB96319; AAB96319; MPN_160. DR GeneID; 876859; -. DR KEGG; mpn:MPN160; -. DR PATRIC; 20021643; VBIMycPne110_0178. DR OMA; NIANHFG; -. DR OrthoDB; EOG6MD92G; -. DR BioCyc; MPNE272634:GJ6Z-167-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 377 Uncharacterized protein MG147 homolog. FT /FTId=PRO_0000210443. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TRANSMEM 292 312 Helical. {ECO:0000255}. FT TRANSMEM 339 359 Helical. {ECO:0000255}. SQ SEQUENCE 377 AA; 42971 MW; AB0380C41E1A7AC7 CRC64; MLWTRALILE LKTNKQSRLL WLLAIPLLIS LTLLTYGLVL FSSSGRIDHG DHFHLRERFV LTTEELVTFV VASVVFALTV ALFGLGCWKL LQGPKVDRTN IKLANSNPAP QAVVLQADCD HFQVGDHCVF SAEKQHFKQQ FKQDFLGKSK FSFRNELYRF CLIGVLISLN LALSMVEIPG IVLPWGSSIQ FRFFNTAILF IAIRFVGLLS TSLIAIITPW IHLLLHPVHT PISTVFYMGN DLVVLWIFYF FYYHIFKAEV KQTTTVVNNK EFSQLVNTHK TKVAKALALI PVNLICGFIE GLGFYVGYFL ILGKFGSVGH KIFYDSQANR DLINSANVIY FLLTTTTIFS LKYLFELLFF YSVEKGILNI SRHFGLY // ID Y161_MYCPN Reviewed; 445 AA. AC P75584; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MG148 homolog; GN OrderedLocusNames=MPN_161; ORFNames=MP670, VXpSPT7_orf445; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96318.1; -; Genomic_DNA. DR PIR; S73996; S73996. DR RefSeq; NP_109849.1; NC_000912.1. DR RefSeq; WP_010874518.1; NC_000912.1. DR ProteinModelPortal; P75584; -. DR EnsemblBacteria; AAB96318; AAB96318; MPN_161. DR GeneID; 877334; -. DR KEGG; mpn:MPN161; -. DR PATRIC; 20021645; VBIMycPne110_0179. DR OMA; DITHFES; -. DR OrthoDB; EOG6CP3W2; -. DR BioCyc; MPNE272634:GJ6Z-168-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR019219; DUF2130. DR Pfam; PF09903; DUF2130; 1. DR PIRSF; PIRSF005850; UCP005850; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 445 Uncharacterized protein MG148 homolog. FT /FTId=PRO_0000210445. SQ SEQUENCE 445 AA; 52867 MW; A95C29C67D2134BB CRC64; MSDVKYLQVE IVDKNTIRLQ EDGKKGQQIR LDQIIKVDQS NILNTLEQAQ REAYEREAQS RYQTKLAKEL SEKDNTFLKQ KAAWNQAHNT QIQQLYQQIT NLENQVNNIK RETESKKDNE YQQQIVKLET QLQSIKKETE SQKDLEYERK ANKTKEENQQ ELERQRQYFL EQLEQAQKDI EELKTREERF SKWAIAKKGK ELEKWCWEAY KNYEELFQNC VFAPYSELVK GAKKSIGVED DESNINEKAD FIFQVFNPNN DKEPFFSICC EMKTEFTESK SRTKNEDHVK KLIADAKRAK CQYGFLVSEL ELNTENDVQV QRMHTSNSEV EVYLVRPMFF IVMLRLFYFL AKKMFAQVDV NSEYLDKEAL NASFSDLKKS LLEKTFTDLN KVFQNNIDEL EKIEGLVTKL KAANEKALNS RLNNWEEKIR KFEFKLNKDI VKKLE // ID Y205_MYCPN Reviewed; 438 AA. AC P75571; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MPN_205; GN OrderedLocusNames=MPN_205; ORFNames=GT9_orf438V, MP626; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAB96274.1; -; Genomic_DNA. DR PIR; S73952; S73952. DR RefSeq; NP_109893.1; NC_000912.1. DR RefSeq; WP_010874562.1; NC_000912.1. DR EnsemblBacteria; AAB96274; AAB96274; MPN_205. DR GeneID; 877056; -. DR KEGG; mpn:MPN205; -. DR PATRIC; 20021737; VBIMycPne110_0225. DR OMA; GSAPQQW; -. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-212-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF12378; CytadhesinP1; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 438 Uncharacterized protein MPN_205. FT /FTId=PRO_0000210655. SQ SEQUENCE 438 AA; 47925 MW; D6CB89515576AD7E CRC64; MRDNTAKGIT AGSGSQQTTY DPARTEATLT TTTFALRRYD LAGRALYDLD FSKLNPQTPT RDANCQITFN PFGGFGLSGS APQQWNEVKN KVPVEVAQDP TDPYRFAVLL VPRSVVYYEQ LQRGLALPNQ GSSSGSGQQN TTIGAYGLKV KNAEADTAKS NEKLQGDESK SSNGSSSTST TTQRGSTNSD TKVKALKIEV KKKSDSEDNG QLQLEKNDLA NAPIKRGEES GQSVQLKADD FGTAPSSSGS GGNSNPGSPT PWRPWLATEQ IHKDLPKWSA SILILYDAPY ARNRTAIDRV DHLDPKVMTA NYPPSWRMPK WNHHGLWDWK ARDVLFQTTG FDESNTSNTK QGFQKEADSD KSAPIALPFE AYFANIGNLT WFGQALLVFG GNGHVTKSAH TAPLSIWLYI YLVKAVTFRL LLANSLLSKS NIYKKTAN // ID Y233_MYCPN Reviewed; 454 AA. AC P75538; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized lipoprotein MG095 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_233; ORFNames=G07_orf454, MP598; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96246.1; -; Genomic_DNA. DR PIR; S73924; S73924. DR RefSeq; NP_109921.1; NC_000912.1. DR RefSeq; WP_010874590.1; NC_000912.1. DR EnsemblBacteria; AAB96246; AAB96246; MPN_233. DR GeneID; 877133; -. DR KEGG; mpn:MPN233; -. DR PATRIC; 20021791; VBIMycPne110_0252. DR OMA; GNNNFWF; -. DR OrthoDB; EOG6W720M; -. DR BioCyc; MPNE272634:GJ6Z-240-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 22 454 Uncharacterized lipoprotein MG095 FT homolog. FT /FTId=PRO_0000014027. FT COMPBIAS 56 60 Poly-Ser. FT COMPBIAS 371 375 Poly-Ser. FT LIPID 22 22 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 22 22 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 454 AA; 49820 MW; D6209DA59DC842EC CRC64; MKYKTVKSIP LFLLGSIVFT ACSTPQSTFH LPVQTTVSAI KKDISGKTAT AVKAASSSSS TTTSNDDNNQ KGYFLETNRS TGTYDPNNST RLIKLGESGD FHAADQNKPE EALFERLYGG IASLLNFRII KPALTYWNTV TPSLKAIGKS SNLITFSQDI DETELQRALA NNLIVADDGN NNFWFGLKSL SFNSAKLTDN AQTQMAQKTT QAVTLKSQAQ MSSTNTKNTN KKIDLRDKIT LSSTMNTQGS GDNKNPSSGL IQKLVSVENI EAEFSFVKTG FNGNEIKFGD FVTENSPTTT QLKQVWKKKW GTELKKTNYK LQLNNFSLLL TYTPEVNKVE KGNNGDSNKG TIATPNGFSF LYPANLNETP SSSSSYWTNV TDLTKAATDT ENTNLLNDLQ KSQEQVNQFV AAITQNHLDV SEAALTKKQF GSLSISDFFK AIFKENGKDT KAKS // ID Y255_MYCPN Reviewed; 251 AA. AC P75519; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MG116 homolog; GN OrderedLocusNames=MPN_255; ORFNames=A65_orf251b, MP578; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96226.1; -; Genomic_DNA. DR PIR; S73904; S73904. DR RefSeq; NP_109943.1; NC_000912.1. DR RefSeq; WP_010874612.1; NC_000912.1. DR ProteinModelPortal; P75519; -. DR EnsemblBacteria; AAB96226; AAB96226; MPN_255. DR GeneID; 876842; -. DR KEGG; mpn:MPN255; -. DR PATRIC; 20021835; VBIMycPne110_0274. DR OMA; FILIEAN; -. DR OrthoDB; EOG6B3662; -. DR BioCyc; MPNE272634:GJ6Z-262-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 251 Uncharacterized protein MG116 homolog. FT /FTId=PRO_0000210420. SQ SEQUENCE 251 AA; 29048 MW; 737A9180DEC416C1 CRC64; MQRTLNVGVI LCESFISNAQ NPVNSYIKIY ENVRMFEFAI KLLQESRINF QKILLYVLEE QIPLVEKVVA KYENCWVFRS KHNEVEDIYE AKGFIEDKYK IGLKSSKNQA SSYYDNCCFV VLEACRPLTS KKVVKNVYEK AMIDGAAVAV LPFERQLVCG DNTKAVRQLK DKGNMNYWRQ SSTWELQFPQ AYTLNKLNQY HKNLFMKARN MLDLMNISAK NPLSIVDGSA YSFRVVTSLD FEILLGILRN G // ID Y010_MYCPN Reviewed; 131 AA. AC P75103; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=UPF0134 protein MPN_010; GN OrderedLocusNames=MPN_010; ORFNames=D12_orf131, MP144; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95792.1; -; Genomic_DNA. DR PIR; S73470; S73470. DR RefSeq; NP_109698.1; NC_000912.1. DR RefSeq; WP_010874367.1; NC_000912.1. DR PDB; 2BA2; X-ray; 1.80 A; A/B/C=46-130. DR PDBsum; 2BA2; -. DR ProteinModelPortal; P75103; -. DR SMR; P75103; 50-130. DR EnsemblBacteria; AAB95792; AAB95792; MPN_010. DR GeneID; 877377; -. DR KEGG; mpn:MPN010; -. DR PATRIC; 20021293; VBIMycPne110_0010. DR OMA; AVQNQNI; -. DR OrthoDB; EOG6FBWTD; -. DR BioCyc; MPNE272634:GJ6Z-10-MONOMER; -. DR EvolutionaryTrace; P75103; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 131 UPF0134 protein MPN_010. FT /FTId=PRO_0000221590. FT HELIX 56 63 {ECO:0000244|PDB:2BA2}. FT HELIX 69 128 {ECO:0000244|PDB:2BA2}. SQ SEQUENCE 131 AA; 15232 MW; 2965F8DC41B594B7 CRC64; MAYSPSLNDI KSILNKYTSK DYELKCENRY DGKLELWLKG VFEEIVKTPG TRYVTHKQLD EKLKNFVTKT EFKEFQTVVM ESFAVQNQNI DAQGEQIKEL QVEQKAQGKT LQLILEALQG INKRLDNLES K // ID Y020_MYCPN Reviewed; 1030 AA. AC P75093; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized ATP-dependent helicase MPN_020; DE EC=3.6.4.-; GN OrderedLocusNames=MPN_020; ORFNames=D12_orf1030, MP134; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC -!- SIMILARITY: Contains 1 SWIM-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95782.1; -; Genomic_DNA. DR PIR; S73460; S73460. DR RefSeq; NP_109708.1; NC_000912.1. DR RefSeq; WP_010874377.1; NC_000912.1. DR ProteinModelPortal; P75093; -. DR IntAct; P75093; 15. DR EnsemblBacteria; AAB95782; AAB95782; MPN_020. DR GeneID; 876986; -. DR KEGG; mpn:MPN020; -. DR PATRIC; 20021315; VBIMycPne110_0019. DR OMA; VYRIIAK; -. DR OrthoDB; EOG64R61X; -. DR BioCyc; MPNE272634:GJ6Z-22-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR007527; Znf_SWIM. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR Pfam; PF04434; SWIM; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50966; ZF_SWIM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 1030 Uncharacterized ATP-dependent helicase FT MPN_020. FT /FTId=PRO_0000074381. FT DOMAIN 590 751 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 867 1021 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT ZN_FING 51 86 SWIM-type. {ECO:0000255|PROSITE- FT ProRule:PRU00325}. FT NP_BIND 603 610 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 702 705 DEAQ box. SQ SEQUENCE 1030 AA; 119602 MW; 7272E2B162AF1737 CRC64; MTIAEIRKFA QTTQKFVEAE NLFEHGNVVL PKKYLNKARG MAEVLYNSQV IKVSFTAKDG ELTCKCSCLA NVDNCVHIVA VLLKYHQMLV ESKRSFNLAE AFHLDCDQAE MLIENLSLEI IAGGWNFKLG FTINLDKHNP QPSVLRFYCC DATFVYFLHL ENDTLHSVEL SKFKPEERAT LLFFDKLCKQ FTVGYDRNSL LFPLAGFLKE LQANTEPTIF VFNDDKIDNI LFLRISKKHH GLNHVCGFSG KKVFDFVTYK QKEKQIVLRS AYLSKFTDFK FPYTINIYKL QFGEPLFFYF LIQLKRDGFK NFYFQSEDSI VKEKEYLPKL YFKVEYDPVK NKFVSDAFFK YKNHFNKGTT TVYPHRYYMA KKSDRGGFNR LLFYEEAVEN FYQDQFDLGY FRKFEHLPIQ DKNQIEAFKA ALDDLMPVDL AEVSLSDNLL HQKPLHFALS DLEAVAVDDK QIKLSFAPSA VELKLIKRIL SAYHKGNVVC IDQESWYDLK QPAAKELIQF WNQFDLRNAT SDGNHIYLPK YYLFEVAKIF SQYLDIKNLF DVPTIKKIED QNNNVFDLSL EHKKITSLRN YQQEGVKWIR GLEENKFGGI LADEMGLGKT VQVIFALLDS YLKNHVNLPS LIIVPASLLL NWKSEFEKFA PQIKVKVANI PSKERGELYE KLTNEILIVS FNVLRSDVKL ITKQRFHYVV IDEAQGIKND SSSITKAAKK VKGNFCLALT GTPIENRLLD LWSCFDFVLP SFLGNKKQFT DQFEKEKTDQ SFHLLMQRTS PFILRRTKSK VLKELPNKIT TDIYVELNPM HQKLYEEERD RGLEEIKQIQ DKSSFNILTL ILKLRHLCSL PKNSQGILEN SAKKEAALEI IHEAIENQRK IILFTQFIDV IDHFKDTFKE QGIEYFIFDG RKSPKSRHSI IEKFNNAKNP CVLLASLKAG GVGINLTAAE VVIHFDVWWN TAVENQATDR AHRIGQKKTV QVYRIIAKNT IEERVCQVQA EKQELVSKTL VEDVNFFESL TNEELLRLFE // ID Y075_MYCPN Reviewed; 299 AA. AC P75042; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized glycosyltransferase MG060 homolog; DE EC=2.4.-.-; GN OrderedLocusNames=MPN_075; ORFNames=D09_orf299, MP080; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; U00089; AAB95728.1; -; Genomic_DNA. DR PIR; S73406; S73406. DR RefSeq; NP_109763.1; NC_000912.1. DR RefSeq; WP_010874432.1; NC_000912.1. DR ProteinModelPortal; P75042; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB95728; AAB95728; MPN_075. DR GeneID; 877325; -. DR KEGG; mpn:MPN075; -. DR PATRIC; 20021429; VBIMycPne110_0076. DR OMA; ISAYHKE; -. DR OrthoDB; EOG6DRPFQ; -. DR BioCyc; MPNE272634:GJ6Z-77-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; 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 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 299 Uncharacterized glycosyltransferase MG060 FT homolog. FT /FTId=PRO_0000059244. SQ SEQUENCE 299 AA; 35079 MW; 6E3F89EDAE420417 CRC64; MKISVIISTY NCGALIVKAL CSLVSNQTPA CELEVLVIDD GSIDNTRQII KKFQAKVSFT LKYFYKKNGN WGSVINYVKE NRLANGDWIT VLDSDDTLKP NTLNKLANLV EKADYDLVVF DYTKCWKKIK LKIHTYPTWW KNMTRELQKQ TPFCIPLGKF LKRNLFYKLP KLKEKVSFQD ALYTASSLKL AKKVRHVNQS GGNYHFKRAG NSMSIPWNIK RFSAELDICK DLIRLNAQEI ALVHLLRQQF RVQLKEKQIQ LAVTRDFNFS GFSWYTRCFL WMVYQTMLKR YFYLQTTKQ // ID Y102_MYCPN Reviewed; 272 AA. AC P75567; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Putative MgpC-like protein MPN_102; GN OrderedLocusNames=MPN_102; ORFNames=C09_orf272, MP052; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95700.1; -; Genomic_DNA. DR PIR; S73378; S73378. DR EnsemblBacteria; AAB95700; AAB95700; MPN_102. DR PATRIC; 20021499; VBIMycPne110_0107. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-108-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 272 Putative MgpC-like protein MPN_102. FT /FTId=PRO_0000210719. SQ SEQUENCE 272 AA; 29312 MW; F9609271F5AD2B84 CRC64; MASSTSLGNV GDTTALTPLL RGATTTTTVQ LKQTDSNSQD QQKFQKYLNT AQALHQMGVI VPELSQGGWQ SQTARHSSTR GLQSAGANRG ASLAARTTTT VGVGRRDSTS TTLELPNVIT QLYHTSTSQL AYLNGQIVVM GSNAVPSLWY WVVDERTTSG RATWWAKTHL NFGTEVQKNF VENQLGFKSE DNSNTSLTNF KSQGLTQPAY LISGLDVVAD HLVFAAFKAG AVGYDMTTDS NASTYNQALT WSTTAGLDSD GGTTTWWRIL RG // ID Y112_MYCPN Reviewed; 130 AA. AC P75450; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MPN_112; GN OrderedLocusNames=MPN_112; ORFNames=C09_orf130b, MP042; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95690.1; -; Genomic_DNA. DR PIR; S73368; S73368. DR RefSeq; NP_109800.1; NC_000912.1. DR RefSeq; WP_010874469.1; NC_000912.1. DR ProteinModelPortal; P75450; -. DR EnsemblBacteria; AAB95690; AAB95690; MPN_112. DR GeneID; 877263; -. DR KEGG; mpn:MPN112; -. DR PATRIC; 20021523; VBIMycPne110_0119. DR OMA; YWEISAL; -. DR OrthoDB; EOG6C2WBV; -. DR BioCyc; MPNE272634:GJ6Z-118-MONOMER; -. DR Proteomes; UP000000808; 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; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 130 Uncharacterized protein MPN_112. FT /FTId=PRO_0000210649. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. SQ SEQUENCE 130 AA; 14730 MW; CCF7F807EB9968D7 CRC64; MLDKLLQKFR DQKKPVFHKE EGYWEISALR KWAAILIIAF GAGIIYIVPY FAFFQFKTAV ANVTGVEPNR ISLLLTAYGI VSLLFYIPGG WLADRISAKA LFSVSMFGTG IITFWYFLVG LKGIVWITPN // ID Y135_MYCPN Reviewed; 329 AA. AC P75263; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable ABC transporter permease protein MG188 homolog; GN OrderedLocusNames=MPN_135; ORFNames=E07_orf329, MP019; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. MalFG subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95667.1; -; Genomic_DNA. DR PIR; S73345; S73345. DR RefSeq; NP_109823.1; NC_000912.1. DR RefSeq; WP_010874492.1; NC_000912.1. DR ProteinModelPortal; P75263; -. DR IntAct; P75263; 1. DR EnsemblBacteria; AAB95667; AAB95667; MPN_135. DR GeneID; 877306; -. DR KEGG; mpn:MPN135; -. DR PATRIC; 20021585; VBIMycPne110_0149. DR KO; K02025; -. DR OMA; NEAFISW; -. DR OrthoDB; EOG625K13; -. DR BioCyc; MPNE272634:GJ6Z-142-MONOMER; -. DR Proteomes; UP000000808; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 329 Probable ABC transporter permease protein FT MG188 homolog. FT /FTId=PRO_0000060286. FT TRANSMEM 30 50 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 96 116 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 128 148 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 176 196 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 234 254 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 283 303 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 88 303 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 329 AA; 37488 MW; 7DE0D96DDB01C89B CRC64; MFKWLLKHRS KPTPLELGIF DQKVSFWKPF LLFCPALLTT FLFTLVPFFL TLQKGFSHNE DIYRVDSQQF GFQTFANLFS ESNFILGLRN SFLYSIISLP LTIVLAIIIS SAIVFVYRKL ARGFWQTVFF LPYVTSGVAV SIAFIYILDS SSGILNNIFH VNIKWLDSGE RDTFNALWGI LIFGIWKNMA FNVLVISTAM LSVDPTLYKV ANLDGAKPIR QFFKITLPSI RPTLIFLLTL LILGGMQVFP ISLFNGNDSE AVTNGGSTIL LYIFQKIRDQ NNNFAGAATL VLFILGVCYG LVLRNGFRLI EWAQWKIKRH YVQTKLNLV // ID Y234_MYCPN Reviewed; 417 AA. AC P75537; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MPN_234; GN OrderedLocusNames=MPN_234; ORFNames=G07_orf417, MP597; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB96245.1; -; Genomic_DNA. DR PIR; S73923; S73923. DR EnsemblBacteria; AAB96245; AAB96245; MPN_234. DR PATRIC; 20021793; VBIMycPne110_0253. DR OMA; TINFATL; -. DR BioCyc; MPNE272634:GJ6Z-241-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 417 Uncharacterized protein MPN_234. FT /FTId=PRO_0000215254. SQ SEQUENCE 417 AA; 47650 MW; 8880670173D369C9 CRC64; MQFHAVYQNN DTKANLDFAL NISTINFATL QELQNSFDLQ GSDLTAGLFY KYSVNKLTSG TNDLTTIAKT ALGENIIQKQ VSLTQSIIKP RLEAAKTQYK QDIIAPFAKE RQAALAQHLK EIEEAKQRAE QLLKEQQEAE KRRQEEVKNV AETQQFNDSL TSAQKFKEYW LKQGKDVTKK VELIQALKSS FFRNQNRTFN FLIAGFRTAI DWYYNQEKNN TTAKNNAFGK NGIQFPVAGF QGIYMSQWLR DELSGKTDIK LNLKSLSVQN ENKNSSINWN KQKRIEIKQV KPFNYSFEIN LKYTGSYNVS LWYLIGAAIG GIPTSWSGTM DMKFIVDGDL DSGIVTKQDY PGSKFEFTED KLWFTLHVKQ QIKVKEQGFM NLLKGQSLDN LDLRTGTTKP PVVDLASYLH FVILTAK // ID Y236_MYCPN Reviewed; 479 AA. AC P75535; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Uncharacterized protein MG098 homolog; GN OrderedLocusNames=MPN_236; ORFNames=G07_orf479, MP595; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GatC 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; U00089; AAB96243.1; -; Genomic_DNA. DR PIR; S73921; S73921. DR RefSeq; NP_109924.1; NC_000912.1. DR RefSeq; WP_010874593.1; NC_000912.1. DR ProteinModelPortal; P75535; -. DR EnsemblBacteria; AAB96243; AAB96243; MPN_236. DR GeneID; 877199; -. DR KEGG; mpn:MPN236; -. DR PATRIC; 20021797; VBIMycPne110_0255. DR OMA; IFSAIIE; -. DR OrthoDB; EOG6Q2SJC; -. DR BioCyc; MPNE272634:GJ6Z-243-MONOMER; -. DR Proteomes; UP000000808; 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:0006450; P:regulation of translational fidelity; IEA:InterPro. 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 479 Uncharacterized protein MG098 homolog. FT /FTId=PRO_0000105364. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. FT TRANSMEM 287 307 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. SQ SEQUENCE 479 AA; 54161 MW; 9FE5ED0A49FC8C0E CRC64; MDKLINKPQP LTSDISTSGF IYFAVVFVAI MGYLLFKNLL FLFFFKRYPK NTPKIGVGNI TTIAMIIAVA VSIVLVLMAL AGGLAAALFR GYPGFRVTLE LILVKISGLL FGPIVGIFSA ATIDFLTVIF SGGVFNVGYV LGAILTGMIA GILREVLIST ALLHNRNLSD FAYLVLSIGM VIAAFLITQF FVLGISNNLK EIKGDEEFRL KFNAPSIVFE LSLTQYANIL LYFTIAIVIA MLVLYIVWLV KQRHLSFEHS RFFYRSYKHA NHQFTLFVLT KENWFYLILN VITLASTSLL MINIAFIPIF DTQTTGQTYE FWLLARLLFA PVIFLLDIIV IYPILLLLTP LMLKGFKTAV SKNQRKTLKQ SFTDLQSVVL PIINKRKHQQ LRQEELKRLA RATHFDLTEG EMEKLLVEFK TITQSFDRVM NIDTTSVEPM YAPFNTSPTP LRKDKVIVEK HPEKLLANCK EMSVGFVKV // ID Y254_MYCPN Reviewed; 157 AA. AC Q9EXC9; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Protein MG115 homolog; GN OrderedLocusNames=MPN_254; ORFNames=A65_orf157, MP578.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SIMILARITY: Belongs to the CinA 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; U00089; AAG34758.1; -; Genomic_DNA. DR RefSeq; NP_109942.1; NC_000912.1. DR RefSeq; WP_010874611.1; NC_000912.1. DR ProteinModelPortal; Q9EXC9; -. DR IntAct; Q9EXC9; 1. DR EnsemblBacteria; AAG34758; AAG34758; MPN_254. DR GeneID; 876878; -. DR KEGG; mpn:MPN254; -. DR PATRIC; 20021833; VBIMycPne110_0273. DR KO; K03743; -. DR OMA; CVREMAL; -. DR OrthoDB; EOG61S359; -. DR BioCyc; MPNE272634:GJ6Z-261-MONOMER; -. DR Proteomes; UP000000808; 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 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Protein MG115 homolog. FT /FTId=PRO_0000156789. SQ SEQUENCE 157 AA; 16959 MW; 4D3FB7EF94556B6F CRC64; MYARLIAEKL LNHKLTIATA ESVTGGLLSS SLTDIAGASR FFKGAIVAYS NELKKSLLNV KQSTLINHGA VSRYCVREMA LGLMQKLNVD IAVACSGVAG PDALENQAVG SLFFCVIVAN KAYDFETKLP AGSRNELRQL FVQKILQTVE HILSEIS // ID Y258_MYCPN Reviewed; 572 AA. AC P75516; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative carbohydrate transport ATP-binding protein MPN_258; GN OrderedLocusNames=MPN_258; ORFNames=MP575; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Part of the ABC transporter complex involved in CC carbohydrates import. Probably responsible for energy coupling to CC the transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96223.1; -; Genomic_DNA. DR PIR; S73901; S73901. DR RefSeq; NP_109946.1; NC_000912.1. DR RefSeq; WP_010874615.1; NC_000912.1. DR ProteinModelPortal; P75516; -. DR IntAct; P75516; 1. DR EnsemblBacteria; AAB96223; AAB96223; MPN_258. DR GeneID; 876920; -. DR KEGG; mpn:MPN258; -. DR PATRIC; 20021841; VBIMycPne110_0277. DR KO; K02056; -. DR OMA; MENICKS; -. DR OrthoDB; EOG6QK4RR; -. DR BioCyc; MPNE272634:GJ6Z-265-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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; 2. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Repeat; Sugar transport; KW Transport. FT CHAIN 1 572 Putative carbohydrate transport ATP- FT binding protein MPN_258. FT /FTId=PRO_0000092517. FT DOMAIN 6 253 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 327 572 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 572 AA; 64863 MW; 2B803BC7A5E8CE37 CRC64; MSKIAFRMEN ICKSFDNGRV KANVDVNLTV YENTVHTLLG ENGAGKSTLT SILFGLYQPD SGKIFIGEEE VHFKSSKDAV QHKIGMVHQH FKLVDNYTVL DNIILGNESS FSIPFTNGKL KLPLLHRKAS EAKIQAMMER YDLHVNLHQK VSRLTVGQQQ RVEILKVLFR DSDILIFDEP TAVLSDQEIK SFLNIIKNFK KMGKTIVLIS HKLNEIKEVA ETATILRQGH SVGTFQIKDT SIDEMARLMM GKELKETKNN TQFTAKGEPV LKVENLHLYL NQNWFYKLIA RWNQKRINQL QKQGKPAKTL WLKSWLEGLA AIEKTPRFIR GIVNNLGFGS QQVFDKGISF EIHKGEIFAI AGVEGNGQNQ LIDLICGLEK AAPKKVFFNG FDISRYSIRK RINAGIGFVL EDRHKYGLIL DQTVRFNAVN NQIDRKQFSS WNFLNQMQIA VYTNQIVDKF DVRGAVQGTA IVRLLSGGNQ QKLIIGRELT KQNELLVFAQ VTRGLDVGAI SFIHQKILDA KKQNNAILLV SYELDEILAI ADTIGVINKG NLLEVNKRDV MTRERIGKLI MQ // ID Y266_MYCPN Reviewed; 145 AA. AC P75509; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MG127 homolog; GN OrderedLocusNames=MPN_266; ORFNames=A65_orf145, MP567; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96215.1; -; Genomic_DNA. DR PIR; S73893; S73893. DR RefSeq; NP_109954.1; NC_000912.1. DR RefSeq; WP_010874623.1; NC_000912.1. DR ProteinModelPortal; P75509; -. DR IntAct; P75509; 1. DR EnsemblBacteria; AAB96215; AAB96215; MPN_266. DR GeneID; 877348; -. DR KEGG; mpn:MPN266; -. DR PATRIC; 20021857; VBIMycPne110_0285. DR KO; K16509; -. DR OMA; FITASCI; -. DR OrthoDB; EOG6WQDCS; -. DR BioCyc; MPNE272634:GJ6Z-273-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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; Oxidoreductase; Reference proteome. FT CHAIN 1 145 Uncharacterized protein MG127 homolog. FT /FTId=PRO_0000162586. SQ SEQUENCE 145 AA; 16809 MW; C84B8D7142706E31 CRC64; MLKKKVNNDA GKTFILISSS CSSCQKAIEY FKENNLSYTI ENFYKKPISD KRFRDILSLS EDGTESLFSK RADQIRSNTN QSVEDLTIPE LIKLIRERPS ILRRPIIIQY NSSGIPKRMR IGYNAAEIKV FERSLMEPKV RTVKK // ID Y287_MYCPN Reviewed; 118 AA. AC P75490; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=UPF0134 protein MPN_287; GN OrderedLocusNames=MPN_287; ORFNames=A65_orf118, MP548; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96196.1; -; Genomic_DNA. DR PIR; S73874; S73874. DR RefSeq; NP_109975.1; NC_000912.1. DR RefSeq; WP_010874644.1; NC_000912.1. DR ProteinModelPortal; P75490; -. DR EnsemblBacteria; AAB96196; AAB96196; MPN_287. DR GeneID; 877090; -. DR KEGG; mpn:MPN287; -. DR PATRIC; 20021909; VBIMycPne110_0311. DR OMA; QIKAKGE; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-294-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 118 UPF0134 protein MPN_287. FT /FTId=PRO_0000221605. SQ SEQUENCE 118 AA; 13359 MW; 3719782312A28B5D CRC64; MGFSDNLNHM EKRKSGYVTQ KQFSEFKDAN NQRLIKIETT LATQGEQLNQ LIKVVILQGE QIKELQVEQK AQGEQIKAKG EQIKAQSEQI KTQGETLKLI LQALGGINKR LDKVDPPK // ID Y030_MYCPN Reviewed; 168 AA. AC P75084; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG027 homolog; GN OrderedLocusNames=MPN_030; ORFNames=B01_orf168, MP124; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95772.1; -; Genomic_DNA. DR PIR; S73450; S73450. DR RefSeq; NP_109718.1; NC_000912.1. DR RefSeq; WP_010874387.1; NC_000912.1. DR ProteinModelPortal; P75084; -. DR SMR; P75084; 29-168. DR EnsemblBacteria; AAB95772; AAB95772; MPN_030. DR GeneID; 876895; -. DR KEGG; mpn:MPN030; -. DR PATRIC; 20021335; VBIMycPne110_0029. DR OMA; ALLIMDH; -. DR OrthoDB; EOG6S7XWB; -. DR BioCyc; MPNE272634:GJ6Z-32-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.940.10; -; 1. DR InterPro; IPR015268; DUF1948. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR Pfam; PF09185; DUF1948; 1. DR SUPFAM; SSF48013; SSF48013; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 168 Uncharacterized protein MG027 homolog. FT /FTId=PRO_0000210390. SQ SEQUENCE 168 AA; 19214 MW; C37192BBA3A82D4B CRC64; MCPSSFVLVI RLWFPPLTGA IVNGTTSKLT RTQRRIAIVE FIFATLFFLP KTADQIQAAF LDYDVPERPL NDWQKEIVKV FSERCVEFIE LIENQQQRNQ AEVQSKYNKV SGKKVDLLTK AVILCALSEQ HAQATDKPLL ISEALLIMDH YSQVPEKKQT HALLDKLL // ID Y036_MYCPN Reviewed; 673 AA. AC P75078; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MPN_036; GN OrderedLocusNames=MPN_036; ORFNames=B01_orf666, MP118; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75502:MPN_275; NbExp=1; IntAct=EBI-2260490, EBI-2260703; CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95766.1; -; Genomic_DNA. DR PIR; S73444; S73444. DR RefSeq; NP_109724.1; NC_000912.1. DR RefSeq; WP_010874393.1; NC_000912.1. DR IntAct; P75078; 1. DR EnsemblBacteria; AAB95766; AAB95766; MPN_036. DR GeneID; 877269; -. DR KEGG; mpn:MPN036; -. DR PATRIC; 20021347; VBIMycPne110_0035. DR OMA; LHNLERQ; -. DR OrthoDB; EOG6Z0QJK; -. DR BioCyc; MPNE272634:GJ6Z-38-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 673 Uncharacterized protein MPN_036. FT /FTId=PRO_0000215248. SQ SEQUENCE 673 AA; 76630 MW; 9C004DFDC3C15F8E CRC64; MKTLHKLLLG LFLPAILGPL FGLLVTKTDA ESPVAALHKS KSFSKNLDSF RALFVGEDIE EQLAKVQQQT PEVSFASFQQ KFPDKASLRN GFQPIDVYNF LSGWKGALEN FLAKVVELQK KIKAADDIFP NQKKNPDKKD NPNVLEVLGE YGGDGFFPTL GNNGLNIPDQ VFQSFNNFQI ENYKISDFKV DIASERDIVQ HDKFRFSYVV NIGLELALLV NKRPVYFNFS LDLRTNNFSN QAGFNEIFNA PGNAATNWQF FSKVKVKQLN YDGNDSTHLA NTLLQDQFNT LNLNLQKSIY ELPLTEMETK FQQEYVELLL AKRREEKRLW DEEQKRIEAE RKQKEAELAR IQRELKEKAE KDAAVKQAQT NLKTALSSVE GFVKFWTEGE DRIKLGFTKE DNLYTRAGLV KALKISFANY RAWTFYITLL GWKAGSEKLL RKTSWTNLLS DVNFQNAFGL KNTASEEQVG KTSLPGYGYY GIRMSNWLRW ALGYYANTHV GSPQNVKATI DGNPSDTTKV WIAPEDFKQG VHIGVGEHFK GKAYKFKFEV SFELEGSIAA HWWTLALRGN IPGYWKGKLQ VTHTFDGDVP SWYYGSVHTH APEYRFTEDN KLLFVPHSIQ KITAVGGDSN GVNGLLKSQN LHNLERQSYE VTAPIDLVSY LMFAIAKEPT NNW // ID Y047_MYCPN Reviewed; 451 AA. AC P75067; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MG037 homolog; GN OrderedLocusNames=MPN_047; ORFNames=D09_orf451, MP107; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the NAPRTase 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; U00089; AAB95755.1; -; Genomic_DNA. DR PIR; S73433; S73433. DR RefSeq; NP_109735.1; NC_000912.1. DR RefSeq; WP_010874404.1; NC_000912.1. DR ProteinModelPortal; P75067; -. DR IntAct; P75067; 1. DR EnsemblBacteria; AAB95755; AAB95755; MPN_047. DR GeneID; 877412; -. DR KEGG; mpn:MPN047; -. DR PATRIC; 20021371; VBIMycPne110_0047. DR KO; K03462; -. DR OMA; NDHELAN; -. DR OrthoDB; EOG6P06VT; -. DR BioCyc; MPNE272634:GJ6Z-49-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR016471; Nicotinamide_PRibTrfase. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR PANTHER; PTHR11098; PTHR11098; 1. DR Pfam; PF04095; NAPRTase; 1. DR PIRSF; PIRSF005943; NMPRT; 1. DR SUPFAM; SSF51690; SSF51690; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 451 Uncharacterized protein MG037 homolog. FT /FTId=PRO_0000205860. SQ SEQUENCE 451 AA; 51103 MW; C1FE0AF6896FAB45 CRC64; MVQTPSEINT HLKHLLACDA YKLSHRLMYP NDTTNLYSCL TARGGRGGFP NFVWNHEFAK KIILEVFGNF CDSVLAVQND PGLAQALTDK VTTVFGDPQF GLEFTQHICY LANFLKQHHQ LPLTVKIHQS SEGLAFRTPL VTITGSDQMV PELVWLVNYF ETVLLENIWL YQTTLTVAQS LKLLLERYAN ETADNTEFTH FQCHDFSMRG MSSLQSALYV ANAHLQYFSG SDTILGGVAA KSILASEHSV MCADGQEGEL NTFKRLLEQF PNKNLSLVID SYDMWHVLDN ILPQLKDLVL QRQEKLYLRP DSGNFETLIC QGKRFNPEDK TTWGVIDYLD YHFGSTVNQK GYKVLNQKLG IVYGDGITYE RIEYILEQLK QRGFCSSNIV FGVGSTTYQN LNRDTLGFVY KLTAIKKGNT WHDVTKSPIT DPTKQSIGGR FDNPNLIQVY G // ID Y048_MYCPN Reviewed; 518 AA. AC P75066; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MPN_048; GN OrderedLocusNames=MPN_048; ORFNames=D09_orf518, MP106; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P78003:metK; NbExp=1; IntAct=EBI-2259927, EBI-2258805; CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95754.1; -; Genomic_DNA. DR PIR; S73432; S73432. DR RefSeq; NP_109736.1; NC_000912.1. DR RefSeq; WP_010874405.1; NC_000912.1. DR IntAct; P75066; 2. DR EnsemblBacteria; AAB95754; AAB95754; MPN_048. DR GeneID; 877173; -. DR KEGG; mpn:MPN048; -. DR PATRIC; 20021373; VBIMycPne110_0048. DR OMA; NNIFPVE; -. DR OrthoDB; EOG6RVG4C; -. DR BioCyc; MPNE272634:GJ6Z-50-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 518 Uncharacterized protein MPN_048. FT /FTId=PRO_0000215252. SQ SEQUENCE 518 AA; 58873 MW; A0D753FC77DC22EC CRC64; MNELQTKVNE ANNIFPVEAF KVPKVPEKLF GFVNQGFFPK LNPKGLNIAD NVASLFEQYS LKQASLKDFD ILLEKKNDIV LEHKVRYNFA LQFHFETTYV GTGGEINLQF ALQASTTNFS SLEELQASFS KTGDNLTAQL FWKPTVTKLV SGENDLTHIA QTAIGESLFD SRVDLSASII NSEATLKTAE ATFTTQVLNP FKAEREKALA IKKAEEEKIK KELEEQKKRQ EELSKQQRDK EALQKSLWNF QEFISYWTGQ GKDVKQKEQF IQALEAAFST NWNEVFNLLI AGFRSAIQTY YKDGKADQSQ NAKIAFGEKG IQFPKSGPGL DGIFMSDFLR GNLTGNAHFD LKLKKVEVKN TQGKDAQGND KKASINWQAK QNNFPFRQVN PWDFSFEVEL KYEGSYGLYP GARFLNLFGS LGIPNDWKGE MSVKFVLDGK TPQWIADKPD YPGSLFKFEK NQLKFTPHVK EHVHVENKQF MEKLKSQNLH NLELATGATK PPVVDLASYL HYLILNHK // ID Y049_MYCPN Reviewed; 632 AA. AC P75065; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MPN_049; GN OrderedLocusNames=MPN_049; ORFNames=D09_orf632, MP105; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95753.1; -; Genomic_DNA. DR PIR; S73431; S73431. DR RefSeq; NP_109737.1; NC_000912.1. DR RefSeq; WP_010874406.1; NC_000912.1. DR EnsemblBacteria; AAB95753; AAB95753; MPN_049. DR GeneID; 877309; -. DR KEGG; mpn:MPN049; -. DR PATRIC; 20021375; VBIMycPne110_0049. DR OMA; ISIEWNE; -. DR OrthoDB; EOG6RVG4C; -. DR BioCyc; MPNE272634:GJ6Z-51-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 632 Uncharacterized protein MPN_049. FT /FTId=PRO_0000215253. SQ SEQUENCE 632 AA; 72697 MW; 42CCC0AE709D23F4 CRC64; MRFRYKAFLL TLFASTTTLT GFIIPTLSQH GSSTDPSFVA LRNNSSLSCD GKSRLLEFGN DLGFSKEETD VLAKQKNWEQ NYTNFKKQFE HKLLDPKSFS LTDVYNLFSG FQQSVADTVK LMNELQTQVN KANDIYPVES FQVPKVPQKL FGFVDQGFFP KLNPKGLNIA DNVASLFEKY SLKQATLKDF DIVLEKKNDI VLEHKVRYNF ALQFHFETTY IGSGGEINLQ FALQASTTNF SSLEELQASF SKVGNNLTAQ LFWKPVVNKL TSGENDLTHI AQTAVGESLF DSRVDLTSSI INNEAAIKTT QQQFETEVLA LFKAEREKAL AEYKAEQERI AKELEEQRKE LERLKKEQQN KQELVESLYN VANFVSYWEK RGKDVTDKKQ LIQALKSAFA TNWNEVFQLL TAGMREGIKE YYKHNKPDQS ANAKKAFGQN GLAFPRTGFD GIYMSDWLRG ELRNKGNINL HLKQNETTVK KIRDDISIEW NESKGGIEFH QTYPYWFEFE VNFKYIGGYS LNWWDAIWAK VAGIPGSWKG EMNLKLVIDG EIHKWMVTKP DYPRTFFQFD DQFDKLWFTL HVSQEISVRD ESFMNLLKKQ GLDKLDLRTG STKPPVVDLA SYLHYLILAD KS // ID Y068_MYCPN Reviewed; 125 AA. AC P75048; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MG055 homolog; GN OrderedLocusNames=MPN_068; ORFNames=D09_orf125, MP086; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95734.1; -; Genomic_DNA. DR PIR; S73412; S73412. DR RefSeq; NP_109756.1; NC_000912.1. DR RefSeq; WP_010874425.1; NC_000912.1. DR EnsemblBacteria; AAB95734; AAB95734; MPN_068. DR GeneID; 877320; -. DR KEGG; mpn:MPN068; -. DR PATRIC; 20021415; VBIMycPne110_0069. DR KO; K03073; -. DR OMA; IHELHRQ; -. DR OrthoDB; EOG67433G; -. DR BioCyc; MPNE272634:GJ6Z-70-MONOMER; -. DR Proteomes; UP000000808; 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; IPR005807; SecE_bac. DR TIGRFAMs; TIGR00964; secE_bact; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 125 Uncharacterized protein MG055 homolog. FT /FTId=PRO_0000210398. FT TRANSMEM 92 112 Helical. {ECO:0000255}. SQ SEQUENCE 125 AA; 14458 MW; B5F843C4B4CCC84D CRC64; MEKKKLPFGL KNKEKLTAYN DEKIHELHRQ LKAKIEAKKA KEKQDSKTKD TDKKVDQTPK VKVPFTKKFS NLWFGIDKEV NKIVWVTSKK LITIFLLIVL VSAIMIGIYF GINHLFIALG VFKGK // ID Y081_MYCPN Reviewed; 465 AA. AC P75612; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Putative ABC transporter ATP-binding protein MG065 homolog; GN OrderedLocusNames=MPN_081; ORFNames=MP074, R02_orf465; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95722.1; -; Genomic_DNA. DR PIR; S73400; S73400. DR RefSeq; NP_109769.1; NC_000912.1. DR RefSeq; WP_010874438.1; NC_000912.1. DR ProteinModelPortal; P75612; -. DR IntAct; P75612; 2. DR EnsemblBacteria; AAB95722; AAB95722; MPN_081. DR GeneID; 877115; -. DR KEGG; mpn:MPN081; -. DR PATRIC; 20021445; VBIMycPne110_0083. DR KO; K02003; -. DR OMA; RENIEIG; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-84-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 465 Putative ABC transporter ATP-binding FT protein MG065 homolog. FT /FTId=PRO_0000093240. FT DOMAIN 232 465 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 268 275 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 465 AA; 53512 MW; F8F85014C4A1A25D CRC64; MRYFALTDLT KPTAKFTTDA MELRQISNAY LNQAQAYLQK GLKQLKKDYK NAILYTPKTE YKRFLKWKQT FLQDLNQTQK RFFIVRAQHF SYVLLFNLLD EQVEAVIATF NNFLDEHRLE AQSKQFDLDT AVNELHDYFD QLQKNTAYSE DLPTHLTQKT EQLINARNTQ LTNLLNKIAT TKPPLNKQQR LLASFRNYHE HLFLKNEVKK VTWLNEPRAK KESVTPDEEH IIELKNVYKY ITNGVTTNAV LKGIDLKLKA HDFIVILGPS GSGKTTLLNI ISGMDRPSSG SVVVNGQEMI CMNDRQLTNF RRNYVGYIFQ QYGLLPNLTV RENVEVGANL QRNPDKRINI DELLEAVGMK HLQKKLPNEL SGGQQQRVSI ARAFAKNPLL IFGDEPTGAL DLEMTQIVLK QFLAIKQRYK TTMVIVTHNN LIAQLADLVI YVADGKIQAL QANPNPKQVE DINWI // ID Y087_MYCPN Reviewed; 150 AA. AC P75606; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 04-FEB-2015, entry version 70. DE RecName: Full=Uncharacterized protein MPN_087; GN OrderedLocusNames=MPN_087; ORFNames=MP068, R02_orf150; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_085 central region. {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; U00089; AAB95716.1; -; Genomic_DNA. DR PIR; S73394; S73394. DR RefSeq; NP_109775.1; NC_000912.1. DR RefSeq; WP_010874444.1; NC_000912.1. DR ProteinModelPortal; P75606; -. DR EnsemblBacteria; AAB95716; AAB95716; MPN_087. DR GeneID; 877139; -. DR KEGG; mpn:MPN087; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; MPNE272634:GJ6Z-90-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 150 Uncharacterized protein MPN_087. FT /FTId=PRO_0000210638. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. SQ SEQUENCE 150 AA; 17549 MW; FF60FF60C08809B2 CRC64; MTLIYVPTTL NLIDSFNYSE SIYKWGDYFF RHLESRDFYF SNFGFISLFL LLFVIPTITL TTLGCFLFSY LRFTDINKIK IQIYSLLTVF IFIDVFGLVV SVLFGYLLPL AFDSLPFSVN LTREVFLSLA MIVIFANSVI FTLRQKRNID // ID Y088_MYCPN Reviewed; 101 AA. AC P75605; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Uncharacterized protein MPN_088; GN OrderedLocusNames=MPN_088; ORFNames=MP067, R02_orf101; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95714.1; -; Genomic_DNA. DR PIR; S73393; S73393. DR RefSeq; NP_109776.1; NC_000912.1. DR RefSeq; WP_010874445.1; NC_000912.1. DR EnsemblBacteria; AAB95714; AAB95714; MPN_088. DR GeneID; 877141; -. DR KEGG; mpn:MPN088; -. DR OMA; TEDINTN; -. DR BioCyc; MPNE272634:GJ6Z-91-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 101 Uncharacterized protein MPN_088. FT /FTId=PRO_0000210639. SQ SEQUENCE 101 AA; 11595 MW; E4395AB5E5C6CA4A CRC64; MHWIFKKEPN ISVQQNPTKE NVSDVSMIEI NNLTALERDE KVETEDINTN VIANTYTVQA NVPTAFQTSE TNSNTVTNVP KSPELISIQR LERLKNRYTF L // ID Y093_MYCPN Reviewed; 301 AA. AC P75599; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Putative MgpC-like protein MPN_093; GN OrderedLocusNames=MPN_093; ORFNames=MP061, R02_orf301; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95709.1; -; Genomic_DNA. DR PIR; S73387; S73387. DR EnsemblBacteria; AAB95709; AAB95709; MPN_093. DR PATRIC; 20021461; VBIMycPne110_0091. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-96-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 301 Putative MgpC-like protein MPN_093. FT /FTId=PRO_0000210718. SQ SEQUENCE 301 AA; 32698 MW; 4C22653799F09E09 CRC64; MGSNAVPSLW YWVVGEDQES GRATWWAHTE LNWGTDKQKQ FVENQLGFKD DSNSDSKNSN LKAQGLTQPA YLIAGLDVVA DHLVFAAFKA GAVGYDMSTE NSAATKDQAL AWSTTAGLDS AGGYKALVEN TAGLNGPING LFTLLDSFAY VTPVSGMKGG SQNNEEVQTK YPVKDDSKAS AKIASLINAS PLNSYGDDGV TVFDALGLNF NFKLNEARLP SRTDQLLVYG IVNESELKSA RENAQSTSDA NSNTKVKWTN TASHYLPVPY YYSANFPEVG NRRRAEQRNG VITIKRPSTQ R // ID Y097_MYCPN Reviewed; 541 AA. AC P75595; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MPN_097; DE Flags: Precursor; GN OrderedLocusNames=MPN_097; ORFNames=MP057, R02_orf541; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75216:nadE; NbExp=1; IntAct=EBI-2260341, EBI-2260344; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95705.1; -; Genomic_DNA. DR PIR; S73383; S73383. DR IntAct; P75595; 2. DR EnsemblBacteria; AAB95705; AAB95705; MPN_097. DR PATRIC; 20021481; VBIMycPne110_0098. DR OMA; YAFAGEN; -. DR BioCyc; MPNE272634:GJ6Z-103-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 541 Uncharacterized lipoprotein MPN_097. FT /FTId=PRO_0000018725. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 541 AA; 59153 MW; AD2FCB2B826B1E9C CRC64; MQFKYGALIF SGFLGLSIVL ASCGARGKFD QVDDGKIKLA SSLTSRSASA ALQKVVEKYN KVKGVNDYPI EITQIAGGYD GGRTDLQTRV SVKDKTSFYN MILNYPDLVS VLARNGMELP FDGVNVDKLS PNFLKFNERI SGVAKKANYA IPISMSTDIL ILNAPVLHYI LNSAKKNDGN TKVQVKAQSK DSQTKVKGTM EIGTDESTKN LWSDIQKKAG ENGKATTEGT KKAAAKSTHL TLLTKSEQST QGNNGASESD KKIEETWGTY SEVDGGLKNY TFKADVFDTW HGLIDFSTRV AKSFKNKVSD ISTKKGTDIQ GVLGLDSTPN ALFTSVFAAG DSNFDNFFYK VKDGRADFSN FNENGTSYKN LEKVFNDYKK LTDSNGLFVN KGGSYTSNFQ KFHQLAYSIS SSSGYAYAFA GENSKRLKFN DDTFIEYPSF TQEIHAPGQS SQKEGGQQQS NSKDNGNLLG TFTIEAAKSK TKTEVKKTED TQNQGKKAEG TPNQGKKAEG TENQGKTIFL YKTSIPNDKQ DGVDAVLIKD K // ID Y098_MYCPN Reviewed; 147 AA. AC P75594; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized lipoprotein MPN_098; GN OrderedLocusNames=MPN_098; ORFNames=MP056, R02_orf147; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95704.1; -; Genomic_DNA. DR PIR; S73382; S73382. DR EnsemblBacteria; AAB95704; AAB95704; MPN_098. DR PATRIC; 20021483; VBIMycPne110_0099. DR OMA; TESASYI; -. DR OrthoDB; EOG6JMMQZ; -. DR BioCyc; MPNE272634:GJ6Z-104-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004890; Lipoprotein_10_C. DR Pfam; PF03202; Lipoprotein_10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized lipoprotein MPN_098. FT /FTId=PRO_0000215276. SQ SEQUENCE 147 AA; 16413 MW; CB2ABFBA77430D52 CRC64; MMTQGPNLIG IHTNTKENEE TQKFVNWFLN TSLTWDNNES KTPAQYFTES ASYILPLKET FTGSNNKGQS GKNDGKNSNN TFKAKALELF KEQSENKIVG YSDPSDFRGG KFRESIGSAF NATVNSHVDF NTFVANFRAN LGSGYDK // ID Y107_MYCPN Reviewed; 251 AA. AC P75562; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MPN_107; GN OrderedLocusNames=MPN_107; ORFNames=C09_orf251, MP047; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95695.1; -; Genomic_DNA. DR PIR; S73373; S73373. DR RefSeq; NP_109795.1; NC_000912.1. DR RefSeq; WP_010874464.1; NC_000912.1. DR EnsemblBacteria; AAB95695; AAB95695; MPN_107. DR GeneID; 877226; -. DR KEGG; mpn:MPN107; -. DR PATRIC; 20021511; VBIMycPne110_0113. DR OrthoDB; EOG6S7XXT; -. DR BioCyc; MPNE272634:GJ6Z-113-MONOMER; -. DR Proteomes; UP000000808; 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; Reference proteome. FT CHAIN 1 251 Uncharacterized protein MPN_107. FT /FTId=PRO_0000210646. SQ SEQUENCE 251 AA; 28794 MW; D44D83581F212D0B CRC64; MTNQNLQDFL DGVLLKEENL NKITEVSLEK GLPHLLDEGI HNEDNFQIFT SQKIVADMIK MVGVKEMKNV HTTVLEPTSG DGAFTCAILD LRLKNIKKSD SFLKEALTGL STIYSVEIDE ELVWLQRNNL YSIFLAFLKK HGIFNEELSL LVKKILMINV SWGELITETK DNENFVCNYD YFLRNKKTKK KPAKHKHEFP EGLFSNGEGK CKSLFVNWSF ADVINEIAHN SNFYFAKIAK IPGEIIQFQI N // ID Y128_MYCPN Reviewed; 149 AA. AC P75347; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 07-JAN-2015, entry version 53. DE RecName: Full=Uncharacterized protein MPN_128; GN OrderedLocusNames=MPN_128; ORFNames=C09_ORF149a, MP026; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAB95674.1; -; Genomic_DNA. DR PIR; S73352; S73352. DR EnsemblBacteria; AAB95674; AAB95674; MPN_128. DR PATRIC; 20021563; VBIMycPne110_0138. DR BioCyc; MPNE272634:GJ6Z-135-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 149 Uncharacterized protein MPN_128. FT /FTId=PRO_0000210651. SQ SEQUENCE 149 AA; 15638 MW; 9ADF5E451915638F CRC64; MFGLKVKNAE ADTAKSNEKL QGAEATGSST TSGSGQSTQR GGSSGDTKVK ALQVAVKKKS GSQGNSGDQG TEQVELESND LANAPIKRGS NPASPTQGSR LRHHPIQFGI WSIRHPHPLK AVACDRANSQ GPPQMIRLDP HSVRCALCL // ID Y133_MYCPN Reviewed; 301 AA. AC P75265; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Uncharacterized lipoprotein MG186 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_133; ORFNames=E07_orf301, MP021; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 TNase-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00272}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95669.1; -; Genomic_DNA. DR PIR; S73347; S73347. DR RefSeq; NP_109821.1; NC_000912.1. DR RefSeq; WP_010874490.1; NC_000912.1. DR ProteinModelPortal; P75265; -. DR IntAct; P75265; 1. DR EnsemblBacteria; AAB95669; AAB95669; MPN_133. DR GeneID; 877227; -. DR KEGG; mpn:MPN133; -. DR PATRIC; 20021581; VBIMycPne110_0147. DR KO; K02027; -. DR OMA; NAKINIW; -. DR OrthoDB; EOG6HF5WJ; -. DR BioCyc; MPNE272634:GJ6Z-140-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.90; -; 2. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR SMART; SM00318; SNc; 1. DR SUPFAM; SSF50199; SSF50199; 2. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS50830; TNASE_3; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Endonuclease; Hydrolase; KW Lipoprotein; Membrane; Nuclease; Palmitate; Reference proteome; KW Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 301 Uncharacterized lipoprotein MG186 FT homolog. FT /FTId=PRO_0000034399. FT DOMAIN 46 243 TNase-like. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 301 AA; 33218 MW; 153C8A774CB3AEFB CRC64; MKGFSCSRPG YLTGLLLLAV APILTACTRD YTTKNEFQLT TAQQAKLKPA TIEYWRDGDT PEINYASEER RKEAEQKSKE NAKKEDKKEE KKTEDSQDSS SASTQVRSSK HGLRIYGIDT PEKHVSSKGD STGDEKIEAE KASNYAEKLI PKGSTVWVWS LNTYSYDREV GALFFKSNPK QTFFQSFEVA MVEAGHAIPI AGTGLNLIAD PELSADDPLS VIGLQLANAA NKAYNAKINI WSHDTDGYRS LTAVYKLRGA DISWTRFLDE ANGYSSASAG TGASLYQLWD QRQAKLAQKG S // ID Y198_MYCPN Reviewed; 319 AA. AC Q50290; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized adenine-specific methylase MPN_198; DE EC=2.1.1.72; DE AltName: Full=M.MpnIP; GN OrderedLocusNames=MPN_198; ORFNames=GT9_orf319V, MP633; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase 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; U34795; AAC43683.1; -; Genomic_DNA. DR EMBL; U00089; AAB96281.1; -; Genomic_DNA. DR PIR; S62810; S62810. DR RefSeq; NP_109886.1; NC_000912.1. DR RefSeq; WP_010874555.1; NC_000912.1. DR REBASE; 6710; M.MpnI. DR EnsemblBacteria; AAB96281; AAB96281; MPN_198. DR GeneID; 876831; -. DR KEGG; mpn:MPN198; -. DR PATRIC; 20021719; VBIMycPne110_0216. DR KO; K00571; -. DR OMA; PNNCLWL; -. DR OrthoDB; EOG60CWHX; -. DR BioCyc; MPNE272634:GJ6Z-205-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR025247; EcoRI_methylase. DR Pfam; PF13651; EcoRI_methylase; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 319 Uncharacterized adenine-specific FT methylase MPN_198. FT /FTId=PRO_0000088018. SQ SEQUENCE 319 AA; 36870 MW; C665CA40A958A78B CRC64; MHYFNRAKKA KNNEFYTLFE DIAAEVACYP NAFKGKVVLC NCNDGYQSNF WQFFQSQFHA LGLKKLVAIA FNPLGNSYQL NFDGKEIKEL PLAGNGSFDS AEAIVLLKQS DIVVTNPPFS LFQDFVCLLA EHGKQFLVLG HNGAVGYNQI FKLFKEEQLW YGHTVNSSML FQVQSNFKLY DPKSVNFVKK DGQLFQKVPG ISWFTNLKKN QQPAWLKTKS RYQGNEHKYP KFDWYDAIFV SKVKEIPLDW FGYMGVPLTF LNCFNPKQFE LIDCLANPYA TLDTLKTNAY VRSHHGDVRN VKGKRRYVRV VIKQRQNVI // ID Y204_MYCPN Reviewed; 148 AA. AC P75572; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=UPF0134 protein MPN_204; GN OrderedLocusNames=MPN_204; ORFNames=GT9_orf148, MP627; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96275.1; -; Genomic_DNA. DR PIR; S73953; S73953. DR RefSeq; NP_109892.1; NC_000912.1. DR RefSeq; WP_010874561.1; NC_000912.1. DR ProteinModelPortal; P75572; -. DR IntAct; P75572; 2. DR EnsemblBacteria; AAB96275; AAB96275; MPN_204. DR GeneID; 876970; -. DR KEGG; mpn:MPN204; -. DR PATRIC; 20021735; VBIMycPne110_0224. DR OMA; NEKEFHE; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-211-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 148 UPF0134 protein MPN_204. FT /FTId=PRO_0000221603. SQ SEQUENCE 148 AA; 17298 MW; CB528054C812BD6A CRC64; MKEKTPFKNE KEFHEMVKKT KKGTFSGWYI IDKDNNSVEF SGKFNRQFKL NKPVITVNTE YVTRKELNEY KDSNDQRLTK IETTLAAQGE QINKLTQTVE KQGEQIRELQ VEQKAQGEQI KAQGETLKLI LQTLQKMSDR LDKIDPSK // ID Y241_MYCPN Reviewed; 280 AA. AC P75530; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG103 homolog; GN OrderedLocusNames=MPN_241; ORFNames=K04_orf280, MP590; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96238.1; -; Genomic_DNA. DR PIR; S73916; S73916. DR RefSeq; NP_109929.1; NC_000912.1. DR RefSeq; WP_010874598.1; NC_000912.1. DR IntAct; P75530; 1. DR EnsemblBacteria; AAB96238; AAB96238; MPN_241. DR GeneID; 877264; -. DR KEGG; mpn:MPN241; -. DR PATRIC; 20021807; VBIMycPne110_0260. DR KO; K09762; -. DR OMA; NEYDFNF; -. DR OrthoDB; EOG68WR87; -. DR BioCyc; MPNE272634:GJ6Z-248-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR023054; Sporulation_regulator_WhiA_C. DR Pfam; PF02650; HTH_WhiA; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 280 Uncharacterized protein MG103 homolog. FT /FTId=PRO_0000210416. SQ SEQUENCE 280 AA; 32194 MW; 5B42DB3CBFC26AAA CRC64; MSFSVQIKHE LATNPLIKTE WSSFLAGYFQ NGLKLLATGQ WSFKTSTATL KALFSNALQF SFQIHETSTH CEFSFRASQT EVDQLLAFDA TQSDLPLQKA YVIGAFLSGG SVSDLLHSSN FHLQISTNNE LQIKQLMKLF HPFKQTTKRH QLLVYVKSYQ AICDFFKLVE AFDGYLAFEE NQLQKNFALE QVRKSNLEIA NLMRTLKTST STAEQLKILI NSADFKKQSL NFQRFCLVKL DHPDWSLEQI AQFFERKYKV QITRSGIQHL NAKLKKLNQN // ID Y274_MYCPN Reviewed; 266 AA. AC P75503; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MG133 homolog; GN OrderedLocusNames=MPN_274; ORFNames=A65_orf266, MP561; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96209.1; -; Genomic_DNA. DR PIR; S73887; S73887. DR RefSeq; NP_109962.1; NC_000912.1. DR RefSeq; WP_010874631.1; NC_000912.1. DR ProteinModelPortal; P75503; -. DR EnsemblBacteria; AAB96209; AAB96209; MPN_274. DR GeneID; 876855; -. DR KEGG; mpn:MPN274; -. DR PATRIC; 20021875; VBIMycPne110_0294. DR OMA; INDWNAF; -. DR OrthoDB; EOG6423CJ; -. DR BioCyc; MPNE272634:GJ6Z-281-MONOMER; -. DR Proteomes; UP000000808; 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; IPR011631; DUF1600. DR Pfam; PF07667; DUF1600; 1. DR PIRSF; PIRSF006834; UCP006834; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 266 Uncharacterized protein MG133 homolog. FT /FTId=PRO_0000210435. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 232 252 Helical. {ECO:0000255}. SQ SEQUENCE 266 AA; 31214 MW; 3A9AEB091B1FB238 CRC64; MKKTIGLAYR FFYLNNNCDF YLLFLAPFSL FNLGVMVASA VISVVYNNQP QLIWFTNFDT FTYQSNTIAA VCVLMYLCKR RCKLFDNNAL FLSAAGYLVF TVIFFNLYVL SRVTGFVNVE EHVKGWFSTI TSEMPYSFSG NPLTDWISFA QLFLHVIYPA SFFGFIWIFF KTYKMREPLH ELGKFLLKAG VYPSLYAFYL QTVPFLKIWD NGHDSYSVYG FFSQTKYNSY VWFWSIPIFA SMFLILWGLF VINNRYYGAK TKYGKQ // ID Y281_MYCPN Reviewed; 377 AA. AC P75496; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MPN_281; DE Flags: Precursor; GN OrderedLocusNames=MPN_281; ORFNames=A65_orf377, MP554; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96202.1; -; Genomic_DNA. DR PIR; S73880; S73880. DR IntAct; P75496; 1. DR EnsemblBacteria; AAB96202; AAB96202; MPN_281. DR PATRIC; 20021889; VBIMycPne110_0301. DR OMA; ANGETNQ; -. DR BioCyc; MPNE272634:GJ6Z-288-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 377 Uncharacterized lipoprotein MPN_281. FT /FTId=PRO_0000018729. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 377 AA; 41454 MW; 8C6A7C6EE34818B5 CRC64; MKFKYGTVVL GSFLGLSVVL AACGARGKFD QFDDGKIKLA SSLTSKAAAN ALQTIIEKYN IVKSGKDYPI EITQIAGGYD GGRTDLQTRV SVKDKTNFYN LILNYPDLVS VLARSGMELL FDKVNVDKLE PNFLKFNEQI SGVAKSGNYG IPVSLSTDIL VLNGPVLHYI LNSAKKEEAN SQVKSQIKTS QIQAKGSLTI DTDENTKSLW EKIQNSAKAN GETNQKGRKA AKSNKTALVQ LKNGADTTTN EENKDTKTSD DKVKQTWGDY VEKDDGLKNY TFRASVFENW HDFLDFSTRV AKSFTEKVSN ITNKKGTDIQ GVLGVDSSPN VLFASVFAAG GGNYENFFYK LKDGRADFSN FKNKGSSYQN LQSVFKD // ID Y283_MYCPN Reviewed; 115 AA. AC P75494; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=UPF0134 protein MPN_283; GN OrderedLocusNames=MPN_283; ORFNames=A65_orf115, MP552; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75344:dnaK; NbExp=1; IntAct=EBI-2262486, EBI-2258839; CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96200.1; -; Genomic_DNA. DR PIR; S73878; S73878. DR RefSeq; NP_109971.1; NC_000912.1. DR RefSeq; WP_010874640.1; NC_000912.1. DR ProteinModelPortal; P75494; -. DR IntAct; P75494; 3. DR EnsemblBacteria; AAB96200; AAB96200; MPN_283. DR GeneID; 877089; -. DR KEGG; mpn:MPN283; -. DR PATRIC; 20021897; VBIMycPne110_0305. DR OMA; QGEQIKS; -. DR BioCyc; MPNE272634:GJ6Z-290-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 115 UPF0134 protein MPN_283. FT /FTId=PRO_0000221604. SQ SEQUENCE 115 AA; 13260 MW; 38E6CB133DDC04F2 CRC64; MKEKISKKEY NALIRKTGEK HFDGEKEEYG DGTVGLWTYE LRKYKLKPPV KVKYVTQEEF GEFKDATNQR LTKIENALVA QGEQIRAQGE QLSQLIKVVL LQGEQIKSQG EQIKS // ID Y288_MYCPN Reviewed; 787 AA. AC P75489; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized lipoprotein MPN_288; DE Flags: Precursor; GN OrderedLocusNames=MPN_288; ORFNames=A65_orf787o, MP547; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96195.1; -; Genomic_DNA. DR PIR; S73873; S73873. DR RefSeq; NP_109976.1; NC_000912.1. DR RefSeq; WP_010874645.1; NC_000912.1. DR EnsemblBacteria; AAB96195; AAB96195; MPN_288. DR GeneID; 876803; -. DR KEGG; mpn:MPN288; -. DR PATRIC; 20021911; VBIMycPne110_0312. DR OMA; NTESWEV; -. DR OrthoDB; EOG6JMMQZ; -. DR BioCyc; MPNE272634:GJ6Z-295-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 787 Uncharacterized lipoprotein MPN_288. FT /FTId=PRO_0000018731. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 787 AA; 86890 MW; FFA8237DD18D3A05 CRC64; MKFKYCAIFF SGFLGLSAIL AACGARGKFD QVDDGKIKLA FSLTSKSASN ALQAIVKKYN EVKKPGDYHI EITQIAGGYD GGRSDLQTRV NVKDTTNFYN LILNYPDLVS TLGRVGMELL FDKVNTDKLS DRFLDFNKRI SAISKPGIYG IPVSLSTEVL SINGPVLHYI LKSAKGDSDN VKVSQRTGET TQKSKVTNPL KINTQNDPAT KDLWEKIEAS AKANGKSNKD GQTKGKKKVE KSSSSSLVNL KQSTDQTTTD DGSQKSDNKI KESWGEYQEV DGGLKNFEFK ASIFENWHDL LDFSTRVAKS FTNVKGKDIK KGTDIQGVLG VDSTPNSLFT SVFAAGGGDY NNFFYKIENG RADFSNFKNK GTSYQNLQKV FGDFKGLIDK NGIFVNKGGS YSSNFQKFHQ LAYSISSTSG FFYSFAGNSA KRLKFGDNFI EFPRFTQEIK APSTENGGQS NLLGTFEVKD SSKSKEVKKT NRKEDGAQNQ GKKESDKKTI YLYKSQIPSD KTEGENAILI KEQNVINQLE QAAKKDEKGE TVTNKVASLE TKAANAKKDS SKTIIGYTTT DNVHEDGKNI FKINKLKTED YDRKIIVGAT EEVLEQSSTL QSDEAIVLPA PGKYQSGDAK KVTITQGPNI IGIHANEKEN AETQKFVNWF LNNTESWEVK NGKDSSTKQQ TAAEFFAESA SYILPLKEIF DKDNKKATEN KDNNTSNKKQ ANTYAEKALD LFQQISKGDI VSYSDPSDFR SGKFRDGIGS NFNAAVSSKA DFDRFVKGFI ATLGSEI // ID Y291_MYCPN Reviewed; 196 AA. AC P75486; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MG208 homolog; GN OrderedLocusNames=MPN_291; ORFNames=H10_orf196, MP544; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96192.1; -; Genomic_DNA. DR PIR; S73870; S73870. DR RefSeq; NP_109979.1; NC_000912.1. DR RefSeq; WP_010874648.1; NC_000912.1. DR ProteinModelPortal; P75486; -. DR EnsemblBacteria; AAB96192; AAB96192; MPN_291. DR GeneID; 877347; -. DR KEGG; mpn:MPN291; -. DR PATRIC; 20021917; VBIMycPne110_0315. DR OMA; FVKLCKA; -. DR OrthoDB; EOG647TXQ; -. DR BioCyc; MPNE272634:GJ6Z-298-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022496; T6A_YeaZ. DR Pfam; PF00814; Peptidase_M22; 1. DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 196 Uncharacterized protein MG208 homolog. FT /FTId=PRO_0000210455. SQ SEQUENCE 196 AA; 22464 MW; E8E554512BC381BF CRC64; MRFFNKYKLF LDCAYKHLNI VLLDFKTNTV VDQLTIPVQQ NLTELAVYHL EKLLKKNKVR NNTVRQFYVT TGPGSFTGQR VGAIIAKTWC TVNPNCQLFA LNSLRLQIPY GCGISKISAG NEKNYCGLFT ETTSEIALLA KPDFVKLCKA NTELPVYENF ENIDSIEELF LNNIERFELV ENPQNLELLY LKDPVN // ID Y297_MYCPN Reviewed; 149 AA. AC P75481; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MG211 homolog; GN OrderedLocusNames=MPN_297; ORFNames=H10_orf149, MP539; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96187.1; -; Genomic_DNA. DR PIR; S73865; S73865. DR RefSeq; NP_109985.1; NC_000912.1. DR RefSeq; WP_010874654.1; NC_000912.1. DR IntAct; P75481; 1. DR EnsemblBacteria; AAB96187; AAB96187; MPN_297. DR GeneID; 876782; -. DR KEGG; mpn:MPN297; -. DR PATRIC; 20021929; VBIMycPne110_0321. DR OMA; NNEGEYD; -. DR OrthoDB; EOG6ZWJKD; -. DR BioCyc; MPNE272634:GJ6Z-304-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR019933; DivIVA_domain. DR TIGRFAMs; TIGR03544; DivI1A_domain; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 149 Uncharacterized protein MG211 homolog. FT /FTId=PRO_0000210459. SQ SEQUENCE 149 AA; 17765 MW; 708D806367801C49 CRC64; MDNDKKDKII LSGELTNHRF NFTKDGENGY SAYEVDRFLD QLVHTLTHYE AQRNREEEMK TAYEKLFQDR DEILKRCSKL EAELNNFYEN GYSNRVLISR VQALENKIES LPSGQNDRLE RIEKLLKRVI KHWTDGEDLS YGDFDDDFF // ID Y330_MYCPN Reviewed; 294 AA. AC P75455; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Uncharacterized protein MG237 homolog; GN OrderedLocusNames=MPN_330; ORFNames=F10_orf294, MP506; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96154.1; -; Genomic_DNA. DR PIR; S73832; S73832. DR RefSeq; NP_110018.1; NC_000912.1. DR RefSeq; WP_010874686.1; NC_000912.1. DR PDB; 1TD6; X-ray; 2.50 A; A=1-294. DR PDBsum; 1TD6; -. DR ProteinModelPortal; P75455; -. DR SMR; P75455; 5-290. DR EnsemblBacteria; AAB96154; AAB96154; MPN_330. DR GeneID; 876968; -. DR KEGG; mpn:MPN330; -. DR PATRIC; 20022014; VBIMycPne110_0354. DR OMA; SELANDQ; -. DR OrthoDB; EOG66MQNX; -. DR BioCyc; MPNE272634:GJ6Z-347-MONOMER; -. DR EvolutionaryTrace; P75455; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 1.10.472.40; -; 1. DR Gene3D; 1.20.1480.10; -; 1. DR Gene3D; 3.30.1790.10; -; 1. DR InterPro; IPR024503; DUF3196. DR InterPro; IPR023344; Uncharacterised_MG237_C. DR InterPro; IPR023402; Uncharacterised_MG237_central. DR InterPro; IPR023403; Uncharacterised_MG237_N. DR Pfam; PF11428; DUF3196; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 294 Uncharacterized protein MG237 homolog. FT /FTId=PRO_0000210476. FT HELIX 22 33 {ECO:0000244|PDB:1TD6}. FT TURN 34 36 {ECO:0000244|PDB:1TD6}. FT HELIX 40 56 {ECO:0000244|PDB:1TD6}. FT HELIX 60 70 {ECO:0000244|PDB:1TD6}. FT HELIX 78 99 {ECO:0000244|PDB:1TD6}. FT HELIX 101 105 {ECO:0000244|PDB:1TD6}. FT HELIX 108 116 {ECO:0000244|PDB:1TD6}. FT TURN 117 122 {ECO:0000244|PDB:1TD6}. FT HELIX 123 128 {ECO:0000244|PDB:1TD6}. FT HELIX 139 144 {ECO:0000244|PDB:1TD6}. FT HELIX 146 149 {ECO:0000244|PDB:1TD6}. FT HELIX 156 166 {ECO:0000244|PDB:1TD6}. FT HELIX 170 172 {ECO:0000244|PDB:1TD6}. FT STRAND 176 181 {ECO:0000244|PDB:1TD6}. FT TURN 182 185 {ECO:0000244|PDB:1TD6}. FT STRAND 186 191 {ECO:0000244|PDB:1TD6}. FT STRAND 194 197 {ECO:0000244|PDB:1TD6}. FT HELIX 201 217 {ECO:0000244|PDB:1TD6}. FT HELIX 222 238 {ECO:0000244|PDB:1TD6}. FT TURN 239 241 {ECO:0000244|PDB:1TD6}. FT HELIX 248 262 {ECO:0000244|PDB:1TD6}. FT STRAND 263 265 {ECO:0000244|PDB:1TD6}. FT HELIX 272 281 {ECO:0000244|PDB:1TD6}. FT TURN 282 284 {ECO:0000244|PDB:1TD6}. SQ SEQUENCE 294 AA; 34135 MW; DB9F1896E24073AC CRC64; MINKPNQFVN HLSALKKHFA SYKELREAFN DYHKHNGDEL TTFFLHQFDK VMELVKQKDF KTAQSRCEEE LAAPYLPKPL VSFFQSLLQL VNHDLLEQQN AALASLPAAK IIELVLQDYP NKLNMIHYLL PKTKAFVKPH LLQRLQFVLT DSELLELKRF SFFQALNQIP GFQGEQVEYF NSKLKQKFTL TLGEFEIAQQ PDAKAYFEQL ITQIQQLFLK EPVNAEFANE IIDAFLVSYF PLHPPVPLAQ LAAKIYEYVS QIVLNEAVNL KDELIKLIVH TLYEQLDRPV GDEN // ID Y334_MYCPN Reviewed; 326 AA. AC P75444; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Putative ABC transporter ATP-binding protein MPN_334; GN OrderedLocusNames=MPN_334; ORFNames=F10_orf326, MP502; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96150.1; -; Genomic_DNA. DR PIR; S73828; S73828. DR RefSeq; NP_110022.1; NC_000912.1. DR RefSeq; WP_010874690.1; NC_000912.1. DR ProteinModelPortal; P75444; -. DR EnsemblBacteria; AAB96150; AAB96150; MPN_334. DR GeneID; 876729; -. DR KEGG; mpn:MPN334; -. DR PATRIC; 20022022; VBIMycPne110_0358. DR KO; K01990; -. DR OMA; NTHEYLY; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; MPNE272634:GJ6Z-351-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 326 Putative ABC transporter ATP-binding FT protein MPN_334. FT /FTId=PRO_0000093253. FT DOMAIN 7 239 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 42 49 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 326 AA; 37885 MW; 09943C12ACF1399B CRC64; MSVTPIVEVK HLEKEFGFWR KNRILKDVNF AIMPGEFHAF IGQNGAGKTT TIKCLISSYQ RFKDEINIDG ISNKNAKSKG VISYIPEYAV FPKHLNTHEY LYTLGKLSGC SLQTIKEKVD YWLARFQIEH LRFKKPNDFS SGQKKKVLLI QALFNDPKLL IMDEPTANLD PKTRNEFMDV CYELNVRNKM AVFVSSHILA ELENYCDSLT VIHEGEILFN GKTKNIAKDN FGYRLKVNNS DSLRKWLKAQ KIAYKYFPAT DDFQVDLKQK QSNKFAVELY QQPDFEVFIF ARQGNSLQNI YNNLIEQYEY DQVQRAVAIR EQDEAV // ID Y335_MYCPN Reviewed; 741 AA. AC P75443; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MPN_335; GN OrderedLocusNames=MPN_335; ORFNames=F10_orf741, MP501; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_333. {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; U00089; AAB96149.1; -; Genomic_DNA. DR PIR; S73827; S73827. DR RefSeq; NP_110023.1; NC_000912.1. DR RefSeq; WP_010874691.1; NC_000912.1. DR EnsemblBacteria; AAB96149; AAB96149; MPN_335. DR GeneID; 877324; -. DR KEGG; mpn:MPN335; -. DR PATRIC; 20022024; VBIMycPne110_0359. DR KO; K01992; -. DR OMA; FFINTHN; -. DR OrthoDB; EOG6JTC77; -. DR BioCyc; MPNE272634:GJ6Z-352-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 741 Uncharacterized protein MPN_335. FT /FTId=PRO_0000210662. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TRANSMEM 655 675 Helical. {ECO:0000255}. FT TRANSMEM 715 735 Helical. {ECO:0000255}. SQ SEQUENCE 741 AA; 85026 MW; 1776A96BCF83567F CRC64; MKLFKNWSDV NNVKQRQLLL AYFRFILKQI VKSWLLWVTA GLVLFLLALV LLIIPAFTKQ DPLFLWSHPV VQMSSLIIPF IALFATIITF QVFINGYYNG LEILLITRFF TRGRLFFARL AVLFIWITGT AFLSGLFVSL TATLGATSQT VTDLVLSVFF GVLLLSLLFS CVLIIIAQFL NRTQSMLLLL LGVSLASFTT VILAFSIKPP SENLRDNGYQ PLNLSLISKS KSKSVENVFT IIDSSNVSDP RNKKKSIVKT NPQAIWDEYG ESSFFQSQYY WNVGYWINSL FRLNSLSDYR NFDVNLYFLN TKLNFDREVD TDKMVDFVSF RDQRHLYFLS YSFFINTHNL PTQPLPRILT YDNNGAFLEK IVPSFDDIKL DPPRVKKVYK FFSDTIIQSF RDYEAEEKER QEKEEKEKAE KDNGNGQDSN KVNSVSTEPN NKNSSDADSK DNNDSSDSQG KDSSKSKPKF RPRLPQFFDR VSINYSKFSS SFNTQLKHIH QGLSTRDEAM EIFKDKVALF YALSMAYDNF TFQKDSGIID NTSLNKFKTE FNKKQKELTE KNKQKQDGKD QKSQRMTQGA DKAVTVEPKA MQSEIGMTDQ TNDQSSSETK DSMDSSDSSD TVDNTDESED KQSEEEEKFD EEIENAKKMP KAEDAFFNTA SIWLSSPFLF FENGAKREQR YEIHLLNSNT QVNNEIIKTN SFYYVSGEPI VGQEVIIAMV LVVTLGLLVG SFFAYQKRDI K // ID Y364_MYCPN Reviewed; 677 AA. AC P75417; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MPN_364; GN OrderedLocusNames=MPN_364; ORFNames=H91_orf677, MP472; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96120.1; -; Genomic_DNA. DR PIR; S73798; S73798. DR RefSeq; NP_110052.1; NC_000912.1. DR RefSeq; WP_010874720.1; NC_000912.1. DR EnsemblBacteria; AAB96120; AAB96120; MPN_364. DR GeneID; 876897; -. DR KEGG; mpn:MPN364; -. DR PATRIC; 20022094; VBIMycPne110_0391. DR OMA; ENWHELL; -. DR BioCyc; MPNE272634:GJ6Z-384-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 677 Uncharacterized protein MPN_364. FT /FTId=PRO_0000215280. SQ SEQUENCE 677 AA; 75592 MW; E785B68BD679F04D CRC64; MELPLDNVDL SKLSPNFLKF NERISGVAKK ANYAIPVSLS TEVLALNGPV LHYILNSAKG GNETAVTQRT ASTNQQNTLQ NSLKINESDP ITKELWEKIQ KAAETNGKAK EQGKSKKQGT EKTTTLTLLK TESSQQSNTT KDGKATSDEA IKKTWGDYQK VENGLKGYTF KASVFENWHE LLDFSARIAR SFTNIHTKET KKGTDIQGVL GIDSTPNALF TSVFAAGGGN YDNFFYKVQD GRADFSNFKN KETSYQNLQK VFSDYKELID KNGLFVNKGG SYSSNFQKFH QLAYSISSTS GFFYSFAGNS AKRLKFDDGN FIEFPRFTQP VKAPNKTTQS GGENNNKSEN NLLGTFEIED KSKKRESVES SEKSSSGTQS KSKKGKSMKT IYLYKAQIPE GKNKGDNAIL ITNQTVIDKL EKAAKEDGKS GTQVSTIASK STTKENQENK IIGYTSTDNL REDNKNIFDI DDLNDEKYDR KIIVSATEEV LEQSNTLQSE EAVVLPAPAK YKASDSTKIA ITQEPNLIGI HANEKENEET RKFVNWFLNS EQTWESKKYS KNKQNSNEKR TPAQFFADSA SYILPLKKTF DNANKKEDQS KANNKTNSQR TNTYIEKALE IFKGISQNQI TSYSDPSDFR SGRFRDGIGS NFNAVVNSKV DFNKFINNFI ASLGSDI // ID Y371_MYCPN Reviewed; 211 AA. AC P75410; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 52. DE RecName: Full=Uncharacterized protein MPN_371; GN OrderedLocusNames=MPN_371; ORFNames=A19_orf211, MP465; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96113.1; -; Genomic_DNA. DR PIR; S73791; S73791. DR EnsemblBacteria; AAB96113; AAB96113; MPN_371. DR BioCyc; MPNE272634:GJ6Z-391-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 211 Uncharacterized protein MPN_371. FT /FTId=PRO_0000210664. SQ SEQUENCE 211 AA; 23592 MW; A5E240288852DDB2 CRC64; MRIEAANLAG SLWICSVVNH GVQGVGVPSW VPDPELEGAV PKSSALSWTC WLLLEPRLIG ALARLLVSSS IWPLSSESDF FFTATCNALT LVSPDEPHVG WIGQIQMWLK NQWPQRPGVF HCSSRCPPRR SSPSSQTLPR WWKYFDHSRF AAVVSPTPFA TAHSTPRCAA RVKRQTGRDW RGLAPPRRGP CFWPRFTVGV QPHSNQSRQR G // ID Y386_MYCPN Reviewed; 229 AA. AC P75396; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MG268 homolog; GN OrderedLocusNames=MPN_386; ORFNames=F11_orf229, MP451; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96099.1; -; Genomic_DNA. DR PIR; S73777; S73777. DR RefSeq; NP_110074.1; NC_000912.1. DR RefSeq; WP_010874742.1; NC_000912.1. DR ProteinModelPortal; P75396; -. DR IntAct; P75396; 1. DR EnsemblBacteria; AAB96099; AAB96099; MPN_386. DR GeneID; 877095; -. DR KEGG; mpn:MPN386; -. DR PATRIC; 20022148; VBIMycPne110_0417. DR OMA; YIVENHS; -. DR OrthoDB; EOG6423DZ; -. DR BioCyc; MPNE272634:GJ6Z-407-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019206; F:nucleoside kinase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002624; DCK/DGK. DR InterPro; IPR031314; DNK_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01712; dNK; 1. DR PIRSF; PIRSF000705; DNK; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 229 Uncharacterized protein MG268 homolog. FT /FTId=PRO_0000210497. FT NP_BIND 22 29 ATP. {ECO:0000255}. SQ SEQUENCE 229 AA; 27020 MW; 97A17C27F9D25425 CRC64; MKTPLKPKFQ PAKIANAVVV GGMIAFGKTT IAESLAKHLK GSKVIYELEE QDQLADLLLA KMYERNDELL YAPLFQLYFT LNRFNKYRKE CNNKTPTIFD RSIFEDWLFA KQNIHRPSIF TYYNHLWNGI VKELIFKHGI PALYVILEGD WELFEQRLFQ RNRKVEIDNF AKNKDYFKNL YKIYGEFIKN VCYDFGISHC IVNANQSVES ITKQVLEVLK SKNLDWEII // ID Y408_MYCPN Reviewed; 760 AA. AC P75376; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized lipoprotein MPN_408; DE Flags: Precursor; GN OrderedLocusNames=MPN_408; ORFNames=F11_orf760, MP430; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96078.1; -; Genomic_DNA. DR PIR; S73756; S73756. DR RefSeq; NP_110096.1; NC_000912.1. DR RefSeq; WP_010874764.1; NC_000912.1. DR EnsemblBacteria; AAB96078; AAB96078; MPN_408. DR GeneID; 877379; -. DR KEGG; mpn:MPN408; -. DR PATRIC; 20022210; VBIMycPne110_0442. DR OMA; LEWINID; -. DR BioCyc; MPNE272634:GJ6Z-437-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 760 Uncharacterized lipoprotein MPN_408. FT /FTId=PRO_0000018733. FT LIPID 24 24 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 24 24 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 760 AA; 83344 MW; 285E22E068F7FDFE CRC64; MVIKKGFFAL SSCTLGLGLI LTACGARGKF DQVDDGVIKL ATSIQNKDSI AALNTIYKKY KERHPGSYPV QNFQVPGGYS GLRNDIRTRL SAKDGNNFYN IVLNYPDVVS SLATSDMQLI LDNVDTKLLS KNFLSFNERI GGVRQKGIYA IPISLSTELM VLNGPVLHYI LNSAKKKENG AQMIKRSGSF STVQKGTMAI DMNDQKTKDL WQKIENAAKA NGKTTSTQTS PQPKNAVSSL QLKQAAEGTS TDNSQDAENS DNEIKKTWGE YKEEGNHTLK GYTFKASVFE NWNELLDFST RVANSFPDKI KNQASKKATE LQGVFGVDSV SGALFSATFA AGGGDYDKFF FNVKNGRGNF RNLLEKGSSY NNLQKVFNDY KQLISSNGLY INKGGAYSSN FLKFHQLAFS VGSSSGYHFA FAGESAKRLE FGQKAIEYPR DTYEIKAPTN SQNGNGTLLG SFTKSKSNGK EQSGQDEDNQ TSETIELYKS SVPSGKEAGK NALAITNQQL ISALENAAKD NKTSQPQARS LTASDQVQIT QSSDKVIGYI TTSNLDIDNN NTFDVGKLNG DKSTSKIIVN ATLKTLNKIN TLQSEEGIIL PHPQKYKSTD PQAVATVQGP SIIGVHANAK ENAETQKFIN WFINQKETWP ENSKGNKNGQ NGQMTAAQYF AKSSGYVLPY SETFTKQSED EHSTTKDAYK ILKDVNDGKL VGYSDPSDFR SGKFRDTIVA AFSGAVSSKA DFNKFFKGFE QQLGQEYRRG // ID Y413_MYCPN Reviewed; 139 AA. AC Q9EXD6; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JUN-2015, entry version 51. DE RecName: Full=Uncharacterized protein MPN_413; GN OrderedLocusNames=MPN_413; ORFNames=A05_orf139, MP426.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SIMILARITY: To M.pneumoniae MPN_091 and MPN_463. {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; U00089; AAG34747.1; -; Genomic_DNA. DR RefSeq; NP_110101.1; NC_000912.1. DR RefSeq; WP_010874769.1; NC_000912.1. DR IntAct; Q9EXD6; 1. DR EnsemblBacteria; AAG34747; AAG34747; MPN_413. DR GeneID; 877323; -. DR KEGG; mpn:MPN413; -. DR BioCyc; MPNE272634:GJ6Z-442-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 139 Uncharacterized protein MPN_413. FT /FTId=PRO_0000210674. SQ SEQUENCE 139 AA; 15796 MW; 0CD89C29543B5182 CRC64; MGGWMSCGPP IYTPHTNSWT ESGWDRTSWW RWSAQRWSGW SFKIVRANKA LRVMAKTKMP LVLIPPSPNK PYSKLAINQE LHLIPPKKTS PATSSSLKPP RRPRGCLNGR LSWRCPTLSR KVRVPTIKVP MVRAPSTPP // ID Y423_MYCPN Reviewed; 129 AA. AC P75364; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG296 homolog; GN OrderedLocusNames=MPN_423; ORFNames=A05_orf129, MP418; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96066.1; -; Genomic_DNA. DR PIR; S73744; S73744. DR RefSeq; NP_110111.1; NC_000912.1. DR RefSeq; WP_010874779.1; NC_000912.1. DR PDB; 2I15; X-ray; 2.40 A; A/B/C=1-129. DR PDBsum; 2I15; -. DR ProteinModelPortal; P75364; -. DR SMR; P75364; 1-129. DR IntAct; P75364; 1. DR EnsemblBacteria; AAB96066; AAB96066; MPN_423. DR GeneID; 877277; -. DR KEGG; mpn:MPN423; -. DR PATRIC; 20022242; VBIMycPne110_0458. DR OMA; FETFRIN; -. DR OrthoDB; EOG6JX7T2; -. DR BioCyc; MPNE272634:GJ6Z-452-MONOMER; -. DR EvolutionaryTrace; P75364; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 1.20.120.510; -; 1. DR Gene3D; 1.20.890.20; -; 1. DR InterPro; IPR027371; Mg296_homologue_C. DR InterPro; IPR027374; Mg296_homologue_N. DR InterPro; IPR019097; Mg296_protein. DR Pfam; PF09644; Mg296; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MG296 homolog. FT /FTId=PRO_0000210521. FT HELIX 3 17 {ECO:0000244|PDB:2I15}. FT HELIX 21 35 {ECO:0000244|PDB:2I15}. FT TURN 41 43 {ECO:0000244|PDB:2I15}. FT HELIX 51 69 {ECO:0000244|PDB:2I15}. FT HELIX 86 107 {ECO:0000244|PDB:2I15}. FT HELIX 114 122 {ECO:0000244|PDB:2I15}. SQ SEQUENCE 129 AA; 14939 MW; 50C460E2D5967D9A CRC64; MKPQLLALKQ FVQTEFEKVD FETFRQNFNR CLEREQSTLL IYEDDDYDDQ SFFLKPMLSD AFFISSEVVK QLDLLAVLVD NPKGDVKSCC QSFYEALTLF ISALAITKGV DVGRYHQQLG KRFGVLTVY // ID Y090_MYCPN Reviewed; 329 AA. AC P75603; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MPN_090; GN OrderedLocusNames=MPN_090; ORFNames=MP065, R02_orf329; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_129. {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; U00089; AAB95712.1; -; Genomic_DNA. DR PIR; S73391; S73391. DR RefSeq; NP_109778.1; NC_000912.1. DR RefSeq; WP_010874447.1; NC_000912.1. DR ProteinModelPortal; P75603; -. DR EnsemblBacteria; AAB95712; AAB95712; MPN_090. DR GeneID; 877144; -. DR KEGG; mpn:MPN090; -. DR PATRIC; 20021457; VBIMycPne110_0089. DR OMA; GHAANGY; -. DR BioCyc; MPNE272634:GJ6Z-93-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 329 Uncharacterized protein MPN_090. FT /FTId=PRO_0000210640. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. FT TRANSMEM 260 280 Helical. {ECO:0000255}. FT TRANSMEM 299 319 Helical. {ECO:0000255}. SQ SEQUENCE 329 AA; 37433 MW; 6C3F978222B28D1D CRC64; MQTILTDQAS FNILTSKRNL INKLTITNIV LWALFVFCAI ATAFLAISHS FHKNFSFFLE SGNSNNEGET TTKVNIHVLV AQILTPIFTV LLILCWMGNI GINSLLFGQL SICQQFQNEK KWLLWAIFIP QLTLTNSLLV REKLKNILDA NSNSSTQKNR LTWWMIGFFV VWFIQLFLGF LIYLPAYSAE ARLNLNLSFL SFALNSPLPV GHAANGYFFL GLIFAFMDLT IIVLLVISGF ILKHLIQTNK TEHKKYQLMF FWTALAIDVI GLIMTISFIV VSFSLEKGDD YLLKTPFFGS SLMALITIAT LVTTILLFIR FNKKRLLKD // ID Y100_MYCPN Reviewed; 183 AA. AC P75592; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0134 protein MPN_100; GN OrderedLocusNames=MPN_100; ORFNames=MP054, R02_orf183o; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95702.1; -; Genomic_DNA. DR PIR; S73380; S73380. DR RefSeq; NP_109788.1; NC_000912.1. DR RefSeq; WP_010874457.1; NC_000912.1. DR ProteinModelPortal; P75592; -. DR IntAct; P75592; 2. DR EnsemblBacteria; AAB95702; AAB95702; MPN_100. DR GeneID; 876783; -. DR KEGG; mpn:MPN100; -. DR PATRIC; 20021493; VBIMycPne110_0104. DR OMA; EFNEYKV; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-106-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 183 UPF0134 protein MPN_100. FT /FTId=PRO_0000221594. SQ SEQUENCE 183 AA; 21046 MW; 05349A8AC4CF426E CRC64; MKEKIPFYNE KEFHDMVKKT KKGTFSGWYI IDKDNKSVEF SGSFNRQFKL NKPVIPVNTE YVTRKEFNEY KVSNDQRLTK IETTLAAQGE QINKLTQTVE KQGEQINQLV QVVLLHGEQI NKLTQTVEKQ GEQIKELQVE QKAQGEQIKA QGKQIKAQGK TLKSILQALG GINKRLDKID PPK // ID Y118_MYCPN Reviewed; 236 AA. AC P75446; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MG199 homolog; GN OrderedLocusNames=MPN_118; ORFNames=C09_orf143b, MP036; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP SEQUENCE REVISION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34735.1; -; Genomic_DNA. DR PIR; S73362; S73362. DR RefSeq; NP_109806.1; NC_000912.1. DR RefSeq; WP_010874475.1; NC_000912.1. DR ProteinModelPortal; P75446; -. DR IntAct; P75446; 8. DR EnsemblBacteria; AAG34735; AAG34735; MPN_118. DR GeneID; 877266; -. DR KEGG; mpn:MPN118; -. DR PATRIC; 20021535; VBIMycPne110_0125. DR KO; K03470; -. DR OMA; EVACASI; -. DR OrthoDB; EOG6W723H; -. DR BioCyc; MPNE272634:GJ6Z-124-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 236 Uncharacterized protein MG199 homolog. FT /FTId=PRO_0000210451. SQ SEQUENCE 236 AA; 26322 MW; 699BBEB5B3D79359 CRC64; MQHANTTALY LIGSDESGKG DSFGGIAVSA VLIHKDKINT LHQIGVGDSK QFNDYQIKAL VPKIKAAVHD QVTLSVDAKT YNQLVQSFKN VNVMLTFLHC KVYHQLLQQN KLTAQQCDIS IDEFANVKLF TQYTQKLTSL QNELKELVIP NHFLIRGESY SKVIAAASIL ARAAFIAQME QLSHQYGVQF PKGSAHGIVE ALHLLKTKRQ FHKFAQYSAV CKTTFKNVAS FLKQLA // ID Y132_MYCPN Reviewed; 256 AA. AC P75266; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 54. DE RecName: Full=Putative adhesin P1-like protein MPN_132; GN OrderedLocusNames=MPN_132; ORFNames=E07_orf256L, MP022; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95670.1; -; Genomic_DNA. DR PIR; S73348; S73348. DR RefSeq; NP_109820.1; NC_000912.1. DR RefSeq; WP_010874489.1; NC_000912.1. DR EnsemblBacteria; AAB95670; AAB95670; MPN_132. DR GeneID; 877239; -. DR KEGG; mpn:MPN132; -. DR PATRIC; 20021577; VBIMycPne110_0145. DR BioCyc; MPNE272634:GJ6Z-139-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 256 Putative adhesin P1-like protein MPN_132. FT /FTId=PRO_0000210708. SQ SEQUENCE 256 AA; 27307 MW; 16CC649D91A327F4 CRC64; MGLQLSGLDA SDSDQRELIW AKRPWAAFRG SWVNRLGRVE SVWDLKGVWA DQAHSAVSES QAATSSTTTT ATGDTLPEHP NALAYQISST DKDSYKASTQ GSGQTNSQNT SPYLHLIKPK KVTASDKLDD DLKNLLDPNE VRVKLRQSFG TDHSTQPQPQ PLKTTTPVFG TNSGNLGSVL SGGGTTQDSS TTNQLSPVQR VSGWLVGQLP STSDGNTSST NNLAPNTNTG NEVVGVGDLS KRASIESSRL WIALKP // ID Y139_MYCPN Reviewed; 163 AA. AC P75259; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=UPF0134 protein MPN_139; GN OrderedLocusNames=MPN_139; ORFNames=E07_orf163, MP015; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95663.1; -; Genomic_DNA. DR PIR; S73341; S73341. DR RefSeq; NP_109827.1; NC_000912.1. DR RefSeq; WP_010874496.1; NC_000912.1. DR ProteinModelPortal; P75259; -. DR EnsemblBacteria; AAB95663; AAB95663; MPN_139. DR GeneID; 877170; -. DR KEGG; mpn:MPN139; -. DR PATRIC; 20021593; VBIMycPne110_0153. DR OMA; KTQGEAM; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-146-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 163 UPF0134 protein MPN_139. FT /FTId=PRO_0000221600. SQ SEQUENCE 163 AA; 19116 MW; 0D8AF31CEC157FAD CRC64; MKEKIPFYNE KEFHDMVKKT KKGTFSGWYI INKNNNSVEF SGSFNRQFKL NKPVIPVNTE YVTRKEFNEY KDSNDQRLTK IETELKSQGQ RIQVVEDKVD RLTEVVMVQS QQIKTQGEAM NARMDRFESL VLKSLESIGN TLTDFGKRLD VIETRLDKID PPK // ID Y146_MYCPN Reviewed; 265 AA. AC P75140; Q50350; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MPN_146; GN OrderedLocusNames=MPN_146; ORFNames=E07_orf265, MP008; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-125. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95656.1; -; Genomic_DNA. DR EMBL; Z32651; CAA83572.1; -; Genomic_DNA. DR PIR; S73334; S73334. DR EnsemblBacteria; AAB95656; AAB95656; MPN_146. DR PATRIC; 20021611; VBIMycPne110_0162. DR OMA; ANTTEGN; -. DR OrthoDB; EOG6VB6X7; -. DR BioCyc; MPNE272634:GJ6Z-153-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03305; Lipoprotein_X; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 265 Uncharacterized protein MPN_146. FT /FTId=PRO_0000215277. FT CONFLICT 122 122 S -> R (in Ref. 2; CAA83572). FT {ECO:0000305}. FT CONFLICT 125 125 S -> P (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 265 AA; 29140 MW; 44F9408C17061BC3 CRC64; MLASCGAKGR FDQVDDGKIK LASSLTGKRD VILQEVLNKY NSRKAKDDYP IEITKIAGSY DGGRSDLQTR LSVKDKTTFY NMILNYSDTI STLGRSNMEL PLDSVDVSQF SENFLSFNDR ISGISRKGIY GIPVSMSTDI LVINGPVLHY ILNSAKKKDG AVTKKNASNS NGNEGTLTVN NDQQTTELWK KIEEAAKTNG KTTQEQTKRD AKQSTSLIQL KEGSANTTEG NASESDKEIK KSWGNYQEVD GGLKGYTFKA SVFEN // ID Y151_MYCPN Reviewed; 133 AA. AC P75035; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=UPF0134 protein MPN_151; GN OrderedLocusNames=MPN_151; ORFNames=E07_orf133, MP003; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95651.1; -; Genomic_DNA. DR PIR; S73329; S73329. DR RefSeq; NP_109839.1; NC_000912.1. DR RefSeq; WP_010874508.1; NC_000912.1. DR ProteinModelPortal; P75035; -. DR EnsemblBacteria; AAB95651; AAB95651; MPN_151. DR GeneID; 877294; -. DR KEGG; mpn:MPN151; -. DR PATRIC; 20021623; VBIMycPne110_0168. DR OMA; AQRVEFN; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-158-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 133 UPF0134 protein MPN_151. FT /FTId=PRO_0000221602. SQ SEQUENCE 133 AA; 15479 MW; 113C55267E143776 CRC64; MEFNGNLNHM EKRKSGYVTQ KQFNEYKDSN DQRLIKIETT LAAQGEQISQ LVQIVFLQGK QIKELQAEQK AQRVEFNARM DRFESLVLKS LESIGNTLTD FGKRFDSMET RLDSMDGRLD SMETRLDKID PPK // ID Y153_MYCPN Reviewed; 1113 AA. AC P75033; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized ATP-dependent helicase MG140 homolog; DE EC=3.6.4.-; GN OrderedLocusNames=MPN_153; ORFNames=E07_orf1113, MP001; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase 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; U00089; AAB95649.1; -; Genomic_DNA. DR PIR; S73327; S73327. DR RefSeq; NP_109841.1; NC_000912.1. DR RefSeq; WP_010874510.1; NC_000912.1. DR ProteinModelPortal; P75033; -. DR IntAct; P75033; 3. DR EnsemblBacteria; AAB95649; AAB95649; MPN_153. DR GeneID; 877311; -. DR KEGG; mpn:MPN153; -. DR PATRIC; 20021627; VBIMycPne110_0170. DR OMA; NEWRERN; -. DR OrthoDB; EOG6G4VR9; -. DR BioCyc; MPNE272634:GJ6Z-160-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR025103; DUF4011. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13195; DUF4011; 1. DR SUPFAM; SSF52540; SSF52540; 4. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 1113 Uncharacterized ATP-dependent helicase FT MG140 homolog. FT /FTId=PRO_0000080729. FT NP_BIND 313 320 ATP. {ECO:0000255}. SQ SEQUENCE 1113 AA; 130334 MW; 48A3337EB0E81A40 CRC64; MNDWQWLKNR LVNAKTKAVS FWLAQTTSTI LDIAELIKCC SDLKNTSING LVDLINQQEK LEFNLTRLKE IDGEDARQLF GIEGNVYKHF QTELSRFYKQ TRKHFRETGS ESLFLGLPVI EGINEFNDVF RAPLLYVGVK LKVAPRLERF WLEINREEIF LNPTIIGVEI NKRNSLFKNN YDTTKVDINQ ALEIFRELEY QFRMPLTSEL KSFSKKAKSD FNTEKRTNFL TNNVLLGIFD VKGDQLFQNF NEILNTDPDV LDELLKDRRD LLYDNREFRE NFNLKGTYLF SHLDIFQQYA VKQAFDGDVI IEGPPGTGKS ETIVNILVNL ALNKKKVLFV SEKVTALDVV YNRLGSFKHI ALFNASVASE KKRFYSQFAD YESFFTDNFS KKDLVNEMPV FDGQWVDKIL SEFTNLQNIY DTQINSGNQS YSFKEILSSF PILDVSYIKI KEHDRFDEWV RVFSSQVWLE KHLTYLAFKA ELSKRWQNID NFYALKDLLE KRKNIRVLCY VLDYFEQNNS IIKPKRVLLY TPTERGQKQL HQLQQDVAKY NSLQRFKSAA KFETIKLNLA NKLAQNAKPF FFSWFIQTHA QTLLENLVQT QKQLVKAKQS YLSKIEQYVV SCKRILKATI LANFFELYQT NKNELLDICR EAKNPVLKEI TWWFKKNFAL LSKLFPVHIM TFESAALLTP NQRRLYDYVV IDEASQVYLE RAIPILYRGA KYIIAGDTKQ LKPSNFFQAR AEYDVDEEFE DGNVEAAVHS TSLLHFLKNR SRILTLLKFH YRSDSANLIA FTNNRIYNNE LIFMNKATAD KQVFIVHDVI DGIWRNNRNL QEARDVVQRL EQLTQTAEYQ KSLGVICFNK NQAELIEYMI DKQNNPLLNE WRDRVNAQGE YVGLFVKNIE NVQGDERDII IFSLGYDRSV NSYGPISKQG GENRLNVAIT RAKQRIELFK TNRASDYNGL SSNSLGSKLL VEYLLYCEAM ANNQGESLDF QATQKQAPKA KYELELENQF FNELELIFGE QFTIKRNVNE GAYSFSFVFY FNENPYLAVD FNPALPHSRK EVSENIIYRE QFLKKRKWNL VNIWLDEWKL NPGGVLQKLR NCLTHSENEF EEI // ID Y159_MYCPN Reviewed; 424 AA. AC P75586; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=UPF0053 protein MG146 homolog; GN OrderedLocusNames=MPN_159; ORFNames=MP672, VXpSPT7_orf424; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0053 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC -!- SIMILARITY: Contains 1 DUF21 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; U00089; AAB96320.1; -; Genomic_DNA. DR PIR; S73998; S73998. DR RefSeq; NP_109847.1; NC_000912.1. DR RefSeq; WP_010874516.1; NC_000912.1. DR ProteinModelPortal; P75586; -. DR EnsemblBacteria; AAB96320; AAB96320; MPN_159. DR GeneID; 877287; -. DR KEGG; mpn:MPN159; -. DR PATRIC; 20021641; VBIMycPne110_0177. DR OMA; RIACAND; -. DR OrthoDB; EOG64FKB6; -. DR BioCyc; MPNE272634:GJ6Z-166-MONOMER; -. DR Proteomes; UP000000808; 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; IPR000644; CBS_dom. DR InterPro; IPR002550; DUF21. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01595; DUF21; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 424 UPF0053 protein MG146 homolog. FT /FTId=PRO_0000088379. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT DOMAIN 13 190 DUF21. FT DOMAIN 210 270 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 275 335 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 424 AA; 48528 MW; 9B35BC1D1AC2CB65 CRC64; MESAPSGGLL ALIIISIILL ACISAVVSAY ETAITSITSY KWSNYVKTHN KQKKLTTKIV NHFQKNYSAC LITILVANNI VAILVSNILF LALDQSIKNP AISSALNLLI SGVLLLMLCE ITPKTLARIN IIRVLVYFAV VVYFFYILFW PITKLASIIF AKYEKAPPVS RRDVYFFIDE IEQNGLFTKE DGQLIKRTLI FDQVLVDQIM IKWNRVVYCY EGDPVKTIKE KFLHGQFSRM PVLDQTSNEV VGFIHLKDLF SSLEKSNEPF VLQELLYPAV LVSNTTPIKQ ALRQMRLHRA HLAVVQDKHH HTIGIVSMED IIEELVGEIY DEHDEVEAVQ TLDNNTWLVL PNVKAAFFFN KWIKRDLVKS KNMTIQRYLA SFENDGLNTQ NKLETPWFIA EAIVDSENPE QIRYEIRKKS DVVD // ID Y262_MYCPN Reviewed; 475 AA. AC P75513; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG123 homolog; GN OrderedLocusNames=MPN_262; ORFNames=A65_orf475, MP571; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96219.1; -; Genomic_DNA. DR PIR; S73897; S73897. DR RefSeq; NP_109950.1; NC_000912.1. DR RefSeq; WP_010874619.1; NC_000912.1. DR IntAct; P75513; 1. DR EnsemblBacteria; AAB96219; AAB96219; MPN_262. DR GeneID; 876858; -. DR KEGG; mpn:MPN262; -. DR PATRIC; 20021849; VBIMycPne110_0281. DR OMA; YFKQVCD; -. DR OrthoDB; EOG60654R; -. DR BioCyc; MPNE272634:GJ6Z-269-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 475 Uncharacterized protein MG123 homolog. FT /FTId=PRO_0000210428. FT TRANSMEM 19 39 Helical. {ECO:0000255}. SQ SEQUENCE 475 AA; 55434 MW; 449BC01B605896E9 CRC64; MLASLTSRSA TSFSIIWALV SAILILSILI WLIITIFFAW NLHLKNNKKR TKYHLEPEQI KHKIIQNKTK LGKMLDFYQQ QINTTATELK WLDGQFQQID ETDKKKAHQI AIRLARNQLL QQLSVKLDQK QFSQRANNEL QKLKLSNLES FTNQKIKWDQ EGMKSAVSRV TINEWTFNHF AGKNRVYWDY FKQVCDVDCS IKPLKDQLEI TFSSWSLLKR LQAKNLFNKL IAQSSSVKMS EKLINNALQL VQDNLALQAS ESGNKLLKEF ELSCTNTQLV QLLGFQQFYF GTNLLSLLDL SRSIAVLVRF LNEHCKWELN ERLLVETALF NNLQWVNNND FFLKSHNDLK QLHLSAEQLA IIEQQNRPFY IDAYALLIAG VKQMLMEHDA VEPKQIHFHN AKKVMESFQL FGIDQLALIE YNNCLYGFVT TKLYEIKQLD DLALFKVLFK SFLNKHLKQK FATISLFVNT QTLMI // ID Y271_MYCPN Reviewed; 251 AA. AC P75505; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 74. DE RecName: Full=Uncharacterized lipoprotein MPN_271; DE Flags: Precursor; GN OrderedLocusNames=MPN_271; ORFNames=A65_orf251a, MP563; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB96211.1; -; Genomic_DNA. DR PIR; S73889; S73889. DR RefSeq; NP_109959.1; NC_000912.1. DR RefSeq; WP_010874628.1; NC_000912.1. DR EnsemblBacteria; AAB96211; AAB96211; MPN_271. DR GeneID; 876957; -. DR KEGG; mpn:MPN271; -. DR PATRIC; 20021867; VBIMycPne110_0290. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-278-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 251 Uncharacterized lipoprotein MPN_271. FT /FTId=PRO_0000014056. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 251 AA; 29074 MW; 02C937B168311E90 CRC64; MRKKKFLSRF SFSSLFLLCG TLLSACTGIQ ADLRNLIKET TGKDIDLSKA IKTKEGKKNI IASLKKSYEV NPKDTTKLLL DAWKQSFEEG KLGIADFDFD HVAYPQTNDP FTMERKVDHF QMTYQSFKDL LVEARLSYTF NWFGDYSSGD FTAKRGDKHY FYLFLKIKSD PKKQFSAKKF LTEGEAFTDQ EGKQTTRNLE WIEFSASISW WTKGKDDVSQ KSLKKFLESF ATNTGYSSDI NLFSYLEYLI K // ID Y286_MYCPN Reviewed; 465 AA. AC P75491; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Putative adhesin P1-like protein MPN_286; GN OrderedLocusNames=MPN_286; ORFNames=A65_orf465V, MP549; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96197.1; -; Genomic_DNA. DR PIR; S73875; S73875. DR RefSeq; NP_109974.1; NC_000912.1. DR RefSeq; WP_010874643.1; NC_000912.1. DR EnsemblBacteria; AAB96197; AAB96197; MPN_286. DR GeneID; 877084; -. DR KEGG; mpn:MPN286; -. DR PATRIC; 20021903; VBIMycPne110_0308. DR BioCyc; MPNE272634:GJ6Z-293-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 465 Putative adhesin P1-like protein MPN_286. FT /FTId=PRO_0000210712. SQ SEQUENCE 465 AA; 49148 MW; 6C30958AE1017906 CRC64; MLDYIPWIGN GHRYGNDHRG SNSSTSGVTT QGQQSQNASG TEPASTFSNV GVGLKANVQG TLGGSQTTTT GKDIPKWPTL DQANLQLWTG AGWRNDKASS GQSDENHTKF TSATGSGQQG SSSGTTNSAG NPDSLKQDKV DKSGDSVTVA ETTSGDNLTN YTNLPPNLTP TADWPNALSF TNKNNAQRAQ LFLRALLGSI PVLVNKSGQD DSNKFQATDQ KWSYTELKSD QTKLNLPAYG EVNGLLNPAL VEVYGLSSTQ GSSTGAGGAG GNTGGDTNTQ TYARPGIGFK LPSTDSESSK ATLITPGLAW TAQDVGNLVV SGTSLSFQLG GWLVTFTDFI KPRSGYLGLQ LTGLDANDSD QRELIWAPPA LNRLSWQLGQ PLGPRGECVG FQGGVGGSSS VRLASSYKYH HRNEGYLIGA HQCFGLSGEL YRPGFVQGFH SKLRPKPKHL PLPALGAGEK SRFLW // ID Y311_MYCPN Reviewed; 357 AA. AC P75470; O08089; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MG218.1 homolog; GN OrderedLocusNames=MPN_311; ORFNames=F10_orf357, MP525; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96173.1; -; Genomic_DNA. DR EMBL; U59896; AAB52528.1; -; Genomic_DNA. DR PIR; S73851; S73851. DR RefSeq; NP_109999.1; NC_000912.1. DR RefSeq; WP_010874667.1; NC_000912.1. DR IntAct; P75470; 2. DR EnsemblBacteria; AAB96173; AAB96173; MPN_311. DR GeneID; 876891; -. DR KEGG; mpn:MPN311; -. DR PATRIC; 20021974; VBIMycPne110_0335. DR OMA; DPIQREI; -. DR OrthoDB; EOG6TR0P3; -. DR BioCyc; MPNE272634:GJ6Z-327-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 357 Uncharacterized protein MG218.1 homolog. FT /FTId=PRO_0000210461. SQ SEQUENCE 357 AA; 40580 MW; F828443341D3D7F9 CRC64; MTNDYQQLNY LVETDDEADI IIANLVKQLN ELKEILLSLD NQDLEINQVN HRTTVHNTSS NTSNNSTSNN IADGNYNSNF FHNFSKETLQ TQAKRGFLLL ERCSLVGLQQ LELEYLNVLG RSFESHQDKI NFLVNLRDLT NDHLLDTEKI VSTLEQIFNV IGGTEYTPIL NSFFNQSLND PDPIQREIGL KQFVANLRQR FKTLLQKTNN SIQQLEAEIQ IPTTHIKSDE VMFGPPDMNE RLVLNDSETD AILRSIEAEL ESALQNKKQV VVTAVPPIAA NLATDSISQE TLEHNLNNTE TVNTTTVTVT SASETQVRKP QISLRPIFQG NFPKRLSRED IQRYAHQLQE LEQSNEG // ID Y340_MYCPN Reviewed; 529 AA. AC P75438; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Probable DNA helicase MPN_340; DE EC=3.6.4.12; GN OrderedLocusNames=MPN_340; ORFNames=H91_orf529, MP496; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00560}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96144.1; -; Genomic_DNA. DR PIR; S73822; S73822. DR RefSeq; NP_110028.1; NC_000912.1. DR RefSeq; WP_010874696.1; NC_000912.1. DR ProteinModelPortal; P75438; -. DR IntAct; P75438; 4. DR EnsemblBacteria; AAB96144; AAB96144; MPN_340. DR GeneID; 876772; -. DR KEGG; mpn:MPN340; -. DR PATRIC; 20022034; VBIMycPne110_0364. DR KO; K03657; -. DR OMA; YTETENA; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; MPNE272634:GJ6Z-357-MONOMER; -. DR Proteomes; UP000000808; 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 529 Probable DNA helicase MPN_340. FT /FTId=PRO_0000102082. FT DOMAIN 2 285 UvrD-like helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00560}. FT NP_BIND 23 30 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00560}. SQ SEQUENCE 529 AA; 60529 MW; D80152E4C58DF32A CRC64; MEHLNQEQKA AVTCDNGVNV VYSGAGTGKT TVIAERFAYL VNEKGVNPQS ILAFTFTDKA ASEMRQRIIK LIPQKSLQDL HIYTFHSFAN RFLQKHGKSD FAILSDSNRF FSDYEMGDQL QTVVEIYKNK VVDLELDNLE YNSAFRDACT DTFNEDFSTI SNGQFRKRAA TALRAYQNYL ITNNLFDFSD LIIETCHLLK GNSELLQAFT ESVHYILVDE FQDTNLAQYE LVKLLATTHP NLFLVGDSNQ MIYGWRGAVV EIFELLKNDF QAVKEFYTTQ NYRSIQAVLA VANDVLTAIA RKERKALVLL HSSIDSKAVP VHYKANSLKN QDQWIIYQMK QLHLNNGVPY DQMAVLFRKN KHLDAFSQTV LEDGDLPLAK LNLLTIHAAK GLEFEAVFVY GLVERAFPSL HWDGSDKHKL LEEMKLFYVA ITRAKQFLFL VSVSVESFNA YYEPSRFLKL IEKEHLQTQK AAYFKEQLKT QPKPVNLYTE TENAENLQKA TDSKKWIILG AILLIIVIIT AVLKLFVEN // ID Y359_MYCPN Reviewed; 258 AA. AC P75421; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG256 homolog; GN OrderedLocusNames=MPN_359; ORFNames=H91_orf258, MP477; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96125.1; -; Genomic_DNA. DR PIR; S73803; S73803. DR RefSeq; NP_110047.1; NC_000912.1. DR RefSeq; WP_010874715.1; NC_000912.1. DR EnsemblBacteria; AAB96125; AAB96125; MPN_359. DR GeneID; 876901; -. DR KEGG; mpn:MPN359; -. DR PATRIC; 20022084; VBIMycPne110_0386. DR OMA; SIDSEYF; -. DR OrthoDB; EOG62K24R; -. DR BioCyc; MPNE272634:GJ6Z-379-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 258 Uncharacterized protein MG256 homolog. FT /FTId=PRO_0000210493. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. SQ SEQUENCE 258 AA; 30558 MW; 2C23E52F960CB8D0 CRC64; MNYSYSFKEY IERFAKKVNS IDSEYFEFSS YIERMRTVFG LLIALICFSN VLCFLFIATW FSTKGFGQHY RALIFTLFIP FVTSLLANII FINLNRAFRE YFKISSKSRS FLVICAFSSL PIVNIWLMLW WVAMIKRFTS NYAFAIFDKY NGLTSGVFIF DFADNVNFEG KLVSFDNTKD TNRDFVHFYS EAKLKRDKIT LQTNPIPHER MYVNRMYYQQ KLSMGANQNS PSTAFANLKR YVEHKQQKII KIKQFILT // ID Y368_MYCPN Reviewed; 180 AA. AC P75413; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=UPF0134 protein MPN_368; GN OrderedLocusNames=MPN_368; ORFNames=H91_orf180, MP468; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96116.1; -; Genomic_DNA. DR PIR; S73794; S73794. DR RefSeq; NP_110056.1; NC_000912.1. DR RefSeq; WP_010874724.1; NC_000912.1. DR ProteinModelPortal; P75413; -. DR EnsemblBacteria; AAB96116; AAB96116; MPN_368. DR GeneID; 876877; -. DR KEGG; mpn:MPN368; -. DR PATRIC; 20022106; VBIMycPne110_0397. DR OMA; EKEFHYM; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-388-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 180 UPF0134 protein MPN_368. FT /FTId=PRO_0000221607. SQ SEQUENCE 180 AA; 21073 MW; 2BE940CF9966C65F CRC64; MKEKIPFYNE KEFHYMMKKT KKGTFSGWYI INPENNSVEF SGSFNRQFKL NKPVIPVNTE YVTRKEFNEY KDSNDQRLTK IENKVDKLEI KVDKLEKKVD KLEVKVDKLV ETVNAQGEDL NNFKVEVRGT LQSQGETLQL ILQTLQGMSK RLDSVEGRLD SMDGRLDSME TRLDKIDPLK // ID Y381_MYCPN Reviewed; 292 AA. AC P75401; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Putative phosphatase MPN_381; DE EC=3.1.3.-; GN OrderedLocusNames=MPN_381; ORFNames=A19_orf292, MP456; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- INTERACTION: CC P75135:rbgA; NbExp=1; IntAct=EBI-2260760, EBI-2259776; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; U00089; AAB96104.1; -; Genomic_DNA. DR PIR; S73782; S73782. DR RefSeq; NP_110069.1; NC_000912.1. DR RefSeq; WP_010874737.1; NC_000912.1. DR ProteinModelPortal; P75401; -. DR IntAct; P75401; 1. DR EnsemblBacteria; AAB96104; AAB96104; MPN_381. DR GeneID; 877388; -. DR KEGG; mpn:MPN381; -. DR PATRIC; 20022138; VBIMycPne110_0412. DR KO; K07024; -. DR OMA; VIEDYME; -. DR OrthoDB; EOG6K13W0; -. DR BioCyc; MPNE272634:GJ6Z-402-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 292 Putative phosphatase MPN_381. FT /FTId=PRO_0000054438. FT REGION 60 61 Phosphate binding. {ECO:0000250}. FT ACT_SITE 11 11 Nucleophile. {ECO:0000250}. FT METAL 11 11 Magnesium. {ECO:0000250}. FT METAL 13 13 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 242 242 Magnesium. {ECO:0000250}. FT BINDING 12 12 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 217 217 Phosphate. {ECO:0000250}. FT BINDING 245 245 Phosphate. {ECO:0000250}. SQ SEQUENCE 292 AA; 33839 MW; 544BDF781CE30336 CRC64; MKNKIKYVYS DLDGTIVSWN PKNQFTHQGK TYKNLHEVSH ATVTAFKQLQ AQGIKIGIVT GRDYCRVRWL EKYLNTDLPT ITLDGAIIYF RDEIIRQEVL DKEFIHGINQ IVKRYPTAAF KLNMGWGNYY TCNPSLIFEG DHAYREHFNA DSKFYRKEID NTVDWDINNM KVNQVYFDTF TCPEPMIQEL DNLVEKSDVT AKSYRHSLYI IKKGVSKASA LQNLQRDFLV EMKPANTIVF GDGDNDIEMM QWADHSVSLT GSDPECYKLA KYHTDSVDDD GIAKWINKNL LC // ID Y383_MYCPN Reviewed; 282 AA. AC P75399; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Putative phosphatase MPN_383; DE EC=3.1.3.-; GN OrderedLocusNames=MPN_383; ORFNames=A19_orf282, MP454; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; U00089; AAB96102.1; -; Genomic_DNA. DR PIR; S73780; S73780. DR RefSeq; NP_110071.1; NC_000912.1. DR RefSeq; WP_010874739.1; NC_000912.1. DR ProteinModelPortal; P75399; -. DR IntAct; P75399; 3. DR EnsemblBacteria; AAB96102; AAB96102; MPN_383. DR GeneID; 877093; -. DR KEGG; mpn:MPN383; -. DR PATRIC; 20022142; VBIMycPne110_0414. DR KO; K07024; -. DR OMA; HIFENNE; -. DR OrthoDB; EOG6K13W0; -. DR BioCyc; MPNE272634:GJ6Z-404-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 2. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 282 Putative phosphatase MPN_383. FT /FTId=PRO_0000054440. FT REGION 45 46 Phosphate binding. {ECO:0000250}. FT ACT_SITE 11 11 Nucleophile. {ECO:0000250}. FT METAL 11 11 Magnesium. {ECO:0000250}. FT METAL 13 13 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 230 230 Magnesium. {ECO:0000250}. FT BINDING 12 12 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 207 207 Phosphate. {ECO:0000250}. FT BINDING 233 233 Phosphate. {ECO:0000250}. SQ SEQUENCE 282 AA; 31914 MW; 009F19131B1B01AD CRC64; MKPKVQNLIF DLDGTLLSWG HEPLPQTVTF LKELQKQGFK ITFATGRSHI LIRNTTQFIQ PDLPVISSNG ALIYDFAREK ALHMTQLAPQ SVVPIMRLLL QLEESFCIYT DKKVFGFEKP GIPCKRLRTT QSKIVEPDIT QNNFTINPLT DASKFDFATQ NITKILLITE DRGRISKITK HLDAIENISY VSSMTFALDI MHKDVNKAYG LKALEQQTGL DPQMTMVFGD GDNDVEIFNA VKYSVAMANG SDLAKQNATF ISEFDNDHDG IYHFLQCFLK IE // ID Y387_MYCPN Reviewed; 358 AA. AC P75395; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MG269 homolog; GN OrderedLocusNames=MPN_387; ORFNames=F11_orf358b, MP450; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96098.1; -; Genomic_DNA. DR PIR; S73776; S73776. DR RefSeq; NP_110075.1; NC_000912.1. DR RefSeq; WP_010874743.1; NC_000912.1. DR ProteinModelPortal; P75395; -. DR IntAct; P75395; 1. DR EnsemblBacteria; AAB96098; AAB96098; MPN_387. DR GeneID; 877062; -. DR KEGG; mpn:MPN387; -. DR PATRIC; 20022150; VBIMycPne110_0418. DR OMA; HAIKEAN; -. DR OrthoDB; EOG63VBVS; -. DR BioCyc; MPNE272634:GJ6Z-409-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 358 Uncharacterized protein MG269 homolog. FT /FTId=PRO_0000210499. SQ SEQUENCE 358 AA; 42617 MW; A1EEC0FA233EF6CD CRC64; MTNFEYYRDF DDFQRRETIN FFLSKFPLAS QKQLQDFLEQ ARQAYVQLRQ TNPAHLDWNQ TLLYLAQKFL PEKQSEKDRL KKILVLQEQL KVRYEGEIKR QSQQNSELLI QLGQRDEEII QMQQLFKEKE RQLEVYQKQL NEAKEYNHKL EEHYNKTLEE ALKEYEQQCT DAIHRRDEEI QAIFTSKLNE KNSEITQLQT YLQSAVDENE ALQKQHKLVL FKNQKYEKMV SDLQVDLARI QEINNSLTSE KRDFQRANND LVKQYNKLKN RLEQKLGEIT NAQVNGQTHT VSLADTSQQF HRPQEAVIPQ TQVISYTLDD MDDDMEVEET PPTTNKDLPR GATQPKRNSI KRVSKLID // ID Y400_MYCPN Reviewed; 582 AA. AC P75383; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MG281 homolog; GN OrderedLocusNames=MPN_400; ORFNames=F11_orf582, MP438; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96086.1; -; Genomic_DNA. DR PIR; S73764; S73764. DR RefSeq; NP_110088.1; NC_000912.1. DR RefSeq; WP_010874756.1; NC_000912.1. DR IntAct; P75383; 1. DR EnsemblBacteria; AAB96086; AAB96086; MPN_400. DR GeneID; 877066; -. DR KEGG; mpn:MPN400; -. DR PATRIC; 20022176; VBIMycPne110_0431. DR OMA; QSTEYFN; -. DR OrthoDB; EOG6H7FDC; -. DR BioCyc; MPNE272634:GJ6Z-423-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR030943; M_MG281. DR InterPro; IPR030942; Mycoplas_M_dom. DR TIGRFAMs; TIGR04524; mycoplas_M_dom; 1. DR TIGRFAMs; TIGR04525; prot_M_MG281; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 582 Uncharacterized protein MG281 homolog. FT /FTId=PRO_0000210509. FT TRANSMEM 20 40 Helical. {ECO:0000255}. SQ SEQUENCE 582 AA; 65977 MW; 394B304F442CA1EF CRC64; MKLNFKIKDK KTLKRLKKGG FWALGLFGAA INAFSAVLIV NEVLRLQSGE TLIASGRSGN LSFQLYSKVN QNAKSKLNSI SLTDGGYRSE IDLGDGSNFR EDFRNFANNL SEAITDAPKD LLRPVPKVEV SGLIKTSSTF ITPNFKAGYY DQVAADGKTL KYYQSTEYFN NRVVMPILQT TNGTLTANNR AYDDIFVDQG VPKFPGWFHD VDKAYYAGSN GQSEYLFKEW NYYVANGSPL YNVYPNHHFK QIKTIAFDAP RIKQGNTDGI NLNLKQRNPD YVIINGLTGD GSTLKDLELP ESVKKVSIYG DYHSINVAKQ IFKNVLELEF YSTNQDNNFG FNPLVLGDHT NIIYDLFASK PFNYIDLTSL ELKDNQDNID ASKLKRAVSD IYIRRRFERQ MQGYWAGGYI DRYLVKNTNE KNVNKDNDTV YAALKDINLH LEETYTHGGN TMYRVNENYY PGASAYEAER ATRDSEFQKE IVQRAELIGV VFEYGVKNLR PGLKYTVKFE SPQEQVALKS TDKFQPVIGS VTDMSKSVTD LIGVLRDNAE ILNITNVSKD ETVVAELKEK LDRENVFQEI RT // ID Y420_MYCPN Reviewed; 241 AA. AC P75367; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MG293 homolog; GN OrderedLocusNames=MPN_420; ORFNames=A05_orf241a, MP421; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 GP-PDE domain. {ECO:0000305}. CC -!- SIMILARITY: To glycerophosphoryl diester phosphodiesterases CC (EC 3.1.4.46). {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG385. {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; U00089; AAB96069.1; -; Genomic_DNA. DR PIR; S73747; S73747. DR RefSeq; NP_110108.1; NC_000912.1. DR RefSeq; WP_010874776.1; NC_000912.1. DR ProteinModelPortal; P75367; -. DR IntAct; P75367; 2. DR EnsemblBacteria; AAB96069; AAB96069; MPN_420. DR GeneID; 877296; -. DR KEGG; mpn:MPN420; -. DR PATRIC; 20022236; VBIMycPne110_0455. DR KO; K01126; -. DR OMA; NELIVIH; -. DR OrthoDB; EOG6MD930; -. DR BioCyc; MPNE272634:GJ6Z-449-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.190; -; 1. DR InterPro; IPR004129; GlyceroP-diester-Pdiesterase. DR InterPro; IPR030395; GP_PDE_dom. DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl. DR PANTHER; PTHR23344; PTHR23344; 1. DR Pfam; PF03009; GDPD; 1. DR SUPFAM; SSF51695; SSF51695; 1. DR PROSITE; PS51704; GP_PDE; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 241 Uncharacterized protein MG293 homolog. FT /FTId=PRO_0000210517. FT DOMAIN 5 241 GP-PDE. SQ SEQUENCE 241 AA; 28373 MW; 193328B89FDCDFE9 CRC64; MLKRQLLLAH RGYSDIAPEN TQLAFELAFQ YRFDGVELDV HLTKDGELVI IHDETTTRTA LVDKTIELET LASLKQDDHS AFFKFKTQPQ PIMTLKEFFD QYLDKFQLIN VEIKTDQKEY PGIEAKIDAL AQQYGKKVIE KVVFSSFNFA SLQRLYDINP NYQIAFLFWT KKQFQAVDAL KIKQVCQYLH PWTNIYEKFP DMVLSLQLPL GLWTLNSEVK FHQFRQDRMV YAQIANKKFE V // ID Y421_MYCPN Reviewed; 475 AA. AC P75366; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MG294 homolog; GN OrderedLocusNames=MPN_421; ORFNames=A05_orf475, MP420; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To E.coli YihN. {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; U00089; AAB96068.1; -; Genomic_DNA. DR PIR; S73746; S73746. DR RefSeq; NP_110109.1; NC_000912.1. DR RefSeq; WP_010874777.1; NC_000912.1. DR ProteinModelPortal; P75366; -. DR TCDB; 2.A.1.52.4; the major facilitator superfamily (mfs). DR EnsemblBacteria; AAB96068; AAB96068; MPN_421. DR GeneID; 877303; -. DR KEGG; mpn:MPN421; -. DR PATRIC; 20022238; VBIMycPne110_0456. DR OMA; VNEIRIP; -. DR OrthoDB; EOG6G7R0F; -. DR BioCyc; MPNE272634:GJ6Z-450-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. 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; Reference proteome. FT CHAIN 1 475 Uncharacterized protein MG294 homolog. FT /FTId=PRO_0000210519. SQ SEQUENCE 475 AA; 52731 MW; 5A1F1F0E4B9B886D CRC64; METKLSLKKR LQQFSKKQLI ALIILGAADV FVIAAPYYIK NVVPNLHLYL GITEDEVATL TSIIGYVTLA TQLPGGFLAN RFSSRKLLFL SEISTGVITF WLATNILTRE SQKSNALFVQ YCVIWGLWGI TSTLIFWTPL WKLASQQATQ ENQALGFGIQ GAANGVWGFI FIFLIALIIT AVAYPAGGES SANNPAPFAI YAFIIGGMLL VTGFTVLFFV PEKPIEKYDS HTSLKTAKKN FEQILITLKN WKLWLLSFFL MGMYVFQSTF AYYLLQMMQN AFLAPVILGT VLGGVRTYVL RSAVSVYLGR LADKFRSYIL FLMLCTGLGI IFVLMFILLG FGQVGQQQNY ALIIVSAILY ILTGVLSWGM VTVRYNQVAE IEIGKNNYAS SVGLLSFIGF STDGWLYTVT SVVGKAYTPD GQKNTSIQGY QIIAAICLGI ALFGLLCGTI VFLVNTWELK RLGKTDYRWR TLDNA // ID Y432_MYCPN Reviewed; 353 AA. AC P75356; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 88. DE RecName: Full=Putative ABC transporter ATP-binding protein MG303 homolog; GN OrderedLocusNames=MPN_432; ORFNames=A05_orf382, MP409; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96057.1; 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; U00089; AAB96057.1; ALT_INIT; Genomic_DNA. DR PIR; S73735; S73735. DR RefSeq; NP_110120.1; NC_000912.1. DR ProteinModelPortal; P75356; -. DR EnsemblBacteria; AAB96057; AAB96057; MPN_432. DR GeneID; 876830; -. DR KEGG; mpn:MPN432; -. DR PATRIC; 20022260; VBIMycPne110_0467. DR KO; K16787; -. DR OMA; RIMIVSH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-461-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 353 Putative ABC transporter ATP-binding FT protein MG303 homolog. FT /FTId=PRO_0000093244. FT DOMAIN 72 312 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 107 114 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 353 AA; 39877 MW; A6CDB628E08B7494 CRC64; MQTPQIIWSL IAPQYRGLAN KVNRKLIQSS IKHYFWYCKQ FDKLVHPFYY LTAKKHTPLF NQQLVDLAQS TLYFYNLSVF VDKSNAGQII KNVTGSVEPN QITVIFGPSG SGKTTLIKQL GLVENPTCGF LNCGNFYYFA NQKHNRATKQ FQNSIGYVLQ KAEEQFLCDS VLEEVLTGAI NLGLCQKGDV NFAKKYLEMC GLHHIPLIKN PLELSGGQKK RLALASVLAM QVQFLILDEP TVGLDQEGKA LKSALLKQLK QVTRIMIVSH DVDFIYETAD SLIQLEAGQI VDQMSVADFF NNMQLLQRYE ITPPLVVQTI QLLQAKGVQL NDPLAIKTVH DLIDQLKPLF HDQ // ID Y442_MYCPN Reviewed; 150 AA. AC P75336; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 67. DE RecName: Full=Uncharacterized lipoprotein MPN_442; DE Flags: Precursor; GN OrderedLocusNames=MPN_442; ORFNames=H08_orf150, MP399; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor, GPI- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96047.1; -; Genomic_DNA. DR PIR; S73725; S73725. DR EnsemblBacteria; AAB96047; AAB96047; MPN_442. DR PATRIC; 20022282; VBIMycPne110_0478. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MPNE272634:GJ6Z-471-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 150 Uncharacterized lipoprotein MPN_442. FT /FTId=PRO_0000014060. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 150 AA; 16639 MW; 4C75375FF57387C3 CRC64; MKKLLIKPQF WFLTLGGFIS SSVILVACAT PSNSALQTVF KARSNQFFNG EQGSLQNALA TALKDPEANK QFVAAPLLKA LTAWYENNQD KQVTQFFKDT KKSVDEQYNQ AVDKVVSASR NKNLFVQQDL LDSAGGVRNL KSPEVVWTAH // ID Y444_MYCPN Reviewed; 1325 AA. AC P75334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized lipoprotein MG309 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_444; ORFNames=H08_orf1325, MP397; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96045.1; -; Genomic_DNA. DR PIR; S73723; S73723. DR RefSeq; NP_110132.1; NC_000912.1. DR RefSeq; WP_010874800.1; NC_000912.1. DR EnsemblBacteria; AAB96045; AAB96045; MPN_444. DR GeneID; 877091; -. DR KEGG; mpn:MPN444; -. DR PATRIC; 20022286; VBIMycPne110_0480. DR OMA; NDAINAR; -. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MPNE272634:GJ6Z-473-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 1325 Uncharacterized lipoprotein MG309 FT homolog. FT /FTId=PRO_0000014033. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1325 AA; 146278 MW; 13FEF53D155ECB15 CRC64; MHTFTRKVKW PFMFTAIGLT FGIVAVACAQ PTASTVEGLF KPSSAFADRT DFSLSSILQK SLINRESFNQ YLAMRLAPVL RTFYEDNYDT DIKERLNGFT ADTDNAFVSQ EQNLRNQFRE NYLVHLQTDI FDNTGGNQAA WKLRDVNNKI IDDFISRIFA KNFVEYVQDG VGPLTKPTKS LIENTSNFKN IKLQPKFVNK NAKLKINNDA VYAAIQDKLL DQFITNENPN LVSRVVFTNE TPVDGFDNYF NTKVIQSPTP SYQFQVFNKY NQQSGGTKGA NGFNLLASNL KSYKNDQSKG IDIPNKFSSD SGGKLLLKAS DMFDTFDPSF SAAFIQGYLA LQKKSKGADS KEVDSLIKDK SIIENFFVDN NTQAAAAARA ASSSSEGTIQ LKTASDGGGT TQSTVHKTDL VKIFGDKDVF AGEYKQQIGN TNANQTGGGG SGGGGGTSTG SSTGSSTETT TGNSSKAVVD LIEVKKDSSS QPDYILSRGK DGIHLMAVDG GSHYLTESGR DVAKQKKFLL FRALQTKYGL VDTDTTYDFK LFDEVKKYFD TNRILFLFEA LLDLSSDTNN KDNFLSYPQF KKFADSIKSI EKDLKELVQA HYKQAVFNET AVAENKVTLK LAERNQPFID NERNNQIEQN GLAAKLPYEQ DAKTGHYNDL GNYYKDIIDN VDKKGTSTVK TTSSNTGQTK NFSEEVVSKL KDNKKKVEEA AKKHVEALKV FTIPSPLYSQ VILVQTKLSF TPESTSLGLN LALNNYLTST ELQNSIKLSY FQEDEAFKKI IDITNLTFSQ QSGGTGGTNG NNNLTADNWK IFKETYLLDL FESQAQKSIF GHVGSSDKNS STKTGIEGVL DTLYSSLNLE ERLDSDDVID YLSYLYTAHW LLKDNLKNYK QSLQSKLSRT SNAFLVWSVD SEKNKNDSQS TLSSTASSTS NTGLIQLRSV VSLAQNQAAG QGGDNNSDIT QTEVKNPNFV FGSSVYDWTN SKTPEVNRAA DDTSSFFYTK SSSSSTGAAQ SSATVLRSLN QASGMTTKTA KNRYGFRGIV TSSTSGSLPE AVSRRLFKQF VNQTEKGVKV GGQMLITTAK SGKATLVLKQ QADDAESTTN NAYKGALFSF GSMDNLKNII NGIQTQTEFD ALYNHLTSDL NIDVTGVDKN KTLTEQKTSL TSFVDSNFKQ STQSAQRGDT SARSARSATV QIKKTQEDNQ NTNYKDVFSR FDGYIGDNKV EEKNYTSYQF LSDGGKYHAT FVKQVNLDDV EKIGTDSLKQ EDSSKDKRLN LSLEEFLAAI ALEALDPNNQ TQAINALISG NKKGLVKVGD FRIFSSISAQ WVRRF // ID Y449_MYCPN Reviewed; 448 AA. AC Q50363; P75331; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MG314 homolog; GN OrderedLocusNames=MPN_449; ORFNames=H08_orf448, MP392; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38997; AAA61695.1; -; Genomic_DNA. DR EMBL; U00089; AAB96040.1; -; Genomic_DNA. DR PIR; S73718; S73718. DR RefSeq; NP_110137.1; NC_000912.1. DR RefSeq; WP_010874805.1; NC_000912.1. DR EnsemblBacteria; AAB96040; AAB96040; MPN_449. DR GeneID; 877078; -. DR KEGG; mpn:MPN449; -. DR PATRIC; 20022296; VBIMycPne110_0485. DR OrthoDB; EOG6S52MH; -. DR BioCyc; MPNE272634:GJ6Z-478-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 448 Uncharacterized protein MG314 homolog. FT /FTId=PRO_0000210529. FT CONFLICT 169 169 R -> P (in Ref. 1; AAA61695). FT {ECO:0000305}. SQ SEQUENCE 448 AA; 50547 MW; BACE3D3120592B08 CRC64; MTFSDLLTKL QDNLDIVFNA NALKERIQSD PAFAKTIREQ LKLLYFLEQK QAKAKTKKKD FQPVFQNLEA RFVSLGQTKL ANTELNLKLD LTDATDLANY LPIAVCNLFN RDLNSFSKLS SVQPTAVEKT TNGANKPTVT IDLNQPRIHT TGTVSPELEN FVNESLEARA RQRAFMRVTS ERMVGKIFEF QFKSQWIKWA QLAIFISMLL IGAAAIAYLV VVNLLFYRYV NPDSNLTKAV TGQNNTDRPA LVDLNGGINL FFPVSASTLI TLIFLGFGST SFLLAFQGKP YSFATRSQTF KAMHFLKHQF GVTDFPRIND NYRYKVRIKW IFWTIFLFVA LNALPGGNII TGGILNPSFL LNALRSNELK INSETFKTIF VGFSIFYLAS IIPFALISII AFVLSPKPSS DQTNEVLNRY VQEEMQQPFK TDCDPNNDND LTPPAVFG // ID Y457_MYCPN Reviewed; 329 AA. AC P75326; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_457; GN OrderedLocusNames=MPN_457; ORFNames=H08_orf329V, MP384; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To the C-terminal of MG321/MPN_456. {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; U00089; AAB96032.1; -; Genomic_DNA. DR PIR; S73710; S73710. DR IntAct; P75326; 1. DR EnsemblBacteria; AAB96032; AAB96032; MPN_457. DR PATRIC; 20022320; VBIMycPne110_0494. DR OrthoDB; EOG6SFP68; -. DR BioCyc; MPNE272634:GJ6Z-489-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 329 Uncharacterized protein MPN_457. FT /FTId=PRO_0000210679. SQ SEQUENCE 329 AA; 36102 MW; CE96F88BB71AF2B6 CRC64; MWITTTPWSK HSPNWVLADN GEKLIVPEII LGDAQGPTRN EWYIGLSSVL GFSFWSPDYD GVGTWLDAAT QLNEQGGGDV ITYSSGAHIV RTLLLAASQS NVHSTFTSKA LGNDQTSSMT SSTTAVTVAK SGDGQQQTGE QKEEDWKDIS KADLFKDDPY VLKNFGDSTT QAKMQSGGST NSNGNGSQAS LAFTKKALSL LKFLVDNKIL KKDKVKEAIM NPDQYLSKRS KLDSNNQKPT KDDFIGSEFK DLYENAAKLN RFNSIWAEKD TDNAKFLITV VDSYFPVLPV PAAGLNETSP TLLKPWFQFR SAPSGNGTIR DYGFIPENK // ID Y478_MYCPN Reviewed; 235 AA. AC P75306; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Probable transcriptional regulatory protein MPN_478 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=MPN_478; ORFNames=MP363, P01_orf235; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96011.1; -; Genomic_DNA. DR PIR; S73689; S73689. DR RefSeq; NP_110166.1; NC_000912.1. DR RefSeq; WP_010874834.1; NC_000912.1. DR ProteinModelPortal; P75306; -. DR EnsemblBacteria; AAB96011; AAB96011; MPN_478. DR GeneID; 877384; -. DR KEGG; mpn:MPN478; -. DR PATRIC; 20022380; VBIMycPne110_0517. DR OMA; MKRWGNM; -. DR OrthoDB; EOG6HJ29R; -. DR BioCyc; MPNE272634:GJ6Z-519-MONOMER; -. DR Proteomes; UP000000808; 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 1 235 Probable transcriptional regulatory FT protein MPN_478. FT /FTId=PRO_0000175851. SQ SEQUENCE 235 AA; 25979 MW; 5EE485A47A0D2C73 CRC64; MPRKHLIASQ TNKKQQSNAK QLQKLAKRIA AAVKKGGSNI DANPQLKVAV ELALAHGLSA DSIKRNIHGS EKDPTKLSEF CYEIFGPNGV GIIVFGLTDN PNRLLSSLNG YIAKLKAQLA KPNSVKINFE EKGIALVKHN NFTQDELIEL LISNNINLLD LNEDDDSFEV VVDSPSYFAL KDLLVKNSFT IEASELRLIP LLTVELNAEQ HTLLNRFLNA CEEDDDIQTV VHNAL // ID Y501_MYCPN Reviewed; 196 AA. AC P75286; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=UPF0134 protein MPN_501; GN OrderedLocusNames=MPN_501; ORFNames=MP342, P02_orf196; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95989.1; -; Genomic_DNA. DR PIR; S73668; S73668. DR RefSeq; NP_110189.1; NC_000912.1. DR RefSeq; WP_010874857.1; NC_000912.1. DR ProteinModelPortal; P75286; -. DR EnsemblBacteria; AAB95989; AAB95989; MPN_501. DR GeneID; 877358; -. DR KEGG; mpn:MPN501; -. DR PATRIC; 20022440; VBIMycPne110_0547. DR OMA; KMDKMEV; -. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; MPNE272634:GJ6Z-542-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 196 UPF0134 protein MPN_501. FT /FTId=PRO_0000221610. SQ SEQUENCE 196 AA; 23165 MW; 165C0E960D1EFF48 CRC64; MKEKIPFYNE KEFHDMVKKT KKGTFSGWYI IDKDNNSVEF SGKFNRQFKL NKPVIPVNTE YVTRKEFNEY KNSNDQRLTK IETTLAAQGE QINKLTQTVE KQGEQINQLV QVVLLHGEQI NKLTQTVEKQ GEQIKELQIE QKAQGETLKL ILQTLQKMSD RLDKMEVKMD KMEVKMDKME VKMDKMEKRI DKLESK // ID Y525_MYCPN Reviewed; 413 AA. AC P75253; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MG349 homolog; GN OrderedLocusNames=MPN_525; ORFNames=G12_orf413, MP317; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95965.1; -; Genomic_DNA. DR PIR; S73643; S73643. DR RefSeq; NP_110213.1; NC_000912.1. DR RefSeq; WP_010874881.1; NC_000912.1. DR EnsemblBacteria; AAB95965; AAB95965; MPN_525. DR GeneID; 877354; -. DR KEGG; mpn:MPN525; -. DR PATRIC; 20022518; VBIMycPne110_0584. DR KO; K03346; -. DR OMA; WLITEAN; -. DR OrthoDB; EOG6RVFTF; -. DR BioCyc; MPNE272634:GJ6Z-568-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 413 Uncharacterized protein MG349 homolog. FT /FTId=PRO_0000210554. SQ SEQUENCE 413 AA; 48246 MW; A4CF2C9802316F23 CRC64; MQPNYYRVIK KATSFSGLDM ISHAYGQIAG VEVVGFYLWL ITEANAQAFN SEIRTPISRL QNAFNTTGTK NVNVPDWIYK TIGKLESLGL VRTFFSQEKS EMTFWIVEPL GWKEFNQKKH FKEKLIESMG KLEYDRNCLS FEQIDNIQFD NALEITANFE ANFTSKQDCL SFSFDFEAFH KQLVKQNLFV SFNQKTKAVI NGYFEKYQIT LEGILECVIP SVVNDEVDLE LLQKLLEQLV KNNTAPIVDT VINDRNFFYD NQNLATETKD AISRCHLEYN AEKYLFLLYG KVENEQLDLI RRLRQEFGIA DKVINLIVDF SFWKNNSMWR EQYILKIAES VERYRSHNNY QATLDNFIRA SSLAKKQRTK TKIEKSEPET SAAPVNETDD VNYFLNRIKA INKKNRENGK HKR // ID Y127_MYCPN Reviewed; 180 AA. AC P75348; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=UPF0134 protein MPN_127; GN OrderedLocusNames=MPN_127; ORFNames=C09_orf180, MP027; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95675.1; -; Genomic_DNA. DR PIR; S73353; S73353. DR ProteinModelPortal; P75348; -. DR EnsemblBacteria; AAB95675; AAB95675; MPN_127. DR OrthoDB; EOG6SV5BV; -. DR BioCyc; MPNE272634:GJ6Z-134-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 180 UPF0134 protein MPN_127. FT /FTId=PRO_0000221596. SQ SEQUENCE 180 AA; 21278 MW; 9131CEA153EFFB41 CRC64; MFKLKINNFQ LGFKLVQWPV TNHLLKHFYV FPINNKGGLA IKRIISLALF KKRLNKDKIN NCHVWEEELP DGSYDMGFNG NFNHMEKRKS GYVTQKQFSE FKDANNQRLI KIETTLAIQG EQINKLTQTV EKQGEQINQL VQVVLLQGAS KLENFKWSKK HKDKSLMPAW IVWKIFWWKV // ID Y147_MYCPN Reviewed; 485 AA. AC P75139; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MPN_147; GN OrderedLocusNames=MPN_147; ORFNames=E07_orf485, MP007; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95655.1; -; Genomic_DNA. DR PIR; S73333; S73333. DR ProteinModelPortal; P75139; -. DR EnsemblBacteria; AAB95655; AAB95655; MPN_147. DR PATRIC; 20021613; VBIMycPne110_0163. DR OMA; DSAIEYP; -. DR BioCyc; MPNE272634:GJ6Z-154-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 485 Uncharacterized protein MPN_147. FT /FTId=PRO_0000215278. SQ SEQUENCE 485 AA; 53348 MW; 57B5E5134286B966 CRC64; MVDFATRVAK SFKDKVSGID NKKGTDIQGV LGLDSTPNVL FASVFAAGGG SYDNFFYKVE NGRADFRNFA NKGTSYKNLE KVYNDYKNLI GSNGLFASKD GSYSSNFEKF HQLAFYVGSS SGYNYAFADE TAKRLKFGDS AIEYPNDTLE IKAPTNNSQS GDGNGGTNND NLLGTFDIRE KSNGKKGESN GKQGNGQDKK TISLYKDSIP KEKTEGTDAI LISDNQLINQ LQTAAKTSSS QNKANTAAIT FKQSNKSETD QSTTSQVIGY TTTASLKADK KNIFDVKKLN NEKSERKIIV GATVETLNQA NTLQANEAII KPAPGKYQST DSHKVMITQG PNIVGIHANE KEDKETQKFI NWYLNKEESW SVQNSGSTTT KKQTAAQYFA EQSSYITPLK NNFKADQSAT KDSTVNTNYF TKQTFDLFKE VNDGKVLGFN DPSDFRSGKF RNTIGSTFNA TISSKVDFNK FFENFKASLG SGFER // ID Y163_MYCPN Reviewed; 136 AA. AC P75582; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG149.1 homolog; GN OrderedLocusNames=MPN_163; ORFNames=MP668, VXpSPT7_orf112; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96316.1; 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; U00089; AAB96316.1; ALT_INIT; Genomic_DNA. DR PIR; S73994; S73994. DR RefSeq; NP_109851.1; NC_000912.1. DR ProteinModelPortal; P75582; -. DR EnsemblBacteria; AAB96316; AAB96316; MPN_163. DR GeneID; 877285; -. DR KEGG; mpn:MPN163; -. DR PATRIC; 20021649; VBIMycPne110_0181. DR OMA; FFWSILS; -. DR OrthoDB; EOG6QRWJT; -. DR BioCyc; MPNE272634:GJ6Z-170-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 136 Uncharacterized protein MG149.1 homolog. FT /FTId=PRO_0000210447. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 136 AA; 15939 MW; 24433EC73A8088E8 CRC64; MACKRQTSLE KDKELVSSIV TAKSMIDRFF WSILSFLLTN LVFLFVAFLI LIIYLISEIT QQFAFAFIAT IVFIIFYNIL FLSYLLTMYI KGLKQIEQKS RYLLLVLDVK ADELLPFSFL GSLRKSHMLE EMLLEQ // ID Y199_MYCPN Reviewed; 760 AA. AC Q50289; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MPN_199; DE Flags: Precursor; GN OrderedLocusNames=MPN_199; ORFNames=GT9_orf760, MP632; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U34795; AAC43682.1; -; Genomic_DNA. DR EMBL; U00089; AAB96280.1; -; Genomic_DNA. DR PIR; S62792; S62792. DR RefSeq; NP_109887.1; NC_000912.1. DR RefSeq; WP_010874556.1; NC_000912.1. DR PRIDE; Q50289; -. DR EnsemblBacteria; AAB96280; AAB96280; MPN_199. DR GeneID; 876847; -. DR KEGG; mpn:MPN199; -. DR PATRIC; 20021721; VBIMycPne110_0217. DR OrthoDB; EOG6VB6X7; -. DR BioCyc; MPNE272634:GJ6Z-206-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 760 Uncharacterized lipoprotein MPN_199. FT /FTId=PRO_0000018727. FT LIPID 21 21 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 21 21 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 760 AA; 84150 MW; FC5AC0D7AE96AAB3 CRC64; MKFKLFLGSS FFGVATLLIA CGTGRFDQID DGKIKLAVVT SPSAASSLQT LLDQYNNTKA PADYPVEVVS LDSTGSYTKG KFDTQKRLAA KDKNNFYNLT FNYPDLVSSL AINGMELNLD GVNVSNFEQS FLDFNKNISG VRKPGIYALP ATMSGEVLVL NGPVLHYILN SAKKKDGTES KIKTAQLKTA STQAEVKGTM TMASDEQTTK LWTNIQNAAK ENAANGTTEK AEKTVSASSL QLKNTNKTTE GTLKIGTDDN TKNLWKKIED AAKTNGEKGN EKQEATQSNA SASLVKLDQK NTSQDKTQNT QTSDDEIKKS WGEYKEVEGG LKGYEFKADV FESWEKLNDF AVRVAKSFSK VSEEKKSGSD IQGVFGIGSL ENALYTASFA AGGGDYNNFL FNIKKGRADF SNFFNHNSKT FQSLRDIFNS FKPLIDQKGL ISNKHFDTPV NNYAKFHQLA FYVSSTARFP YSFAKDNVKR LIIGKRELEV NPKSMFAIKK ENGNNGNSNL LGKVALDNNK SIELYENNIP NGKTDAILIK NQTLISALKN PKQTKSSQRS SQSTNTQNDA ICYLAFNSKI RPDDKDIFLL DKFGEKFVTA IVNFEEKTEV KINTLQEKEA VVLPAPQKFK PTDPKSVALV QGPSLIGIHA NANEDRSTIK FLNWYLNAEV DWKDGEKKTP AEYLAEKASY LLPFKKVLEK SKQNIKATSK EGEQNQGKKG DGAQNQGKKG DGAQNGKNDK AKHNGFCRYC RQPIFKRFCR // ID Y202_MYCPN Reviewed; 313 AA. AC Q50286; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Putative adhesin P1-like protein MPN_202; GN OrderedLocusNames=MPN_202; ORFNames=GT9_orf313, MP629; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U34795; AAC43679.1; -; Genomic_DNA. DR EMBL; U00089; AAB96277.1; -; Genomic_DNA. DR PIR; S62808; S62808. DR RefSeq; NP_109890.1; NC_000912.1. DR RefSeq; WP_010874559.1; NC_000912.1. DR EnsemblBacteria; AAB96277; AAB96277; MPN_202. DR GeneID; 876985; -. DR KEGG; mpn:MPN202; -. DR PATRIC; 20021729; VBIMycPne110_0221. DR BioCyc; MPNE272634:GJ6Z-209-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 313 Putative adhesin P1-like protein MPN_202. FT /FTId=PRO_0000210710. SQ SEQUENCE 313 AA; 33407 MW; CB7B0DBC8F427A84 CRC64; MGSQNQGSTT TTSAGNPDSL VTDKVDQKGQ VQTSGQNLSD TNYTNLSPNF TPTSDWPNAL SFTNKNNAQR AQLFLHGLLG SIPVLVNKSG ENNEKFQATD QKWSYTELKS DQTKLNLPAY GEVNGLLNPA LVETYFGTTR TSSTANQNST TVPGIGFKIP EQNNDSKAVL ITPGLAWTPQ DVGNLVVSGT SFSFQLGGWL VSFTDFVKPR AGYLGLQLTG LDASDATQRA LIWAPPALSG LSWQLGQPVG PRGECVGFEG GVGGSSSVRL ARIYHHRNRG YLTGAPECFG LSGECGGSEC LQAKHELRPN PIH // ID Y276_MYCPN Reviewed; 285 AA. AC P75501; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG135 homolog; GN OrderedLocusNames=MPN_276; ORFNames=A65_orf285, MP559; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96207.1; -; Genomic_DNA. DR PIR; S73885; S73885. DR RefSeq; NP_109964.1; NC_000912.1. DR RefSeq; WP_010874633.1; NC_000912.1. DR ProteinModelPortal; P75501; -. DR EnsemblBacteria; AAB96207; AAB96207; MPN_276. DR GeneID; 876846; -. DR KEGG; mpn:MPN276; -. DR PATRIC; 20021879; VBIMycPne110_0296. DR OMA; INANDWE; -. DR OrthoDB; EOG6SJJGV; -. DR BioCyc; MPNE272634:GJ6Z-283-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 285 Uncharacterized protein MG135 homolog. FT /FTId=PRO_0000210439. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. SQ SEQUENCE 285 AA; 32050 MW; B2164AC3975176C0 CRC64; MQSLNYLVVI LTVAGVLVIL GFTPLIRKLK IQFYCLQVFA AILFLYVFFG RQIIYIFPDI YGTAAKAKNA VANVPLDSLR LSRIFLLDLC PFFALIGPIF IFLRQKKVAG VLAIFGFYGA AITLFGELIF TPLKQEEIVK FLFVGLENNQ VYFMMHFLSF LLSLAVFLWD DGFSLISFFY IHVFALAYLS YVALMVNIFK GQITGNTTGI LAEDWLSGEY KNVAVFLKLD PKNADLIFGV SFGLSYFAIV LLTVLVNIPT FIQLTKDKQM VKLALQLKKA QASVA // ID Y313_MYCPN Reviewed; 90 AA. AC P75468; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MG220 homolog; GN OrderedLocusNames=MPN_313; ORFNames=F10_orf90, MP523; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96171.1; -; Genomic_DNA. DR PIR; S73849; S73849. DR RefSeq; NP_110001.1; NC_000912.1. DR RefSeq; WP_010874669.1; NC_000912.1. DR EnsemblBacteria; AAB96171; AAB96171; MPN_313. DR GeneID; 876930; -. DR KEGG; mpn:MPN313; -. DR OMA; YSYKRRN; -. DR OrthoDB; EOG6TFD10; -. DR BioCyc; MPNE272634:GJ6Z-329-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 90 Uncharacterized protein MG220 homolog. FT /FTId=PRO_0000210464. FT TRANSMEM 12 32 Helical. {ECO:0000255}. SQ SEQUENCE 90 AA; 9808 MW; 22501320C6148406 CRC64; MQRLKKSEAK QVVGGLSFWS FSAGVIMIVN AFSTLINTAL DISEAANANN ANGNGSSYSY KRRNSQKDYF STGRFRLGLT PGKSSYSFPV // ID Y316_MYCPN Reviewed; 419 AA. AC P75465; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MG223 homolog; GN OrderedLocusNames=MPN_316; ORFNames=F10_orf419, MP520; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96168.1; -; Genomic_DNA. DR PIR; S73846; S73846. DR RefSeq; NP_110004.1; NC_000912.1. DR RefSeq; WP_010874672.1; NC_000912.1. DR IntAct; P75465; 2. DR EnsemblBacteria; AAB96168; AAB96168; MPN_316. DR GeneID; 876887; -. DR KEGG; mpn:MPN316; -. DR PATRIC; 20021984; VBIMycPne110_0339. DR OMA; FMDNALV; -. DR OrthoDB; EOG65QWFP; -. DR BioCyc; MPNE272634:GJ6Z-333-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 419 Uncharacterized protein MG223 homolog. FT /FTId=PRO_0000210466. SQ SEQUENCE 419 AA; 48781 MW; E15F53E8C5E90F91 CRC64; MYNLKNIYAS ITLYPHEINL VVSDNNNQFH VLYENSIAND ELYTHAGITN KAKFKVVLNQ LINNANDYLG FKLEKVIVVL AELVDDLEIN RFKTDVFFTG YDFNHQDMLS SEKNRFLLKN RHINPNEVLD LVALNYRDLT TDKISKNFKY NCSYRANVIY YTTKNSLVKE LKPFLKRNII VKIDKIVTHH MVLAHSIKQI NKNNLFVYLG EHTTDLMLFM DNALVDLVSE PFGRVNFLES DNDSENKALL EFLVDSTARI GDSGSIGMAY TDGSTYKEIR AVTIDDLIQS VNEKTKYLID FINTNTEIFF QKYGFLPSTL LFYTKSKQLL NNFQLNQNLL SNHFKTVTIF KNEVQFVSRK YLLNCQTIAL SWRQDQINVN PTSFALPFYS DKIEKQFKKS FLMLKVHTHI NKLVQKLIK // ID Y344_MYCPN Reviewed; 216 AA. AC P75434; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=UPF0134 protein MPN_344; GN OrderedLocusNames=MPN_344; ORFNames=H91_orf216, MP492; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96140.1; -; Genomic_DNA. DR PIR; S73818; S73818. DR RefSeq; NP_110032.1; NC_000912.1. DR RefSeq; WP_010874700.1; NC_000912.1. DR ProteinModelPortal; P75434; -. DR EnsemblBacteria; AAB96140; AAB96140; MPN_344. DR GeneID; 877337; -. DR KEGG; mpn:MPN344; -. DR PATRIC; 20022042; VBIMycPne110_0368. DR OMA; FTIIEDQ; -. DR OrthoDB; EOG6RRKW3; -. DR BioCyc; MPNE272634:GJ6Z-361-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 216 UPF0134 protein MPN_344. FT /FTId=PRO_0000221606. SQ SEQUENCE 216 AA; 25343 MW; 30ED658700119BDA CRC64; MPKIISKRKF NILRKTKEEI FSQIVYTKKR NGLHKAAKEY YFKDKDFTII EDQQDRPDKP EELDTPDIPK PPKPPKGPDQ PEEPGQPGGP DDPNSGNKKM PKPDEFVTHR QLQEFKKDLL VELHEIFPTK PELKRVEEKV DVLFELQKAQ GEQIRIQGEQ IKELKVEQKA QGETLQLILQ TLQKMNDRLD KIEGKMDKME SRMDKMETRL DKLESK // ID Y363_MYCPN Reviewed; 102 AA. AC P75418; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized lipoprotein MPN_363; DE Flags: Precursor; GN OrderedLocusNames=MPN_363; ORFNames=H91_orf102, MP473; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96121.1; -; Genomic_DNA. DR PIR; S73799; S73799. DR RefSeq; NP_110051.1; NC_000912.1. DR RefSeq; WP_010874719.1; NC_000912.1. DR IntAct; P75418; 1. DR EnsemblBacteria; AAB96121; AAB96121; MPN_363. DR GeneID; 876956; -. DR KEGG; mpn:MPN363; -. DR PATRIC; 20022092; VBIMycPne110_0390. DR OrthoDB; EOG6VB6X7; -. DR BioCyc; MPNE272634:GJ6Z-383-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 102 Uncharacterized lipoprotein MPN_363. FT /FTId=PRO_0000018732. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 102 AA; 10829 MW; 6B9215D06B52BCE4 CRC64; MKFKYGATLF SGFLGLSAIL AACGAKGKFD QVDDGKIVLA SSLTSKNAAN ALQAVVEKYN QVKGGNDYPI EITQITGGYD GGRGNLQTKL SVKDKTTFYN LI // ID Y370_MYCPN Reviewed; 737 AA. AC P75411; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Putative adhesin P1-like protein MPN_370; GN OrderedLocusNames=MPN_370; ORFNames=A19_orf737V, MP466; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96114.1; -; Genomic_DNA. DR PIR; S73792; S73792. DR RefSeq; NP_110058.1; NC_000912.1. DR RefSeq; WP_010874726.1; NC_000912.1. DR EnsemblBacteria; AAB96114; AAB96114; MPN_370. DR GeneID; 876868; -. DR KEGG; mpn:MPN370; -. DR PATRIC; 20022114; VBIMycPne110_0401. DR BioCyc; MPNE272634:GJ6Z-390-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 737 Putative adhesin P1-like protein MPN_370. FT /FTId=PRO_0000210713. SQ SEQUENCE 737 AA; 78906 MW; DAD0132C546133CF CRC64; MLKLAVGIFI SPTLTRFSTG FNLAGSVLDQ VLDYVPWIGN GHRYGNNHRG VDDITAPKTG AGSSSGTSTN TSGSRSFLPT FSNVGVGLKA NVQGTLGGSQ TTTTGKDIPK WPTLDPANLQ LWTGAGWRND KASNKQSDEN HTTFKSATGS GQQGGSTTGG SAGNPDSLKQ DKISKSGQNL TTQDGAPQSN STTESASNYD HLPPNLTPTS DWPNALSFTN KNNAQRAQLF LRGLLGSIPV LVNRSGSDDS NKFQATDQKW SYTDLKSDQT KLNLPAYGEV NGLLNPALVE TYFGTTRAGG SGSNTTSSPG IGFKIPEQNN DSKAVLITPG LAWTPQDVGN LVVSGTSLSF QLGGWLVTFT DFVKPRAGYL GLQLTGLDAS DATQRALIWA KRPWAAFRGS WVNRLGRVES VWDLKGVWQD QAQAAAQAAT TAAATGDALP EHPNALAYQI SSTDKDSYKA STQSSGQTNS QNTSPYLHLI KPKKVENTTQ LDQGLKTCWT PTRFAPSCAK ALVQTIPPKP NPNPSKQPHR CLGRIVVTLA VCLVVGVLEE QTAPIRWTSP PLNGWVGGLW GNYPVGVGGI VVRILKVCKT LLFISIFISI FFLNCSLTLF IWTTASLATG LTVVGHFTST TTTLKRQQFS YTRPDEVALR HTNAINPRLT PWTYRNTSFS SLPLTGENPG AWALVRDNTA KGITAGSGSQ QTTYDPTRTE AALTTATTFV LRRYDLAGRC TTSTFRS // ID Y440_MYCPN Reviewed; 726 AA. AC P75338; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MPN_440; GN OrderedLocusNames=MPN_440; ORFNames=H08_orf102, MP401; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96049.1; -; Genomic_DNA. DR PIR; S73727; S73727. DR RefSeq; NP_110128.1; NC_000912.1. DR RefSeq; WP_010874796.1; NC_000912.1. DR IntAct; P75338; 1. DR EnsemblBacteria; AAB96049; AAB96049; MPN_440. DR GeneID; 877071; -. DR KEGG; mpn:MPN440; -. DR PATRIC; 20022278; VBIMycPne110_0476. DR OMA; YENETNA; -. DR BioCyc; MPNE272634:GJ6Z-469-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 726 Uncharacterized protein MPN_440. FT /FTId=PRO_0000210677. SQ SEQUENCE 726 AA; 80934 MW; C2E0D644935DB644 CRC64; MQQQGETKDQ YNTFGLRLVR NSVGVSVLGL DGFVKFIKGG SGGSNGGSSS AKKIDKEEQK KFLKFRAFQA KIGTFYNTNF AFSFPLNETL KGWFDKHRGL ILANALVKVT LDTKEKASKA LVDAFSSYKN WLSEYTPVGL ATTMISFYFD QMKALNNKLL ERVRSLNQNV NQANPTPWLN GLSAKLPYVN TNGNYEKLNN YFTFLITKVL WPKVGTEDTN VSEEKSKLKT KTEDVNKIRE KILNNIDSKL KTFVQKLKPT LAPRPAYSNV ILLNINNDKV WSAGANWSLA VLLDPKKVNP LSFMLLKQMF DQNSLFKKAK TLFENIQNKA KTSGSGKSGT TTNDDADALS KVIGNYYYNT WAKLTDKSIY GNLKDDKFDD LFKLAFDSSI NEKSFNVDYK AVIEHYRFIY TLEWLVDKNL KNFKDLLKAN LKFGEIAFIA YKNTETQNFS NPQGIFGSYF NYENETNAAK SATQIIDPNS FFYKTTTKPE AKTTQSANTA VMVQNTQMNN QQTNSYGFTG LSTSSGSMLG AATQQAILDQ ITKTSLQQYG SQADLKKIIG ETKNQLLLDR IANQLIALKP NTSGNSGTQK TIAAYFQTDA VGNPTLDFKA KQKLLLDVLD QYKDFFGNNA QAVQRDSGKS GTGNYLTYTD GSDKITYLQF SYKDIDGLSL SSSNGTSSKF ASDVVAALLL FQAAYKGTQQ LALSSINKPQ LPIGDKRIKT GIDLLK // ID Y454_MYCPN Reviewed; 193 AA. AC P75329; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG319 homolog; GN OrderedLocusNames=MPN_454; ORFNames=H08_orf193, MP387; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96035.1; -; Genomic_DNA. DR PIR; S73713; S73713. DR RefSeq; NP_110142.1; NC_000912.1. DR RefSeq; WP_010874810.1; NC_000912.1. DR IntAct; P75329; 1. DR EnsemblBacteria; AAB96035; AAB96035; MPN_454. DR GeneID; 877070; -. DR KEGG; mpn:MPN454; -. DR PATRIC; 20022308; VBIMycPne110_0491. DR OMA; DVFNRFF; -. DR OrthoDB; EOG6S7Z3T; -. DR BioCyc; MPNE272634:GJ6Z-483-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 193 Uncharacterized protein MG319 homolog. FT /FTId=PRO_0000210535. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. SQ SEQUENCE 193 AA; 21443 MW; BAEE6806C6D80C1D CRC64; MGFFKLLFKL AFLAVLTVAI AYLFLAIFYF GTVSPSFKLA QPMDVFNRFF SKEALDTVTT SGVGATVTAP KAAAASQSHA LILAAEQVAN NANKLDPRFP IDGSLFSQIP GYVDFLKKPN IPAFLEKVGP YLTKYIIPLG MALVSGLIGA LIINFILSKI TRAIIKKRRK AKRAQQSRVD DYYYDEAPRR RRR // ID Y468_MYCPN Reviewed; 208 AA. AC P75315; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Putative adhesin P1-like protein MPN_468; GN OrderedLocusNames=MPN_468; ORFNames=MP373, P01_orf208V; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96021.1; -; Genomic_DNA. DR PIR; S73699; S73699. DR RefSeq; NP_110156.1; NC_000912.1. DR RefSeq; WP_010874824.1; NC_000912.1. DR EnsemblBacteria; AAB96021; AAB96021; MPN_468. DR GeneID; 877389; -. DR KEGG; mpn:MPN468; -. DR PATRIC; 20022358; VBIMycPne110_0506. DR OMA; WRNDSKT; -. DR BioCyc; MPNE272634:GJ6Z-507-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 208 Putative adhesin P1-like protein MPN_468. FT /FTId=PRO_0000210715. SQ SEQUENCE 208 AA; 21805 MW; 67992427E40217B1 CRC64; MLDYIPWIGN GYRYGNGYKG VAGAGHSATN GSPAGNTSST TQSNDVAPTF SNVGVGLKAN VQGTLGDSQT TTVGGHQWPT LDPANLQLWT GAEWRNDSKT QNNTTTNENH TKFASATGSG QQQGSTTTTS AGNPDSLKQD KADKSGNSIS VQEATSGDNL TNYTNLPPNL TPTSDWPNAL SFTNKNNAQR AQLFLRGLLG SIPVLVNN // ID Y469_MYCPN Reviewed; 243 AA. AC P75314; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG323.1 homolog; GN OrderedLocusNames=MPN_469; ORFNames=MP372, P01_orf243; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96020.1; -; Genomic_DNA. DR PIR; S73698; S73698. DR RefSeq; NP_110157.1; NC_000912.1. DR RefSeq; WP_010874825.1; NC_000912.1. DR ProteinModelPortal; P75314; -. DR EnsemblBacteria; AAB96020; AAB96020; MPN_469. DR GeneID; 876796; -. DR KEGG; mpn:MPN469; -. DR PATRIC; 20022360; VBIMycPne110_0507. DR OMA; YLFYSRF; -. DR OrthoDB; EOG6JDWF7; -. DR BioCyc; MPNE272634:GJ6Z-510-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 243 Uncharacterized protein MG323.1 homolog. FT /FTId=PRO_0000210542. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 204 224 Helical. {ECO:0000255}. SQ SEQUENCE 243 AA; 28278 MW; DFD7355C3DD876FE CRC64; MSKINDKLTE INTVEYEVAS KHSQYLFYSR FGLLDTAAYF LFLLSFFVTA VMFLVGIFHT EQFTLNDQNQ GISGFYLFWN VKKPADIFNA NFVYSISSFG IAILALGLFS LFLMIFLGYR WAISLFIKSQ ITKWERVIFS TGFYFSVVAY CFWIALMLLF LVLSDQHFFP RTTTQLKSNP NLSLFFRISH KDNVFSSRLN QLGAFATALC ITLVVYELPF LGLFAFNWNK QRAKAIFCRK RKQ // ID Y489_MYCPN Reviewed; 1300 AA. AC P75296; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 71. DE RecName: Full=Uncharacterized lipoprotein MG338 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_489; ORFNames=MP353, P02_orf1300; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96001.1; -; Genomic_DNA. DR PIR; S73679; S73679. DR RefSeq; NP_110177.1; NC_000912.1. DR RefSeq; WP_010874845.1; NC_000912.1. DR EnsemblBacteria; AAB96001; AAB96001; MPN_489. DR GeneID; 877211; -. DR KEGG; mpn:MPN489; -. DR PATRIC; 20022404; VBIMycPne110_0529. DR OMA; NVEDEHD; -. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MPNE272634:GJ6Z-530-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 1300 Uncharacterized lipoprotein MG338 FT homolog. FT /FTId=PRO_0000014037. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1300 AA; 143063 MW; B8236A003A9879DB CRC64; MGYKLKRWPL VAFTFTGIGL GVVLAACSAL NTSNLFPRQN RSKQLIGFTE NNIIKPEAVL KAALAEDNGT ETILRVNFGE ALKSWYQNNK DRNIATRLTI FSENVEDEHD NLLDQKQQAE PINWPIELQK EYDQWGGSES SWKALKLYDR LIADFQSLIF SNIVANVQLT DGSDQFKPTT KDNLDSTSNK IKFVNSKPND PNGEFFANLQ AYLFAQWVVE ENPLPLTQAF FAYQAPKDGL DSLYDQAAIG SALQLGYAFP AFREPNNGQS QGKTTFDPTP NSAQNFGDFI KAVFPEQKNG QTQQSNTSSR TGLFDWQTKW NTNGAANKLL VTKSNLRGAF KGVGLATAII DQYEYLVGGS KTSSLPEVKV DSNKSNQNPL DSFFMEGKDA VAIRSIVSRA KIAMTDQTPG FKVNPAFVKV KQSQQNDTFY QNQRKLSGGQ SGDNNSQGKH HYLQDAVRLT SSQAMAAAST GADSSSGTNV GGSSGGNSVL IPLPRSAALT HTQQQVQQTT STLQTPVYAR GDDGTYALAI DGGDYFLANN KRDFTKQADI LLYRYLQAKS NNFKENGVEF SLNLLESGSL FQTWAQTGLT AKLYGALVAM MGSGQGTQVK GSVQGSSRAA SVSVQTTQQN RQQSTDTQES EVVKLAKSLL KSSADLAKPF TDNPTFKKAL TDIQSEYKDY LAAAGKLSEF KKDLGEVSGL QQAIIDRADK YIQLEKQAQK SAIGLGQPLP YQRASDGSYP ALEKFFIPED SAADGKVKAS ESGSAALVTL KTTDSQKSTN TVKQPDIKPT RENNDKKLKQ LTSDVETKAS SLITKWGATP QIGSQFSEIV SLKSKDNKPQ TNMILALLSD VGIKWTKILN SFKEWFFTNT NDFKNNYDSE KKELKGNEYK DFNDLVKQTL YLRSWQRLTS KEKFGYYKEL GSVKAQAAQS GMVSLSSSAA VANAVASSGM QKSGDQTLLE LGKKAFESEL EASSSDGQYK YLRFLSTLMW LVKDGAKNYK RLLQQAITVG TRAFVSWTVS YDDTATASAA AAKAQVAVLK TAQATNTQSD NPFNKFVQNP DYVQGSETNW FNDKSTPIKP DSLLESESTY NFTAEPFDDK TKSQKRSTGG TTNEKHFFGF NGLTINSPQS VSTASAGLTE QIFNNFGQLV TSSDKSGALS QYKDKATLKR LIQNTNSDAE LNAFGEVLHR AVNVDTSNLG RFNSSGEPLI SFDNKKKFLV DVVDKLDDVY FNKFEGYVGQ TKVKMSDSSS SSQGTKTIRK PKPHHSPRTR VSRLWAMSFR LPTRTLTKFL LVEKLIRTVL // ID Y497_MYCPN Reviewed; 351 AA. AC P75290; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2015, sequence version 4. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MPN_497; GN OrderedLocusNames=MPN_497; ORFNames=MP346, P02_orf143; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00679}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00679}; CC -!- INTERACTION: CC P75604:MPN_089; NbExp=1; IntAct=EBI-2259752, EBI-2259729; CC -!- SIMILARITY: Belongs to the phosphotriesterase family. CC {ECO:0000255|PROSITE-ProRule:PRU00679}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAB95994.1; Type=Erroneous termination; Positions=54; Note=Translated as Glu.; Evidence={ECO:0000305}; CC Sequence=AAB95994.1; Type=Erroneous termination; Positions=209; Note=Translated as Gln.; Evidence={ECO:0000305}; CC Sequence=AAB95994.1; Type=Frameshift; Positions=278; 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; U00089; AAB95994.1; ALT_SEQ; Genomic_DNA. DR PIR; S73672; S73672. DR RefSeq; NP_110185.1; NC_000912.1. DR IntAct; P75290; 3. DR EnsemblBacteria; AAB95994; AAB95994; MPN_497. DR GeneID; 877244; -. DR KEGG; mpn:MPN497; -. DR PATRIC; 20022424; VBIMycPne110_0539. DR KO; K07048; -. DR OrthoDB; EOG628F2X; -. DR BioCyc; MPNE272634:GJ6Z-538-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009056; P:catabolic process; IEA:InterPro. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001559; Phosphotriesterase. DR PANTHER; PTHR10819; PTHR10819; 1. DR Pfam; PF02126; PTE; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 351 Uncharacterized protein MPN_497. FT /FTId=PRO_0000205368. FT METAL 23 23 Zinc 1; via tele nitrogen. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 25 25 Zinc 1; via tele nitrogen. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 151 151 Zinc 1; via carbamate group. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 151 151 Zinc 2; via carbamate group. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 184 184 Zinc 2; via pros nitrogen. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 212 212 Zinc 2.; via tele nitrogen. FT {ECO:0000255|PROSITE-ProRule:PRU00679}. FT METAL 270 270 Zinc 1. {ECO:0000255|PROSITE- FT ProRule:PRU00679}. FT MOD_RES 151 151 N6-carboxylysine. {ECO:0000255|PROSITE- FT ProRule:PRU00679}. SQ SEQUENCE 351 AA; 39121 MW; E72651DB2ECD69DD CRC64; MKRFVRTVLG DIDPKDLGIC DCHDHLIKNW GPEAKEHPDF VMLSNEAAIK ECLEFVHHGG RSIVTMDPPN VGRDVKRMVA IAEQLKGKLN IIMATGFHKA AFYDKGSSWL AQVPVNEIVP MLVAEIEEGM DLYNYSGPVV KRGKAKAGII KAGTGYAAID RLELKALEAV AITSITTGAP VLVHTQLGTM AYEAAQHLID FGVNPRKIQL SHLNKNPDEY YYAKIIRELG VTLCFDGPDR VKYYPDCLLA KHIKYLVDLG FVKHITLALD AGRVLYQKHY GLEKGKECFG FAYLFERFIP LLKEVGVSDA AINTILVENL AEILAFDAPR QFNPKAVHPR VLALKKQLKI E // ID Y506_MYCPN Reviewed; 793 AA. AC P75280; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MPN_506; DE Flags: Precursor; GN OrderedLocusNames=MPN_506; ORFNames=MP336, P02_orf793; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95984.1; -; Genomic_DNA. DR PIR; S73662; S73662. DR RefSeq; NP_110194.1; NC_000912.1. DR RefSeq; WP_010874862.1; NC_000912.1. DR ProteinModelPortal; P75280; -. DR EnsemblBacteria; AAB95984; AAB95984; MPN_506. DR GeneID; 877247; -. DR KEGG; mpn:MPN506; -. DR PATRIC; 20022456; VBIMycPne110_0555. DR OMA; LAIVNKY; -. DR BioCyc; MPNE272634:GJ6Z-547-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 793 Uncharacterized lipoprotein MPN_506. FT /FTId=PRO_0000018734. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 793 AA; 87494 MW; 331C6F077A718970 CRC64; MKFKYGAIFF SGFLGLSAIL AACGTKGKFD QVDDGKIKLA SSLTSKSASK ALQAIVKKYN EVKKPGDYPI EITQIAGGYD GGRSDLQTRV NVKDTTNFYN LILNYPDLVS TLGRVGMELP FDNVKVDKLS PRFLDFNNRI SAISKPGIYG IPVSLSTEVL SINGPVLHYI LNNAKKKEGT LNQKMTSSSE GKNSSGTLTV ATDTETSSLW KKIEDSAKAN GKSDEKGKGK KKDNKSATFS LVQLKQTQEK TDDSQDTKNS DDQVKKSWGE YQEVDGVLKN FEFKASIFEN WHDLLDFSTR VAKSFKKIHE NSNKKGNDIQ GILGVDSTPN SLFTSVFAAG GGDYNNFFYK IENGRADFSN FKNKGTSYQN LQKVFGDFKG LIDKNGIFVN KGGSYSSNFQ KFHQLAYSIS STSGFFYSFA GKSAKRLNFG DSFIEYPRFT QEIKAPSKNG ENGQTNEGNS TNGEQNLLGT FEVKDDSKPK EEVKSNKNSG KESSQNQGKK SNNNKTIYLY ETKIPDGKTA GDNAILIKDK NVIEKLKSAA KEENKEQTAE ATKAAITSNK AKSTKKESSK VIGYTTTDSV REDGKNIFAI DRVNGENYDR KIIVGAKAET LNQSSTLQSE EAIVLPAPGK YLNGDPKKVT ITQGPNIIGI HANEKENAET QKFVDWFLNS PQTWEKQSRD KKGSSEKQTA AEFFAESASY ILPLKEIFDK NDTKTEKGKN SKTQQRTNTY AEKALELFKQ ISQNQIVSYS DPSDFRSGKF RDAIGATFNA AVSSKADFNK FVQNFTATLG SDI // ID Y514_MYCPN Reviewed; 120 AA. AC P75272; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MPN_514; GN OrderedLocusNames=MPN_514; ORFNames=F04_orf120, MP328; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95976.1; -; Genomic_DNA. DR PIR; S73654; S73654. DR RefSeq; NP_110202.1; NC_000912.1. DR RefSeq; WP_010874870.1; NC_000912.1. DR IntAct; P75272; 1. DR EnsemblBacteria; AAB95976; AAB95976; MPN_514. DR GeneID; 876814; -. DR KEGG; mpn:MPN514; -. DR PATRIC; 20022482; VBIMycPne110_0568. DR OMA; IFLNEEC; -. DR BioCyc; MPNE272634:GJ6Z-555-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 120 Uncharacterized protein MPN_514. FT /FTId=PRO_0000210692. SQ SEQUENCE 120 AA; 13655 MW; 129124FB0996765D CRC64; MEQDINNQTG KKIFLNEECF LELDKLPQHV SVLGVSGFGK SNILLHFLKY AIDNDHPLIF VNGKGDKELI TQFEHYQTSA KQLSPEDGFD TVKLVALKNT SAKIWSLDDR IATIKYNPFK // ID Y547_MYCPN Reviewed; 558 AA. AC P75231; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG369 homolog; GN OrderedLocusNames=MPN_547; ORFNames=G12_orf558, MP295; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 DhaL domain. {ECO:0000255|PROSITE- CC ProRule:PRU00813}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95943.1; -; Genomic_DNA. DR PIR; S73621; S73621. DR RefSeq; NP_110236.1; NC_000912.1. DR RefSeq; WP_010874904.1; NC_000912.1. DR ProteinModelPortal; P75231; -. DR IntAct; P75231; 1. DR EnsemblBacteria; AAB95943; AAB95943; MPN_547. DR GeneID; 876730; -. DR KEGG; mpn:MPN547; -. DR PATRIC; 20022571; VBIMycPne110_0609. DR KO; K07030; -. DR OMA; IMEETIK; -. DR OrthoDB; EOG60PHBN; -. DR BioCyc; MPNE272634:GJ6Z-592-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro. DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro. DR InterPro; IPR019986; DAK2_dom-cont_prot_YloV. DR InterPro; IPR004007; DhaL_dom. DR InterPro; IPR033470; UPF_DhaK. DR Pfam; PF13684; Dak1_2; 1. DR Pfam; PF02734; Dak2; 1. DR SMART; SM01121; Dak1_2; 1. DR SMART; SM01120; Dak2; 1. DR SUPFAM; SSF101473; SSF101473; 1. DR TIGRFAMs; TIGR03599; YloV; 1. DR PROSITE; PS51480; DHAL; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 558 Uncharacterized protein MG369 homolog. FT /FTId=PRO_0000210571. FT DOMAIN 7 206 DhaL. {ECO:0000255|PROSITE- FT ProRule:PRU00813}. SQ SEQUENCE 558 AA; 62438 MW; 36B77146BBF2F656 CRC64; MSTVNLSNFI DMLRLGCKNI ANNFEYINQL NVFPVPDGDT GTNMKVTLSE AFKKLESEIS HIKSFSDLGK SFTRDLLLFS RGNSGVIFSQ IMKGFFSDMI STKTATETEL GIEDFATAFI KAEEVAYKNV SKPVEGTMLT VIRLISTDFK NQKNRAKTVQ KLFEQVIKTA WQTVKKTPQM LPVLKASGVV DSGAYGFACF LEGMLSFYGE KATLNDGKLT SAELSQMTIS GEKHVTEEEF GYCTEYVLKL GMSVSQEVEK QKFNQKKFES KVSKIATSVV VASDKDNGFV KVHAHTEKPN LLLELGLNYG EFELVKIENM NLQVAKQKPA PVKRNIKPAI VVTVPTEAFA DRIREDYDIQ AILCTDDTGA PSVFSLLEAV KLTHSSNIIF LLHDKNYFLS ANEALKQLKH QKISADCVMT TNPIESLAAL TVFNSDLNIH TNVKTMRRFV KGFASATITQ ASKKYKENRI EVNKGDFIAV ANNSICVSEK ELVQCVFNTI DHLLKKVKKP EFLLAYYGKD ITAEEAEAMK EKIEKKYKLF CEFSPGEQKV FSYILGIQ // ID Y551_MYCPN Reviewed; 281 AA. AC P75227; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 68. DE RecName: Full=Uncharacterized protein MG373 homolog; GN OrderedLocusNames=MPN_551; ORFNames=G12_orf281, MP291; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95939.1; -; Genomic_DNA. DR PIR; S73617; S73617. DR RefSeq; NP_110240.1; NC_000912.1. DR RefSeq; WP_010874908.1; NC_000912.1. DR ProteinModelPortal; P75227; -. DR IntAct; P75227; 6. DR EnsemblBacteria; AAB95939; AAB95939; MPN_551. DR GeneID; 877295; -. DR KEGG; mpn:MPN551; -. DR PATRIC; 20022579; VBIMycPne110_0613. DR OMA; RICLTYQ; -. DR OrthoDB; EOG6QP0XX; -. DR BioCyc; MPNE272634:GJ6Z-596-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR Gene3D; 3.90.320.10; -; 2. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR019080; YqaJ_viral_recombinase. DR Pfam; PF09588; YqaJ; 1. DR SUPFAM; SSF52980; SSF52980; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 281 Uncharacterized protein MG373 homolog. FT /FTId=PRO_0000210575. SQ SEQUENCE 281 AA; 32569 MW; FC70957510D7BEF3 CRC64; MGFTKQYKID FDIIDNQIVL SNNYFQKHKG SFRKITGTRF GKVIGISEYE TSLKTWANMV KIYEDEFDET LSRAGQVIEP KIRDYVIAKT GFNFHSYDPK EVKWDLFPEN PVFGGIPDGE PVDVYGKLAY DTNAPMLEIK TTSCDSLVYK KINGNLKIVF DENGMPIVKK INGKKDSWFD SNGKIVISPA YYCQIGLYLY LRNITKGMFA IAFLEPQDYV HPEWFEAKQR DIRLVPVQID RKAFEVLTNK AQLWYNSFIR TGKSPQLTSQ DWEWLRENGI A // ID Y552_MYCPN Reviewed; 269 AA. AC P75226; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MG374 homolog; GN OrderedLocusNames=MPN_552; ORFNames=G12_orf269, MP290; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95938.1; -; Genomic_DNA. DR PIR; S73616; S73616. DR RefSeq; NP_110241.1; NC_000912.1. DR RefSeq; WP_010874909.1; NC_000912.1. DR ProteinModelPortal; P75226; -. DR EnsemblBacteria; AAB95938; AAB95938; MPN_552. DR GeneID; 877338; -. DR KEGG; mpn:MPN552; -. DR PATRIC; 20022581; VBIMycPne110_0614. DR OMA; KEWINSS; -. DR OrthoDB; EOG67X1T2; -. DR BioCyc; MPNE272634:GJ6Z-597-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR023214; HAD-like_dom. DR SUPFAM; SSF56784; SSF56784; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 269 Uncharacterized protein MG374 homolog. FT /FTId=PRO_0000210577. FT NP_BIND 103 110 ATP. {ECO:0000255}. SQ SEQUENCE 269 AA; 30913 MW; 1F891DA23B1810AB CRC64; MDRKIVALDI NPANFFDAAN DLAIWKDFFN KAQEKHQLVF ISSCWQQTIV YLLDLLSLNN VDVIAESGAI TWFCKTNQYD YQAFLDLASI NVIIHHAVIT NSGIFTMGKS RVDDTANLSA NYFISLQKYK DFKSLWLTDF EQTLKYENFL KQLGKLELSS IYVFSPQYHM DLAFIDQIAS GQPRFTHSNF YPNNLLFTSN KVTKFNALEK YTKTQGLMLK DVHYINLDET LVQNSEQLAS AVFIKKQNNE GLTVQDIPDV LQKLCAQLL // ID Y584_MYCPN Reviewed; 135 AA. AC P75196; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 70. DE RecName: Full=Uncharacterized protein MPN_584; GN OrderedLocusNames=MPN_584; ORFNames=D02_orf135L, MP258; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95906.1; -; Genomic_DNA. DR PIR; S73584; S73584. DR RefSeq; NP_110273.1; NC_000912.1. DR RefSeq; WP_010874941.1; NC_000912.1. DR EnsemblBacteria; AAB95906; AAB95906; MPN_584. DR GeneID; 876822; -. DR KEGG; mpn:MPN584; -. DR PATRIC; 20022649; VBIMycPne110_0647. DR BioCyc; MPNE272634:GJ6Z-630-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF00949; Peptidase_S7; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 135 Uncharacterized protein MPN_584. FT /FTId=PRO_0000210733. SQ SEQUENCE 135 AA; 15588 MW; EABA2A014BD118B1 CRC64; MNYDLSQKFK VYLEFSGKKY RIYGQSIGIS HLDLGGGSSG SLLLNDKKQI AGIYFGVDGA NNELGLAQLL RWKPETYHND EARSVAYDLI FGNKNTTKYY AQFVKEHKTH LYEQIKQINN DEFRFVEKTK RHNLG // ID Y585_MYCPN Reviewed; 302 AA. AC P75195; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 82. DE RecName: Full=Uncharacterized lipoprotein MPN_585; DE Flags: Precursor; GN OrderedLocusNames=MPN_585; ORFNames=D02_orf302, MP257; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95905.1; -; Genomic_DNA. DR PIR; S73583; S73583. DR RefSeq; NP_110274.1; NC_000912.1. DR RefSeq; WP_010874942.1; NC_000912.1. DR EnsemblBacteria; AAB95905; AAB95905; MPN_585. DR GeneID; 877317; -. DR KEGG; mpn:MPN585; -. DR PATRIC; 20022651; VBIMycPne110_0648. DR OrthoDB; EOG6PGK11; -. DR BioCyc; MPNE272634:GJ6Z-631-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 302 Uncharacterized lipoprotein MPN_585. FT /FTId=PRO_0000018741. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 302 AA; 35102 MW; 0D2B90B2DC7FC78A CRC64; MLVVFKRLGF IVSIFSLTFL SACAAFDKWQ EFYINNIPSS TEIHRFNYDL NFSLTFTNRI TSNGEAKFSV TYGTGWLIDW KEPDKKKEND PFRAYLATNL HVAASLINPQ DYEPYKNKDD AGWTTTFRLG KYTKVSDFVS PNQFGLPNAA QALVNVQTSV IPKTAFAARD FVDYSFPQEQ KDKEKRKQQW VKNSHTKNSD VQPFAEFAIL EIPLFSKSKV DRKIFNHFIQ PAIRTYKQLG DSLNIFANPT LDQLKQNRYY VLGYPFLKNK VSSLFLNQTG KKKGIFRRKY TNIPWKTSYY LN // ID Y594_MYCPN Reviewed; 122 AA. AC P75191; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MPN_594; GN OrderedLocusNames=MPN_594; ORFNames=D02_orf122A, MP248; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95896.1; -; Genomic_DNA. DR PIR; S73574; S73574. DR RefSeq; NP_110283.1; NC_000912.1. DR RefSeq; WP_010874951.1; NC_000912.1. DR EnsemblBacteria; AAB95896; AAB95896; MPN_594. DR GeneID; 877092; -. DR KEGG; mpn:MPN594; -. DR PATRIC; 20022669; VBIMycPne110_0657. DR OMA; CNSIIFL; -. DR BioCyc; MPNE272634:GJ6Z-640-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 122 Uncharacterized protein MPN_594. FT /FTId=PRO_0000210698. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. SQ SEQUENCE 122 AA; 13439 MW; 07E7EFD95EA37AA7 CRC64; MNFSRRSLRV GAIVNVSVRS LLMRGKNRNK CNSIIFLTVG LLLFIAALAL GVLVLFNGYQ VNVNANGVDL KPFEIVHFPF AVKTFLSVLT FVLAAFGFVC MVASFLYFVS FKKLKPKANS AS // ID Y649_MYCPN Reviewed; 136 AA. AC P75148; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 59. DE RecName: Full=Uncharacterized protein MPN_649; GN OrderedLocusNames=MPN_649; ORFNames=E09_orf136L, MP193; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95841.1; -; Genomic_DNA. DR PIR; S73519; S73519. DR RefSeq; NP_110338.1; NC_000912.1. DR RefSeq; WP_010875006.1; NC_000912.1. DR IntAct; P75148; 1. DR EnsemblBacteria; AAB95841; AAB95841; MPN_649. DR GeneID; 877024; -. DR KEGG; mpn:MPN649; -. DR PATRIC; 20022779; VBIMycPne110_0712. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-695-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 136 Uncharacterized protein MPN_649. FT /FTId=PRO_0000210703. SQ SEQUENCE 136 AA; 15972 MW; FF6D797ACD5A8948 CRC64; MKISLSTSLF SIEQKVEYFN LNYQSLSDFS VVAKLNYTFT WYGNDFSIGF APKKGEKLYF DLFFTFKASP NHPFAAENFK PDSEAIDFYV SFSWRLEGKD EVSKKLFELS VFGRARAFQI DDYKINLFSY LVYVIR // ID Y654_MYCPN Reviewed; 127 AA. AC P75137; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-MAY-2016, entry version 84. DE RecName: Full=Uncharacterized lipoprotein MPN_654; DE Flags: Precursor; GN OrderedLocusNames=MPN_654; ORFNames=E09_orf129, MP188; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95836.1; 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; U00089; AAB95836.1; ALT_INIT; Genomic_DNA. DR PIR; S73514; S73514. DR RefSeq; NP_110343.1; NC_000912.1. DR EnsemblBacteria; AAB95836; AAB95836; MPN_654. DR GeneID; 876997; -. DR KEGG; mpn:MPN654; -. DR PATRIC; 20022793; VBIMycPne110_0719. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-700-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 127 Uncharacterized lipoprotein MPN_654. FT /FTId=PRO_0000014064. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 127 AA; 14433 MW; 5EC770D804B5E381 CRC64; MRKKKLLSRI SFGSLFLLCG TILSACTWIQ ANLRNLLKET TGKDFDLSKA IKIPEGRQNL INSLKKSYEV NPKDTTKLLL DAWKQSSEEG KLGIADLDFD QVTNPTEKDP FKNGAKGRAF RHWISKY // ID Y683_MYCPN Reviewed; 339 AA. AC P75110; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Putative ABC transporter ATP-binding protein MG467 homolog; GN OrderedLocusNames=MPN_683; ORFNames=K05_orf339, MP159; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95807.1; -; Genomic_DNA. DR PIR; S73485; S73485. DR RefSeq; NP_110372.1; NC_000912.1. DR RefSeq; WP_010875040.1; NC_000912.1. DR ProteinModelPortal; P75110; -. DR IntAct; P75110; 2. DR EnsemblBacteria; AAB95807; AAB95807; MPN_683. DR GeneID; 877035; -. DR KEGG; mpn:MPN683; -. DR PATRIC; 20022855; VBIMycPne110_0750. DR OMA; QAINKEY; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-729-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 339 Putative ABC transporter ATP-binding FT protein MG467 homolog. FT /FTId=PRO_0000093250. FT DOMAIN 112 338 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 150 157 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 339 AA; 38138 MW; D4C0D8F08294E6AB CRC64; MKDTEKKTEK ELVWDECVDI LENVKANSFK ATLEYYLASD KKTKKAKPAK VKKVKEPKAK AVKPEQVKPT KTTKAPKPKK PKKQGGLISQ WKEKLEAPYR TPYVEQKQGM VISIDKMWKH VHGEDSKEQI AILSDVSLEI GYGEIVIILG PSGSGKTTLL NLIGGYDSIS LGSCVVANCP LEKCTTEQLL TYRKLNLGYV YQRYNLIELL SAYDNIAISQ NLIPKEQRHL DIEELAAKLD IKEILYKFPY EMSGGQKQRV AIARAIIKEP RLLLCDEPTG ALDSNSAENI IALLQAINKE YKQTILMVTH DETLTRIANR IIKISDGKIV SNELVRPLS // ID Y150_MYCPN Reviewed; 224 AA. AC P75036; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Putative MgpC-like protein MPN_150; GN OrderedLocusNames=MPN_150; ORFNames=E07_orf224, MP004; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95652.1; -; Genomic_DNA. DR PIR; S73330; S73330. DR RefSeq; NP_109838.1; NC_000912.1. DR RefSeq; WP_010874507.1; NC_000912.1. DR EnsemblBacteria; AAB95652; AAB95652; MPN_150. DR GeneID; 877302; -. DR KEGG; mpn:MPN150; -. DR PATRIC; 20021619; VBIMycPne110_0166. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-157-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 224 Putative MgpC-like protein MPN_150. FT /FTId=PRO_0000210721. SQ SEQUENCE 224 AA; 24316 MW; 70678873B12D25ED CRC64; MGSNAVPSLW YWVVDERTTS GRGTWWAHTE LNWGTDKQKE FVENQLGFNE TSATDSHNFK KALLHQPAYL ISGLDVVADH LVFAAFRAGA VGYDMTTDTN ASTYNQALTW STTAGLDSAG GYKALVENTA GLNGPINGLF TLLDTFAYVT PVSGMKGGSK NTEAVQTTYP VKSDQKASAK IASLINASPL NSYGDKKSHP PKVKGRQLQN IFDDWKLTKA VSLM // ID Y152_MYCPN Reviewed; 794 AA. AC P75034; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MPN_152; DE Flags: Precursor; GN OrderedLocusNames=MPN_152; ORFNames=E07_orf794, MP002; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB95650.1; -; Genomic_DNA. DR PIR; S73328; S73328. DR RefSeq; NP_109840.1; NC_000912.1. DR RefSeq; WP_010874509.1; NC_000912.1. DR PRIDE; P75034; -. DR EnsemblBacteria; AAB95650; AAB95650; MPN_152. DR GeneID; 877318; -. DR KEGG; mpn:MPN152; -. DR PATRIC; 20021625; VBIMycPne110_0169. DR OMA; ETTIYLY; -. DR BioCyc; MPNE272634:GJ6Z-159-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 794 Uncharacterized lipoprotein MPN_152. FT /FTId=PRO_0000018726. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 794 AA; 86871 MW; 0DA72D12807F53EE CRC64; MKFKYGAIVF SGLLGVSAIL AACGARGKFN QVDDGKIKLA SSLTSRSAST ALQKVVEKYN KVKGVNDYPI EITQIAGGYD GGRTDLQTRV NVKDTTNFYN LILNYPDLVS TLGRVGMELP FDKVKTDKLA DRFLDFNNRI SAISKKGIYG IPVSLSTEVL SINGPVLHYI LNSAQGKVSS VTSVQRTADS GSGTTNNNGV TKPLKIDKEN ESTKKLWEEI ENKAKENGKK TSSSRRKRNL SSSKQMSTQT QPTDNSNDAN QSDQAIEKTW GKYQEVEGGL KDYTFKASVF ENWHDLLDFS NRVAKSFSNI NTNTNKKGTD IQGVLGIDST PNSLFTSVFA AGGGNYDNFF YKVANGRADF SNFKNKGTSY QNLQKVYGDY KGLIDSNGLF VNKGGSYSSN FQKFHQLAYS ISSTSGFFYS FAGENSKRLK FDGGNFIEFP GFTQAIYAPE NNSQSGGESG DQTTNNEANL LGTFKIKSSN KSKSSSSKSS TKAETGKTSG GDQNQGKKGE GAQNQGKKGE GAQNQGKNGG VETTIYLYKN SIPSGKNKGE NAILIDNKTI VEQLESAAKK EDKKSGESTT EQTQIQSKSV TEQKQPKIIG YTTTGNVHED NKHIFPIDKL TSDRNFDRKI IVGATEETLD KSNTLQSNEA IVLPAPSKYK STDTNKVTIT QGPNIIGIHV NEKENAETQK FVDWFLNSPQ TWEGKGKGKE QTNKTAAEFF AESASYILPL KEIFEQKNEK KEGSDQKDSK SNGRGKQTNL YTEKALELFR GISTDQIVSY SDQVTLGVVV SVME // ID Y162_MYCPN Reviewed; 320 AA. AC P75583; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized lipoprotein MG149 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_162; ORFNames=MP669, VXpSPT7_orf320; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96317.1; -; Genomic_DNA. DR PIR; S73995; S73995. DR RefSeq; NP_109850.1; NC_000912.1. DR RefSeq; WP_010874519.1; NC_000912.1. DR EnsemblBacteria; AAB96317; AAB96317; MPN_162. DR GeneID; 877172; -. DR KEGG; mpn:MPN162; -. DR PATRIC; 20021647; VBIMycPne110_0180. DR OMA; NGETHEH; -. DR OrthoDB; EOG60KNCV; -. DR BioCyc; MPNE272634:GJ6Z-169-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 320 Uncharacterized lipoprotein MG149 FT homolog. FT /FTId=PRO_0000014029. FT LIPID 24 24 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 24 24 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 320 AA; 36096 MW; 705ED260604CD564 CRC64; MKLNLRFPSY FLPVVAASAF LVSCATPNTY EVQRAALIQL VEEDERQNYI QKGSMGANAV MTAAKAETKT AEKTATSTKA ASIELKKTDT DIKTTTTTEN KSASGYKLDT LFGDYILWVV DHLSGLLFSP KTNNSTTTQK IQLITEDKMI LDGGNLTVEK NHEHGHTHKN GETHEHDHDH HEGEEEVIVG RALSFANGLF LVVDLKEEKH EEKKEAKSEM SMNSKDMVMM TKTEMMSKEM KSEQKMEKKE EHEHPHKKLS LSTTAYKFGQ SFNILEFTGA MHHKTAHNNE TEFKNLGKKY GGMTEYTIVD FDFNPPKPTK // ID Y200_MYCPN Reviewed; 798 AA. AC Q50288; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MPN_200; DE Flags: Precursor; GN OrderedLocusNames=MPN_200; ORFNames=GT9_orf798, MP631; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U34795; AAC43681.1; -; Genomic_DNA. DR EMBL; U00089; AAB96279.1; -; Genomic_DNA. DR PIR; S62791; S62791. DR RefSeq; NP_109888.1; NC_000912.1. DR RefSeq; WP_010874557.1; NC_000912.1. DR ProteinModelPortal; Q50288; -. DR IntAct; Q50288; 1. DR EnsemblBacteria; AAB96279; AAB96279; MPN_200. DR GeneID; 877064; -. DR KEGG; mpn:MPN200; -. DR PATRIC; 20021725; VBIMycPne110_0219. DR OrthoDB; EOG6SR92H; -. DR BioCyc; MPNE272634:GJ6Z-207-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 798 Uncharacterized lipoprotein MPN_200. FT /FTId=PRO_0000018728. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 798 AA; 87629 MW; 3E2471D7EF0A3CA0 CRC64; MKFKYGAIVF SGLLGVSAIL AACGTRGKFD QIDDGKIKLA SSLTSKGAAN ALQAIVKKYN EVKKPGDYPI EITQIAGGYD QARVDLQSRV GVKDKTNFYN LILNYPDVVS VLARNQMELP FDGVDVSKIS PNFLNFNERI SGVSKKANYA IPVSVSTDIL VLNGPVLHYI LNSAKGESKG AQKDNKSAEV QRKSTGQKTV TQPLTIATDS ATNGLWKKIE DAAKVNGKKK EEKKSTRSKR ATEGTQTTKE NTGGDAATSD TKIKESWGAY QEVEGGLKGY QFKAIVFENW HDLIDFSTRV AKSFSKVKDN SNKKGNEIQG VLGVDNSPNA LLSSVFAAGN SDYNNFFYKV QNGRADFSNF NNKGSSYKNL KNVFNDYKNL IAQNGLYVNK GGSYSSNFQK FHQLAYSISS TSGFAYSFAG QNSKRFKFTD DGTFVEYPSY TTEVNAPESN NGNDGKQQGQ SDQGNLLGTF EVVDKSTSDI KVKPKTQAES KKSSDSKQTA NTGKGSNSKQ QTPKKTISLY KTKIPQDKTE NVDAFLVTDS ELISKLEKAK NKKEETKASG KSASARVAVQ ATQKKQSNEK QIVGYTTTSA LSEDGKHIFK LGKLNSENYE RKIIVGATVE TLEQSTTLQS EEAIVLAAPG KYKDSDQKRV MITQGPNLIG VHANTKENEE TKKFVNWFLN KTESWEVKGN GKDSQTTKSL TPAQYFAESA SYILPLKETV EKDHKEQTNK NTYVAKALEM LKEVSENKSV SYSDPSDFRS GRFRDALGAN FNATINSKAN FEKFFQGFKA ALGSDFDK // ID Y203_MYCPN Reviewed; 127 AA. AC Q50284; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUN-2015, entry version 54. DE RecName: Full=Putative adhesin P1-like protein MPN_203; GN OrderedLocusNames=MPN_203; ORFNames=GT9_orf127, MP628; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U34795; AAC43677.1; -; Genomic_DNA. DR EMBL; U00089; AAB96276.1; -; Genomic_DNA. DR PIR; S62806; S62806. DR IntAct; Q50284; 1. DR EnsemblBacteria; AAB96276; AAB96276; MPN_203. DR PATRIC; 20021731; VBIMycPne110_0222. DR BioCyc; MPNE272634:GJ6Z-210-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 127 Putative adhesin P1-like protein MPN_203. FT /FTId=PRO_0000210711. SQ SEQUENCE 127 AA; 14350 MW; 536412838B129016 CRC64; MLWPFRWVWW KRVLTSQTRA PAKPNPLTVP PTCTWWSLRK LPNPTKLDDD LKNLLDPNEV RARMLKSFGT ENFTQPQPQP QALKTTTPVF GTSSGNLGSV LSGGGYHAGL KHHQSTVTRS TGEWVDR // ID Y213_MYCPN Reviewed; 1030 AA. AC P75556; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG075 homolog; GN OrderedLocusNames=MPN_213; ORFNames=G07_orf1030, MP618; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96266.1; -; Genomic_DNA. DR PIR; S73944; S73944. DR RefSeq; NP_109901.1; NC_000912.1. DR RefSeq; WP_010874570.1; NC_000912.1. DR EnsemblBacteria; AAB96266; AAB96266; MPN_213. DR GeneID; 877142; -. DR KEGG; mpn:MPN213; -. DR PATRIC; 20021751; VBIMycPne110_0232. DR OMA; VSINLAY; -. DR OrthoDB; EOG68H83X; -. DR BioCyc; MPNE272634:GJ6Z-220-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 1030 Uncharacterized protein MG075 homolog. FT /FTId=PRO_0000210412. FT TRANSMEM 7 29 Helical. {ECO:0000255}. SQ SEQUENCE 1030 AA; 116018 MW; DA4E48D35973E07C CRC64; MKLSAIISLS VAGTVGTTAV VVPTTITLVN KTHQVEHESE QSDFQDIRFG LNSVKLPKAQ PAAATRITVE NGTDKLVNYK SSPQQLFLAK NALKDKLQGE FDKFLSDAKA FPALTADLQE WVDQQLFNPN QSFFDLSAPR SNFTLSSDKK ASLDFIFRFT NFTESVQLLK LPEGVSVVVD SKQSFDYYVN ASAQKLLVLP LSLPDYTLGL NYMFDHITLN GKVVNKFSFN PFKTNLNLAF SNVYNGVDVF EAQKNLVGKG KYLNTHVKAE DVKKDVNANI KNQFDIAKII AELMGKALKE FGNQQEGQPL SFLKVMDKVK EDFEKLFNLV RPGLGKFVKD LIQSSSQAEN KITVYKLIFD NKKTILNLLK ELSIPELNSS LGLVDVLFDG ITDSDGLYER LQSFKDLIVP AVKTNEKTAA LSPLIEELLT QKDTYVFDLI QKHKGILTNL LKNFLADFQK STPFMADQVA IFTELFDNEG AFDLFGEADF VDKIAELFLT KRTVKNGEKI ETKDSLLVTS LKSLLGEKVA ALGDLLDSYI FKNELLNRSV EVAKAEAKDT KGATDYKKEQ AKALKKLFKH IGENTLSKTN LDKITLKEVK NTENVELEET ETTLKVKKLD VEYKVELGNF EIKNGLIKAM LEFLPDTKDL ETTLDKLLFK GESYKAMKDK YIKEGFPGYG WAKGVVPGAF ESIENTFKSA IDKTKSIRDL FGDMLFGNDL SSVKETDSFI TLGGSFDIKY GGENLNVLPA YYSLINSEIG YQIIGVDTTI DATKVKVELK NKEYKGKSPA INGQVKLSQS FFNVWTNMFD SITKQIFQKK YEFKDNIQVF ARNEDNTSRL ELDISDPEQR VIPFAFVDGF GIQLKAVDKN ITKEAGNTEP KSPVIQLYEA LNKEKDQKQQ SKQSPKQLDT KTQLGYLLKL GDNWSKDDYK SLIDDTIINN NYLEASFNSK ITVDRLGIPI DLWLFKIWPK FNLEIPMQGS LQLYSSSVIF PYGIYDTSVQ DAAKIVKRLN FTDMGFKLND PKPNFWFVGF // ID Y239_MYCPN Reviewed; 222 AA. AC P75532; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MG101 homolog; GN OrderedLocusNames=MPN_239; ORFNames=K04_orf222, MP592; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 HTH gntR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00307}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96240.1; -; Genomic_DNA. DR PIR; S73918; S73918. DR RefSeq; NP_109927.1; NC_000912.1. DR RefSeq; WP_010874596.1; NC_000912.1. DR ProteinModelPortal; P75532; -. DR IntAct; P75532; 1. DR EnsemblBacteria; AAB96240; AAB96240; MPN_239. DR GeneID; 877219; -. DR KEGG; mpn:MPN239; -. DR PATRIC; 20021803; VBIMycPne110_0258. DR OMA; WPANTRI; -. DR OrthoDB; EOG6C2WGS; -. DR BioCyc; MPNE272634:GJ6Z-246-MONOMER; -. DR Proteomes; UP000000808; 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; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 222 Uncharacterized HTH-type transcriptional FT regulator MG101 homolog. FT /FTId=PRO_0000050694. FT DOMAIN 8 77 HTH gntR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00307}. SQ SEQUENCE 222 AA; 25850 MW; 7135C171B776D2D7 CRC64; MISAKEQAKK GQIIYRYILL KIQSFKWPAG TRIFSERQLE IRFASSRSLI RTILNTLLGK DLIRHTKGNA GYFVAKNAGF SFFHKTQDNK LPKWAKLSTL MKNHLREVDR DVFSSIDSGV DFGNFKGLEA KLFDENKKNF LNLSFFGKDD VLQIFSEQNL QEQFFKDFAY NGIVVERKSS LICVDDETKN LLIYDLFYDD NNKFIVAMRS EYLNPRIKII NA // ID Y256_MYCPN Reviewed; 223 AA. AC P75518; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MG117 homolog; GN OrderedLocusNames=MPN_256; ORFNames=A65_orf223, MP577; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96225.1; -; Genomic_DNA. DR PIR; S73903; S73903. DR RefSeq; NP_109944.1; NC_000912.1. DR RefSeq; WP_010874613.1; NC_000912.1. DR EnsemblBacteria; AAB96225; AAB96225; MPN_256. DR GeneID; 876905; -. DR KEGG; mpn:MPN256; -. DR PATRIC; 20021837; VBIMycPne110_0275. DR OMA; DQITKNF; -. DR OrthoDB; EOG690MPQ; -. DR BioCyc; MPNE272634:GJ6Z-263-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 223 Uncharacterized protein MG117 homolog. FT /FTId=PRO_0000210422. SQ SEQUENCE 223 AA; 25739 MW; 4298D20E06165CAF CRC64; MDRKIVQLIH NFSGTEKLKA AVFSHDEQCF FDFVSFDELN SKLTGFLLFD SLEKLFKLVE TIQQKRSWLY VDELWLINTA TENQQLNEVS VWLVKKELAQ VGVLTQLDTS LVKLLMASKN TDSALYNTYI KPVELQQFTQ TPAPDNVNAE QSHLTLESTT DLNNSQLANT PALWEVEQTT QELLPTMDFS KFIDELDQIT KNFSDLELEP LSFNEGFDEW NQE // ID Y264_MYCPN Reviewed; 281 AA. AC P75511; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative phosphatase MPN_264; DE EC=3.1.3.-; GN OrderedLocusNames=MPN_264; ORFNames=A65_orf281, MP569; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- INTERACTION: CC P75508:ppnK; NbExp=1; IntAct=EBI-2260121, EBI-2260114; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; U00089; AAB96217.1; -; Genomic_DNA. DR PIR; S73895; S73895. DR RefSeq; NP_109952.1; NC_000912.1. DR RefSeq; WP_010874621.1; NC_000912.1. DR IntAct; P75511; 3. DR EnsemblBacteria; AAB96217; AAB96217; MPN_264. DR GeneID; 876923; -. DR KEGG; mpn:MPN264; -. DR PATRIC; 20021853; VBIMycPne110_0283. DR KO; K07024; -. DR OMA; HLIEITH; -. DR OrthoDB; EOG6B09T7; -. DR BioCyc; MPNE272634:GJ6Z-271-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 281 Putative phosphatase MPN_264. FT /FTId=PRO_0000054436. FT REGION 44 45 Phosphate binding. {ECO:0000250}. FT ACT_SITE 8 8 Nucleophile. {ECO:0000250}. FT METAL 8 8 Magnesium. {ECO:0000250}. FT METAL 10 10 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 228 228 Magnesium. {ECO:0000250}. FT METAL 229 229 Magnesium. {ECO:0000250}. FT BINDING 9 9 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 205 205 Phosphate. {ECO:0000250}. FT BINDING 231 231 Phosphate. {ECO:0000250}. SQ SEQUENCE 281 AA; 32614 MW; BF44564E7C7FBF11 CRC64; MIDLLGLDLD GTLLSRTRQI NDPTKQALAN LIQKKPSLKV MILTGRSLFS TLKYVQELNE LCKKPLVEYF CCYGGAKLYQ LNNNQPQEQY KFLIDSRQVK TVFEIVEQHK GLFLAYLDKP KAPYIILGAN QFYAWLIKQF WYKQRCEYFK NDHLTDGILK INVYFACPLR LKKVYQIIKR QFQDTLNVVN FSKHLIEITH KDGNKGYAIE AIAKKQGLSL KRMAVIGDSL NDRSMFEKVQ YSFAMSKSPD ELKLLATEIG TKTNRFRFSS LVDLITEKII N // ID Y268_MYCPN Reviewed; 117 AA. AC P75507; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Putative phosphotransferase enzyme IIB component MPN_268; DE EC=2.7.1.-; DE AltName: Full=Putative PTS system EIIB component; GN OrderedLocusNames=MPN_268; ORFNames=A65_orf117, MP565; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitant with their translocation across the cell CC membrane. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L- CC histidine/cysteine + sugar = protein EIIB + sugar phosphate. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96213.1; -; Genomic_DNA. DR PIR; S73891; S73891. DR RefSeq; NP_109956.1; NC_000912.1. DR RefSeq; WP_010874625.1; NC_000912.1. DR ProteinModelPortal; P75507; -. DR IntAct; P75507; 2. DR EnsemblBacteria; AAB96213; AAB96213; MPN_268. DR GeneID; 876825; -. DR KEGG; mpn:MPN268; -. DR PATRIC; 20021861; VBIMycPne110_0287. DR OMA; WIVKKSK; -. DR OrthoDB; EOG6FFS9V; -. DR BioCyc; MPNE272634:GJ6Z-275-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1360.60; -; 1. DR InterPro; IPR001996; PTS_IIB_1. DR SUPFAM; SSF55604; SSF55604; 1. DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Phosphoprotein; KW Phosphotransferase system; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 117 Putative phosphotransferase enzyme IIB FT component MPN_268. FT /FTId=PRO_0000210430. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT DOMAIN 42 117 PTS EIIB type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. SQ SEQUENCE 117 AA; 13281 MW; 1C4D912E2718E3DA CRC64; MKVLLWIGYV LSFGLLYLYL VKRAKRAALQ LNNKLVESHT IPFAVRDFIA ACGGRTNFVS LRTSPTQLIV SFAKPELVQI AALQKLGIKG INKSQNQYRF VLGNFVNQLK QQIENER // ID Y270_MYCPN Reviewed; 95 AA. AC Q9EXD1; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MG131 homolog; GN OrderedLocusNames=MPN_270; ORFNames=MP563.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34756.1; -; Genomic_DNA. DR RefSeq; NP_109958.1; NC_000912.1. DR RefSeq; WP_010874627.1; NC_000912.1. DR EnsemblBacteria; AAG34756; AAG34756; MPN_270. DR GeneID; 876907; -. DR KEGG; mpn:MPN270; -. DR PATRIC; 20021865; VBIMycPne110_0289. DR OMA; QYSALIP; -. DR BioCyc; MPNE272634:GJ6Z-277-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 95 Uncharacterized protein MG131 homolog. FT /FTId=PRO_0000210433. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 35 55 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 95 AA; 11066 MW; 56BB869892275C64 CRC64; MQYTVLIPLF IFIGAMVLFG FSFQKKQPQR RIVQILFLAY CVDFLALIIA VMMLTFLSYD DLMLGVLIPV LILSIIMFFV MIIAHYPLMK RLFGH // ID Y318_MYCPN Reviewed; 491 AA. AC P75463; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein MG225 homolog; GN OrderedLocusNames=MPN_318; ORFNames=F10_orf491, MP518; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG226. {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; U00089; AAB96166.1; -; Genomic_DNA. DR PIR; S73844; S73844. DR RefSeq; NP_110006.1; NC_000912.1. DR RefSeq; WP_010874674.1; NC_000912.1. DR ProteinModelPortal; P75463; -. DR EnsemblBacteria; AAB96166; AAB96166; MPN_318. DR GeneID; 876939; -. DR KEGG; mpn:MPN318; -. DR PATRIC; 20021988; VBIMycPne110_0341. DR OMA; VFITFFY; -. DR OrthoDB; EOG6F55D5; -. DR BioCyc; MPNE272634:GJ6Z-335-MONOMER; -. DR Proteomes; UP000000808; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR PANTHER; PTHR11785; PTHR11785; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 491 Uncharacterized protein MG225 homolog. FT /FTId=PRO_0000210468. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 127 147 Helical. {ECO:0000255}. FT TRANSMEM 161 181 Helical. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 347 367 Helical. {ECO:0000255}. FT TRANSMEM 380 400 Helical. {ECO:0000255}. FT TRANSMEM 422 442 Helical. {ECO:0000255}. FT TRANSMEM 452 472 Helical. {ECO:0000255}. SQ SEQUENCE 491 AA; 54925 MW; 7F2CEC9DEA6DBCFB CRC64; MAVASKKFTE RQFLFFVVNY IAGFGFISTA LSLFELGPLS WVIFFLVSLI SLIVTLAFAR VSAIDKNNYG GAYLWAKKAF NSERYSHRLF IFFTGWNNFI ASPLYAAIAP LFILSAFKGI DGIQGNAANT WILIAAGFTF YLLLAFLSTK GTSLNKKLIA VFASIKWAVL LSTLIVALIV IGKNGNGYAI NNDIKQGPFK EREITLGAVA TVFITFFYSY SGAEDISTMT PDVKTTNFRK ILIISFIAVF LFYFVGILIF NGLLNVSQSD DDKGKDGRIA SVADIFRLAG GLGALIFYGV GALFNNVSTR LSTIIANSRK ILPLAQDNYL PTTFSKANSK GEFQNAIWFT FGTTIITMTV LFFVPLITSN FDFDKSTEYA SSIGSAATLV QYILVFFIIF RLIYKKEQLY QKNWTRELEQ ILFGIGVFII LLMLLFYLFP VIDGKTKWQL KNTLTLVVYG VLILIGFALF MTQEYKRNKQ KESYVTPRAV T // ID Y338_MYCPN Reviewed; 632 AA. AC P75440; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG242 homolog; GN OrderedLocusNames=MPN_338; ORFNames=F10_orf632o, MP498; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96146.1; -; Genomic_DNA. DR PIR; S73824; S73824. DR RefSeq; NP_110026.1; NC_000912.1. DR RefSeq; WP_010874694.1; NC_000912.1. DR EnsemblBacteria; AAB96146; AAB96146; MPN_338. DR GeneID; 876771; -. DR KEGG; mpn:MPN338; -. DR PATRIC; 20022030; VBIMycPne110_0362. DR OMA; WIINDIE; -. DR OrthoDB; EOG6K13P2; -. DR BioCyc; MPNE272634:GJ6Z-355-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 632 Uncharacterized protein MG242 homolog. FT /FTId=PRO_0000210482. FT TRANSMEM 255 275 Helical. {ECO:0000255}. FT TRANSMEM 506 526 Helical. {ECO:0000255}. FT TRANSMEM 566 586 Helical. {ECO:0000255}. FT TRANSMEM 603 623 Helical. {ECO:0000255}. SQ SEQUENCE 632 AA; 74335 MW; 344D6771FCDA44A6 CRC64; MEFNKLQLSH CISFYISDVS EVFFESINQH PSRDFVNNIL QKIKSTLSEE ELEKLNTIEE VTKDEKILIM LNHVLKKIVS KTGSSSCDLF QIVKHDRFNE PVYIQSVNAF ENNLINNEFA ERRYDYLIEI NKHSYLRKYV NAIRISFFLD LRAQILSGSF TLDVINKQLE HQNKEELFQA IYLRSLIKHF ISNQLYPISL NSFIFGDKNR ENKTVENDKL SVLKNNWNQI FFSKYFDFVA KNKEERVVDN NCDELFYATM NTLLIMLIII EELRVYFNSK EPALILKLLD NKVSLREDPD QNPETDLHEL IKFAEKNYLE KEKTSRWHKK RVKSLEELLE EIKQINLETK NESLAYPDEI VELELDNVHN FVSTKQVFRH QLDLQTLHGI VINPERYGIG MWSNHFVDWE EFKDLIEQIT DAENGSDLYG FEKDLDESIC QVNKKYLTFI SSDSSSFLII KNDQTKVISN YVWAQLYFET RRWIINDIEY DLYEKGFDKS HFASNIALLE SLNFNWLDPF YGLTSIKEIM QKIDSKSNLK TSIAEMVAKF KHEQRISKKD NERVLMIFAY VAAAVVGFIN FFSMVFTILT VSDLNAGLTP ANIVVIAIAS LLALFLIVIA VLFRFRWKYI KH // ID Y351_MYCPN Reviewed; 213 AA. AC P75427; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Putative tRNA (adenine-N(1)-)-methyltransferase MPN_351; DE EC=2.1.1.-; GN OrderedLocusNames=MPN_351; ORFNames=H91_orf213, MP485; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(1)-methyladenine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TrmK 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; U00089; AAB96133.1; -; Genomic_DNA. DR PIR; S73811; S73811. DR RefSeq; NP_110039.1; NC_000912.1. DR RefSeq; WP_010874707.1; NC_000912.1. DR ProteinModelPortal; P75427; -. DR EnsemblBacteria; AAB96133; AAB96133; MPN_351. DR GeneID; 876927; -. DR KEGG; mpn:MPN351; -. DR PATRIC; 20022062; VBIMycPne110_0378. DR KO; K06967; -. DR OMA; WTITTET; -. DR OrthoDB; EOG6716R9; -. DR BioCyc; MPNE272634:GJ6Z-368-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR006901; TrmK. DR Pfam; PF04816; TrmK; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 213 Putative tRNA (adenine-N(1)-)- FT methyltransferase MPN_351. FT /FTId=PRO_0000210488. SQ SEQUENCE 213 AA; 23943 MW; 1CC74F9E710F6A29 CRC64; MKRRISTIAN LVLQQKPKAF YDIGCDHGYL ARELVQQNPS LVGVNSDISA NALGAAKGLL KDHTNMHFIT SDGFDLLPNL NLDPAVGVIA GLGGLKIMQI LAQHNNFLKH FVLQPQSNII ELRRFLSANQ WTITTETLVE ERGFIYLVLA VDKTKAQTQY LTEEQMILGP HLVNFTDKQM LVKYYNGLLK NFTARLNPSQ FDSQVIHVLN KII // ID Y362_MYCPN Reviewed; 453 AA. AC P75419; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MG259 homolog; GN OrderedLocusNames=MPN_362; ORFNames=H91_orf453, MP474; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75561:MPN_108; NbExp=1; IntAct=EBI-2260750, EBI-2261439; CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96122.1; -; Genomic_DNA. DR PIR; S73800; S73800. DR RefSeq; NP_110050.1; NC_000912.1. DR RefSeq; WP_010874718.1; NC_000912.1. DR ProteinModelPortal; P75419; -. DR IntAct; P75419; 1. DR EnsemblBacteria; AAB96122; AAB96122; MPN_362. DR GeneID; 876873; -. DR KEGG; mpn:MPN362; -. DR PATRIC; 20022090; VBIMycPne110_0389. DR OMA; FCTSANI; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; MPNE272634:GJ6Z-382-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF05175; MTS; 1. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR PROSITE; PS00092; N6_MTASE; 1. DR PROSITE; PS51163; YRDC; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 453 Uncharacterized protein MG259 homolog. FT /FTId=PRO_0000202027. FT DOMAIN 276 437 YrdC-like. {ECO:0000255|PROSITE- FT ProRule:PRU00518}. SQ SEQUENCE 453 AA; 51259 MW; DFB05902223B3BAE CRC64; MNLYELFLNQ KLLYGTDPHF NGVFLTLLEK FGLHFKDLTA LWKHAKTITD FDEQGIVNAL KAYFVDQLPL PYITGSVKLG SLTFKTQPGV FIPRADSLAL LKVVKAQNLK TAVDLCCGSG TLAIALKKRF PHLNVYGSDL NPQALQLAAQ NARLNMVEVQ WIEADFLAAL AQVNTPIDLI ITNPPYLNES QLDQTLNHEP RNSLVADGNG ILFYQKLYNF LLGNRQVKQV ILECSPTQKK EFLALFSIFK TSEIYTSHKQ FIGLSIDNTK LPVLKIAQTK QIKALLDKGM TAIIPTDTQI GLMSYCQQDL DHIKQRDPNK HYVQFLAPSQ INQLPKQLQK LAKLFWPGAY TFIVDGQSYR LPNSPQLLKL LKTVGLIYCT SANQAKQKPF GKLSAYQNDP YWVQQNCFIV QNSFKSNNEP SLIYNLDTKQ IVRGSSTQLQ RFQALLAKHK LRH // ID Y366_MYCPN Reviewed; 272 AA. AC P75415; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 54. DE RecName: Full=Putative MgpC-like protein MPN_366; GN OrderedLocusNames=MPN_366; ORFNames=H91_orf272, MP470; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96118.1; -; Genomic_DNA. DR PIR; S73796; S73796. DR IntAct; P75415; 1. DR EnsemblBacteria; AAB96118; AAB96118; MPN_366. DR PATRIC; 20022098; VBIMycPne110_0393. DR BioCyc; MPNE272634:GJ6Z-386-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 272 Putative MgpC-like protein MPN_366. FT /FTId=PRO_0000210722. SQ SEQUENCE 272 AA; 30353 MW; 9A8DA089A2554A9C CRC64; MGGLDVVRAA HLHPSYELVD WKRVGQNKLV ALVRSALVRV KFQDTTSSDS NNQDTSQNAL SFDTQESQKA LNGSQSGSSD TSGSNSQDFA SYILIFQAAP RATWVFERKI KLALPYVKQE SQGSDDQGSN GKGSLYTTLQ DLLVEQPVTP YTPNAGLARV NGVAQDTVHF GSGQESSWNS QRSQKGLKTT PLPMPSPALS SIRAARTGSW MKVDRCMNPW IRPRRGRGRM RALGKIRKKQ RRKMMPRWWG WLEVVRLEVL LVYKAMARTV RG // ID Y385_MYCPN Reviewed; 114 AA. AC P75397; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG267 homolog; GN OrderedLocusNames=MPN_385; ORFNames=F11_orf114, MP452; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96100.1; -; Genomic_DNA. DR PIR; S73778; S73778. DR RefSeq; NP_110073.1; NC_000912.1. DR RefSeq; WP_010874741.1; NC_000912.1. DR EnsemblBacteria; AAB96100; AAB96100; MPN_385. DR GeneID; 877132; -. DR KEGG; mpn:MPN385; -. DR PATRIC; 20022146; VBIMycPne110_0416. DR OMA; FPNINSW; -. DR OrthoDB; EOG69PQCW; -. DR BioCyc; MPNE272634:GJ6Z-406-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 114 Uncharacterized protein MG267 homolog. FT /FTId=PRO_0000210495. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. SQ SEQUENCE 114 AA; 13227 MW; B9F156AE167F8991 CRC64; MLLKRLIKLA IFLFFVAVGF IIFIGSFWLN TYNTKEWANL LAEKDASGLI VQIIPNINQW FKGTVEQQQK LFQTLVHFFI PVGFGLLFGI AVAIIADLFY HLIKYLIKRS FKKN // ID Y431_MYCPN Reviewed; 317 AA. AC P75357; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MG302 homolog; GN OrderedLocusNames=MPN_431; ORFNames=A05_orf317, MP410; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ 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; U00089; AAB96058.1; -; Genomic_DNA. DR PIR; S73736; S73736. DR RefSeq; NP_110119.1; NC_000912.1. DR RefSeq; WP_010874787.1; NC_000912.1. DR EnsemblBacteria; AAB96058; AAB96058; MPN_431. DR GeneID; 876892; -. DR KEGG; mpn:MPN431; -. DR PATRIC; 20022258; VBIMycPne110_0466. DR KO; K16785; -. DR OMA; GRKVYNT; -. DR OrthoDB; EOG66MQPD; -. DR BioCyc; MPNE272634:GJ6Z-460-MONOMER; -. DR Proteomes; UP000000808; 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; IPR003339; ABC/ECF_trnsptr_transmembrane. DR Pfam; PF02361; CbiQ; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 317 Uncharacterized protein MG302 homolog. FT /FTId=PRO_0000210523. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 253 273 Helical. {ECO:0000255}. SQ SEQUENCE 317 AA; 36302 MW; FA9E4F61FD08F056 CRC64; MTSKNFLSQL PPVLKLWWWI ISLVVAFLPL GLHGLIIINA IFFALVIVVE RKLKTFAIIF GWLLFFFWFN IVVNGFIFLP NSSALASQNE NFLGHFIYSG GEQFGGVSWW SVNTRSLLRS LVIALRISML FATSFLLTAS TSIYELAFGV ERLCTPLRYL KIKTQPLSIL FALVFKLLPI VKGELKRIKQ AQAIRGFKYG KLAFLNPVKL KTLFIPVLLS TVKKTEAVAF ALQAKGYQLD NPNKTHYLQK YNLWGGIVFL GLFVLLSCLL MVNNWHLVYW TNPHYSFTFT HQNFCFFKQI SSPQLLAFWQ LELLAIG // ID Y448_MYCPN Reviewed; 285 AA. AC Q50364; P75332; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 3. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MG313 homolog; GN OrderedLocusNames=MPN_448; ORFNames=H08_orf263, MP393; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38997; AAA61696.1; -; Genomic_DNA. DR EMBL; U00089; AAG34746.1; -; Genomic_DNA. DR PIR; S73719; S73719. DR RefSeq; NP_110136.1; NC_000912.1. DR RefSeq; WP_010874804.1; NC_000912.1. DR ProteinModelPortal; Q50364; -. DR EnsemblBacteria; AAG34746; AAG34746; MPN_448. DR GeneID; 877045; -. DR KEGG; mpn:MPN448; -. DR PATRIC; 20022294; VBIMycPne110_0484. DR OMA; LITIPIY; -. DR OrthoDB; EOG6GTZG2; -. DR BioCyc; MPNE272634:GJ6Z-477-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR024529; ECF_trnsprt_substrate-spec. DR Pfam; PF12822; DUF3816; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 285 Uncharacterized protein MG313 homolog. FT /FTId=PRO_0000210527. SQ SEQUENCE 285 AA; 32944 MW; EA1752C555FB0B17 CRC64; MFPYYPLKVT RNLQLLVWAA VLMALSFIFN IFSINVTSVL KVSFTRIPFA LIGWMFGPVW GFTFGAIADT MDWLTRGYTW FWLFAIQKPM FCFLAGLVKG VYQVRQSSTN WKIDFWILQS ILIGFFVLTL VLLLMYLTDG NFQAAGNQSF GRGFDVNVHI LQGITMAAFI SFFVGLEIFL GWKYTKVKKP KEMILNLYIL MMALLMTLVV SLLIGTVASI EYLVFLSGKP SKNFVKYGSY FFLMPRVLVQ ALLMPLYLAL FKPLIRIAEN NLRNYLRVYN LSWKR // ID Y467_MYCPN Reviewed; 101 AA. AC P75316; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 73. DE RecName: Full=Uncharacterized lipoprotein MPN_467; DE Flags: Precursor; GN OrderedLocusNames=MPN_467; ORFNames=MP374, P01_orf101; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB96022.1; -; Genomic_DNA. DR PIR; S73700; S73700. DR EnsemblBacteria; AAB96022; AAB96022; MPN_467. DR PATRIC; 20022352; VBIMycPne110_0503. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-506-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 101 Uncharacterized lipoprotein MPN_467. FT /FTId=PRO_0000014062. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 101 AA; 11349 MW; 4DF66497B155C006 CRC64; MRKKRLLSRI SFSSLFLLCG TLLSACTGIQ ADLRNLIKET TGKDIDLSKA IKTKEGKKNI IASLKKSYEV NPRDTTKLLL DAWKQSFEEG KLGIPDFDLT M // ID Y509_MYCPN Reviewed; 427 AA. AC P75277; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MPN_509; GN OrderedLocusNames=MPN_509; ORFNames=MP333, P02_orf427; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95981.1; -; Genomic_DNA. DR PIR; S73659; S73659. DR IntAct; P75277; 2. DR EnsemblBacteria; AAB95981; AAB95981; MPN_509. DR PATRIC; 20022464; VBIMycPne110_0559. DR OMA; HITQWIN; -. DR BioCyc; MPNE272634:GJ6Z-550-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 427 Uncharacterized protein MPN_509. FT /FTId=PRO_0000215256. SQ SEQUENCE 427 AA; 49815 MW; 01E40E90B7A0DD67 CRC64; MKFHTVYVGK NTKIDLDFAL QAQTNNFSSL EELRESFTNS GQTLSTQLFW KPVIDKLITD EGNDLTTIAR TAIGENLFDL KVNLTDSVID GTVLTKARKS FEERILNPFI EQRKEAKRIH DEEQARLERE RKQLEEELKG KEKKVQELIR EKTRFLSSFN NVKSFKDYWK GKGKNVEIKS QLIEVLKLAF KTDRNRTFIF LTDAFRNAVD WYYNAKKDDQ DSKKKAFGDV GIELPKLGVD GIFIPNWLRW ELKHRANLKL NLQSVTTKDI HNDINGWGVP KQIFWNEAKN GIEFRQTYPF KYAFQIRMKY TGDYGLKGIY WTLANWGLGG IPPEWKGEME LVLNVDGQLA DWITSKKDYP GTLFQFRDDK LLFTLHITQW INVQDQRFKG LLKKQQLDVL EPWGGDIKVP VVDLASYLHF LILADKS // ID Y513_MYCPN Reviewed; 150 AA. AC P75273; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MPN_513; GN OrderedLocusNames=MPN_513; ORFNames=F04_orf150, MP329; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95977.1; -; Genomic_DNA. DR PIR; S73655; S73655. DR RefSeq; NP_110201.1; NC_000912.1. DR RefSeq; WP_010874869.1; NC_000912.1. DR ProteinModelPortal; P75273; -. DR EnsemblBacteria; AAB95977; AAB95977; MPN_513. DR GeneID; 876811; -. DR KEGG; mpn:MPN513; -. DR PATRIC; 20022476; VBIMycPne110_0565. DR OMA; DITCASE; -. DR OrthoDB; EOG6KT2KK; -. DR BioCyc; MPNE272634:GJ6Z-554-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR019476; T4SS_TraD_DNA-bd. DR Pfam; PF10412; TrwB_AAD_bind; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 150 Uncharacterized protein MPN_513. FT /FTId=PRO_0000210691. SQ SEQUENCE 150 AA; 16844 MW; DB7B0B2F20E0B864 CRC64; MYDMINAKYL GKLIFLDFGQ TITSLEETSD NSTFFIADEF GNFGSHYVGV VLEQVRSFNT VVILSYQSFA NLRNIGGDNF KSQIINNTST LIAHRLIDMM EAEEVANLYG VDITCASEIK SLKVGQALVR SISSYYGEIK DWLVQQIDKS // ID Y570_MYCPN Reviewed; 129 AA. AC P75208; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MG389 homolog; GN OrderedLocusNames=MPN_570; ORFNames=D02_orf129, MP272; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95920.1; -; Genomic_DNA. DR PIR; S73598; S73598. DR RefSeq; NP_110259.1; NC_000912.1. DR RefSeq; WP_010874927.1; NC_000912.1. DR EnsemblBacteria; AAB95920; AAB95920; MPN_570. DR GeneID; 876852; -. DR KEGG; mpn:MPN570; -. DR PATRIC; 20022619; VBIMycPne110_0632. DR OMA; WYNITIM; -. DR OrthoDB; EOG6QP199; -. DR BioCyc; MPNE272634:GJ6Z-616-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 129 Uncharacterized protein MG389 homolog. FT /FTId=PRO_0000210591. FT TRANSMEM 5 25 Helical. {ECO:0000255}. SQ SEQUENCE 129 AA; 15149 MW; AE7D43C6285D3E6C CRC64; MKQKIIGLTL AFFVLFLTAV AILFTVKVQR YLTTSLWAKL SEQTFLVFKN EQDEAQFNQV SWTNFQAETT KKEDKKAFRL YKKKISLEQL ENENQQQLFQ AVNLSINLKQ GWYNITILLP SKALFETVF // ID Y581_MYCPN Reviewed; 265 AA. AC P75199; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MPN_581; GN OrderedLocusNames=MPN_581; ORFNames=D02_orf265V, MP261; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95909.1; -; Genomic_DNA. DR PIR; S73587; S73587. DR RefSeq; NP_110270.1; NC_000912.1. DR RefSeq; WP_010874938.1; NC_000912.1. DR EnsemblBacteria; AAB95909; AAB95909; MPN_581. DR GeneID; 877281; -. DR KEGG; mpn:MPN581; -. DR PATRIC; 20022639; VBIMycPne110_0642. DR OrthoDB; EOG6PGK11; -. DR BioCyc; MPNE272634:GJ6Z-627-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022382; DUF31. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 265 Uncharacterized protein MPN_581. FT /FTId=PRO_0000210731. SQ SEQUENCE 265 AA; 30452 MW; 0C16759A0FACE61C CRC64; MQLEKVPRAE YQTKWATNTV PKPTDFYHQL YNLSFSLTLT SQRWNTYGTG WLIDWKDTST NENKFTAYLA TNFHVADTLK NPHDYPPYNQ VDNTQDLTTS FRIGKYTDPS LFGLYTNVKH AFVDVQLAAL PKMAYAAVDF VDYRFDNKHW KSLNEICPEV GLKPYADFAV LEVPLYLNNK LDYQVWENFI KPAIATYKAL GDSTNLFAST SSSDLQNDTY FALGYPLLES NIDAIHFNQT GATLTSVPVK DRIKVKNQSF WTLNK // ID Y587_MYCPN Reviewed; 150 AA. AC P75193; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 76. DE RecName: Full=Uncharacterized lipoprotein MPN_587; DE Flags: Precursor; GN OrderedLocusNames=MPN_587; ORFNames=D02_orf150, MP255; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95903.1; -; Genomic_DNA. DR PIR; S73581; S73581. DR RefSeq; NP_110276.1; NC_000912.1. DR RefSeq; WP_010874944.1; NC_000912.1. DR EnsemblBacteria; AAB95903; AAB95903; MPN_587. DR GeneID; 876823; -. DR KEGG; mpn:MPN587; -. DR PATRIC; 20022655; VBIMycPne110_0650. DR BioCyc; MPNE272634:GJ6Z-633-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 150 Uncharacterized lipoprotein MPN_587. FT /FTId=PRO_0000018742. FT LIPID 23 23 N-palmitoyl cysteine. {ECO:0000255}. FT LIPID 23 23 S-diacylglycerol cysteine. {ECO:0000255}. SQ SEQUENCE 150 AA; 16957 MW; 77A351BE8C1CDEDE CRC64; MVIALKRFSF LASIATLTVL NACATISLSD KSGEFYINNI PSSAELHRIN YDLTFSLGFT NRIQTKKKNE VNFVAFYGTG LLIDWKEGNQ YQPFRVYLAT NVHVAAGLKN EADYLPYSQP DAELGWTVDF RLGKYTNVKD FVSPNENRIT // ID Y590_MYCPN Reviewed; 217 AA. AC Q50337; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized lipoprotein MPN_590; DE Flags: Precursor; GN OrderedLocusNames=MPN_590; ORFNames=D02_orf217L, MP252; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U43738; AAC43666.1; -; Genomic_DNA. DR EMBL; U00089; AAB95900.1; -; Genomic_DNA. DR PIR; S62795; S62795. DR RefSeq; NP_110279.1; NC_000912.1. DR RefSeq; WP_010874947.1; NC_000912.1. DR IntAct; Q50337; 1. DR EnsemblBacteria; AAB95900; AAB95900; MPN_590. DR GeneID; 877391; -. DR KEGG; mpn:MPN590; -. DR PATRIC; 20022661; VBIMycPne110_0653. DR OMA; NDYEFFN; -. DR BioCyc; MPNE272634:GJ6Z-636-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 32 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 33 217 Uncharacterized lipoprotein MPN_590. FT /FTId=PRO_0000018744. FT LIPID 33 33 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 33 33 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 217 AA; 24705 MW; 4EAD367098412583 CRC64; MPITKATPLF LRYRLKGFVF LTLLLVQGVF TACAPAVPVN NKSVSAVQPE DKQALKPDPA LGEYTSDLKF NTNFIPKKDD PFRPFYDLSF TLQFQDPYTA TYGTGWLIDW KDNNQPNKFT AYIATNLHVA DNLRNVNDYE FFNQFDYFDD PTESFTLGKF VDGNEIKQIV PDAMHEPSLV RIETSKLPKT AYTTTLFIND LGEYRLPAAD FAVLESI // ID Y596_MYCPN Reviewed; 569 AA. AC Q50333; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG397 homolog; GN OrderedLocusNames=MPN_596; ORFNames=D02_orf569, MP246; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43738; AAC43661.1; -; Genomic_DNA. DR EMBL; U00089; AAB95894.1; -; Genomic_DNA. DR PIR; S62851; S62851. DR RefSeq; NP_110285.1; NC_000912.1. DR RefSeq; WP_010874953.1; NC_000912.1. DR IntAct; Q50333; 1. DR EnsemblBacteria; AAB95894; AAB95894; MPN_596. DR GeneID; 877127; -. DR KEGG; mpn:MPN596; -. DR PATRIC; 20022673; VBIMycPne110_0659. DR OMA; YDSLFYL; -. DR OrthoDB; EOG66TG3D; -. DR BioCyc; MPNE272634:GJ6Z-642-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005940; C:septin ring; IEA:InterPro. DR GO; GO:0000921; P:septin ring assembly; IEA:InterPro. DR InterPro; IPR010379; EzrA. DR Pfam; PF06160; EzrA; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 569 Uncharacterized protein MG397 homolog. FT /FTId=PRO_0000210593. FT TRANSMEM 2 22 Helical. {ECO:0000255}. SQ SEQUENCE 569 AA; 66340 MW; BF9358825D309BB4 CRC64; MVVIAALLGS LAVLAFLFYL WYLTIFIIVH KNQQYLEQTK ALYNKLKLSN FNSVIVPFQL LRSEKKALEQ PVKLLKSFQE SFNSEINSAL EQLLVFSEPK ALYNCFWFNR NIKLLRKNLQ GLHDKQQRYV KLTKNAIAYF DSSYDTLVFY RQAFCLLVSF INDFLVHKYD SLFYLNIINR ISLLFKDVEL HIKNKDVKQQ NQALNKLHNN LAQTIITASR QYFFDVKVGY LNYHFQILSQ KVTQLRSMKN KAINSQEVAK FQELITNIGA TLAECSQALG NINLALCEQR INQAKEQIDV LSNAVSVKEK AISLVVSNVD SFLKSINHYQ QQNALLQTLM KEIELMFQNN LDTVNIINQI NEHSLLIAQK TQLLNQENAL TEFIDYEKLF RLMSEAMKLL DGLKNLLNEL FALSANKFDD YRFFVYTLDD FRFKFFQIEN LIANEELIIS EKTLKIISQA KHQFDDIFTQ AKNDYEGAFS YLNEKVRFFQ NQLTHVIVDV VGLMNLRSMC KHTFIFANKY RQESPQINES LETLTQFYQQ QNYSETLSGL ISLLGKIKSS AKQHHLDLN // ID Y605_MYCPN Reviewed; 157 AA. AC Q50325; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MG406 homolog; GN OrderedLocusNames=MPN_605; ORFNames=C12_orf157L, MP237; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43738; AAC43652.1; -; Genomic_DNA. DR EMBL; U00089; AAG34742.1; -; Genomic_DNA. DR PIR; S62842; S62842. DR RefSeq; NP_110294.1; NC_000912.1. DR RefSeq; WP_010874962.1; NC_000912.1. DR EnsemblBacteria; AAG34742; AAG34742; MPN_605. DR GeneID; 877043; -. DR KEGG; mpn:MPN605; -. DR PATRIC; 20022691; VBIMycPne110_0668. DR OMA; ARYLIYL; -. DR OrthoDB; EOG6G4VVV; -. DR BioCyc; MPNE272634:GJ6Z-651-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 157 Uncharacterized protein MG406 homolog. FT /FTId=PRO_0000210595. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. SQ SEQUENCE 157 AA; 18291 MW; 7D9097A405DAD3C4 CRC64; MYNWTNKKLT KAIALIILVL WLVVLVGILV WALTTQHLKV LYGWLLPFPF VALSVVGLLK LGDFFEKFKH LSKQRVTVFF GSFFVARYLL YLIPVLLAFF IRPQYFHVIA TIISTLFFPL LKIVISFAWL PLEYHCKNLI SKLNKKHVTT GDSFKRT // ID Y613_MYCPN Reviewed; 344 AA. AC P75182; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MG415 homolog; GN OrderedLocusNames=MPN_613; ORFNames=C12_orf344, MP229; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG414/MG415 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; U00089; AAB95877.1; -; Genomic_DNA. DR PIR; S73555; S73555. DR RefSeq; NP_110302.1; NC_000912.1. DR RefSeq; WP_010874970.1; NC_000912.1. DR EnsemblBacteria; AAB95877; AAB95877; MPN_613. DR GeneID; 877108; -. DR KEGG; mpn:MPN613; -. DR PATRIC; 20022709; VBIMycPne110_0677. DR OMA; LNANDVW; -. DR OrthoDB; EOG6W19D7; -. DR BioCyc; MPNE272634:GJ6Z-659-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 344 Uncharacterized protein MG415 homolog. FT /FTId=PRO_0000210601. SQ SEQUENCE 344 AA; 39640 MW; E4D72A67B73D0AE1 CRC64; MVFSFQDDTA LTVALNSIKL VKNPEELIPG LIPTNPKTGI FYIAAEITNS NNFFKWGTDS NREIIKGQMY FLKKETKIPT IRTYLFQMRT HKIALNANDV WFQANNDKVK VIVDGIELDQ FDPKLPNVAF FNDYQVDLVS TLTLADKQLL IRRLNLALVG MNLMVDEQAT NIETFPKQIR LTTKSIDQSF DFDVEFNPKA SELNVIVKVD EQPLFKLDYE LVIKNSNTLQ LVNRNKHLGM YIWSVADQRY QAKLLDTLQL FLQSKQMYLK EKIPLKLQDN TATFKIAKQA QPNNGENKNT NFIGYLVIAA SSLFLVVVAF SFYFYKRKKN LKSHKQKAVV KTDK // ID Y664_MYCPN Reviewed; 237 AA. AC P75127; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=DegV domain-containing protein MG450 homolog; GN OrderedLocusNames=MPN_664; ORFNames=K05_orf237, MP178; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and CC may play a role in lipid transport or fatty acid metabolism. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 DegV domain. {ECO:0000255|PROSITE- CC ProRule:PRU00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95826.1; -; Genomic_DNA. DR PIR; S73504; S73504. DR RefSeq; NP_110353.1; NC_000912.1. DR RefSeq; WP_010875021.1; NC_000912.1. DR ProteinModelPortal; P75127; -. DR EnsemblBacteria; AAB95826; AAB95826; MPN_664. DR GeneID; 877027; -. DR KEGG; mpn:MPN664; -. DR PATRIC; 20022813; VBIMycPne110_0729. DR OMA; ISMMPAN; -. DR OrthoDB; EOG65TRSF; -. DR BioCyc; MPNE272634:GJ6Z-710-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR InterPro; IPR003797; DegV. DR Pfam; PF02645; DegV; 1. DR TIGRFAMs; TIGR00762; DegV; 1. DR PROSITE; PS51482; DEGV; 1. PE 3: Inferred from homology; KW Complete proteome; Lipid-binding; Reference proteome. FT CHAIN 1 237 DegV domain-containing protein MG450 FT homolog. FT /FTId=PRO_0000209775. FT DOMAIN 1 236 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 16 16 Fatty acid. {ECO:0000250}. FT BINDING 44 44 Fatty acid. {ECO:0000250}. SQ SEQUENCE 237 AA; 26839 MW; 1E6D6F2BA5D1FDFC CRC64; MANAPKGVKF STSQTTEEIV RAKVSELVEQ YDLIIGIPID KEISASYANW KLVEKDYASK FHVLDARAVE MIIDWLINDI KGWLNTNPYS REGLDRFVEQ YRKKTAAVLF VTDTKPLVAG GRLSNLKSFI IKSLKFHLLI SFLGENGKLQ FFDKARSAHD AHKLAVKFLK KQLLKHSAKL KRGAFLTTVF DEQTNTNLVQ EFDKLLDHSI NIEQSLLSPV ICTHTGLNSY VIVLQGE // ID Y677_MYCPN Reviewed; 425 AA. AC P75115; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG461 homolog; GN OrderedLocusNames=MPN_677; ORFNames=K05_orf425, MP165; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 HD 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; U00089; AAB95813.1; -; Genomic_DNA. DR PIR; S73491; S73491. DR RefSeq; NP_110366.1; NC_000912.1. DR RefSeq; WP_010875034.1; NC_000912.1. DR ProteinModelPortal; P75115; -. DR IntAct; P75115; 2. DR EnsemblBacteria; AAB95813; AAB95813; MPN_677. DR GeneID; 877238; -. DR KEGG; mpn:MPN677; -. DR PATRIC; 20022843; VBIMycPne110_0744. DR KO; K06885; -. DR OMA; LINRYHM; -. DR OrthoDB; EOG6WX4K7; -. DR BioCyc; MPNE272634:GJ6Z-723-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 425 Uncharacterized protein MG461 homolog. FT /FTId=PRO_0000210630. FT DOMAIN 55 184 HD. SQ SEQUENCE 425 AA; 50586 MW; 9807D402C85DEF97 CRC64; MQQIFFKDPI LGEVLFDQQT KWMYELVETE AFRRLRNIKQ LGINFHFYPG GVHTRYSHSL GVYELLRRIL NTPAFAPIDE NKKQTVLVAG LLHDIGHAPH SHAFEIYFAK APNFKKELFI HEEVTTLFVN SEPIKSILKA NQIDPKLVAA LIDENKELKP SNYWMRQLIS SDLDADRMDY LLRDSYFTGT SHSLIDYQTI IKEMDCVKVK GIYEIFFKDK CLPLIENFLI TRHHMYQSIY SDGRSISTEL NLWFVFQRIK DLVDKNQFDF NGYKTLEQVC LPLLKNEHFD KKMLPAFVKL DDYVFQSFFV NLYQTTKDKI LKKLLDSYLN SLKFEIKFYE TKEQRDLDFE KQASKYKDAK YFITKFNNQF KGFYEGWSSH KNELKIKTMQ NKHTNLSEIS MLVKRSNELF FENALYKWAN VFYRL // ID Y195_MYCPN Reviewed; 434 AA. AC Q50292; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MG181 homolog; GN OrderedLocusNames=MPN_195; ORFNames=GT9_orf434, MP636; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ 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; U34795; AAC43686.1; -; Genomic_DNA. DR EMBL; U00089; AAB96284.1; -; Genomic_DNA. DR PIR; S62813; S62813. DR RefSeq; NP_109883.1; NC_000912.1. DR RefSeq; WP_010874552.1; NC_000912.1. DR IntAct; Q50292; 1. DR PRIDE; Q50292; -. DR EnsemblBacteria; AAB96284; AAB96284; MPN_195. DR GeneID; 876880; -. DR KEGG; mpn:MPN195; -. DR PATRIC; 20021713; VBIMycPne110_0213. DR KO; K16785; -. DR OMA; WRIVPIN; -. DR OrthoDB; EOG6ZSP8P; -. DR BioCyc; MPNE272634:GJ6Z-202-MONOMER; -. DR Proteomes; UP000000808; 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; IPR003339; ABC/ECF_trnsptr_transmembrane. DR Pfam; PF02361; CbiQ; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 434 Uncharacterized protein MG181 homolog. FT /FTId=PRO_0000210449. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 244 264 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 387 407 Helical. {ECO:0000255}. SQ SEQUENCE 434 AA; 49137 MW; 63D0B734447F697D CRC64; MDSFFINGYV PRDTFIHRLH PTTKLLIFLL FVILVFVPIG FVFQSVIFVF ATVIFFVAKL PGRFYLSSIK SISLLFLLLL FVNWFTFRDP GFYITADQVN TVKPHFNGNN FNFWNISLFN YQDNVFSQVF NFNRANMTEL NKINFFFKET ANANAYTKVT GIDKLAEMLA SKNLFKFNGS TNGIDKNKIL GAFLDHKIAV YLGRSWGGDF SGFVIDVSVS DKTSTFTIKP FLANSNYVLT LRAIILAFYV TQKILIMIIL ATVLTSTSSS VELAYGIERL LWPLKLLRVP VNVFAMTIAI AIRFVPSLLL ESQRILNAQA SRGLDFKNGN FFVKMRSLSS LVVPMISIAF RNAGELASAM EARGYDPTKK RTTYRKFKID WVDATALILT ALYFVVIIFL TVKGAVFLDL GTPEWLLTGK IKEQVERSLS VKSA // ID Y259_MYCPN Reviewed; 517 AA. AC P75515; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein MG120 homolog; GN OrderedLocusNames=MPN_259; ORFNames=A65_orf517, MP574; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96222.1; -; Genomic_DNA. DR PIR; S73900; S73900. DR RefSeq; NP_109947.1; NC_000912.1. DR RefSeq; WP_010874616.1; NC_000912.1. DR ProteinModelPortal; P75515; -. DR IntAct; P75515; 1. DR EnsemblBacteria; AAB96222; AAB96222; MPN_259. DR GeneID; 876922; -. DR KEGG; mpn:MPN259; -. DR PATRIC; 20021843; VBIMycPne110_0278. DR KO; K02057; -. DR OMA; GPIGHLQ; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; MPNE272634:GJ6Z-266-MONOMER; -. DR Proteomes; UP000000808; 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 InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 517 Uncharacterized protein MG120 homolog. FT /FTId=PRO_0000210424. FT TRANSMEM 35 55 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 102 122 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 302 322 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 352 372 Helical. {ECO:0000255}. SQ SEQUENCE 517 AA; 58585 MW; 3BF2FB0D10C40E4F CRC64; MNALNYLKHR FLFSKDKFWY APFKQKQRRS IYSTFSLIVL SFIVSFFLIV AIPGIKGGTF LEIFTRLFKD RINIENFARQ IAIYTLAALA FSFCMSVGVF NIGISGQMMA GANFGFMMIL KVFPESFRPA FGGQIITILL MILGSVTVAM VVAALKVFFK VNEVVSAIML NWVIVLVSAY LVGTYIKPEK TDTSQFYSIE LPDAFALYNF SDVQQKYGWL TSLVIAIAAA IFIAVLMKFT VFGHKLKSTG LSVTGSQAAG YSVKKYQFLS FVISGILSGL LAAVVYTASF EKQLTFSDVG DFGITSVPIT GFDGIAIGLI ALNSPARIVI VSTIISFVTI GAKPAGLNAA TASLVLGIMM YFAAIYNLMI YIKPWRMIVK LNISKMNEAA YDEFQNEMAA NLETLSFQRF LDKQKRKHDK ERMVWFDTKR FEEYQKKKQA TLQTFHENSS QNLLQYWKQQ LLVADVKRLT FKWDFLTFKH QQKYILRWYK GKNKKQTALE NEFASLNEAI SQKLEEK // ID Y260_MYCPN Reviewed; 311 AA. AC P75514; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein MG121 homolog; GN OrderedLocusNames=MPN_260; ORFNames=A65_orf311, MP573; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96221.1; -; Genomic_DNA. DR PIR; S73899; S73899. DR RefSeq; NP_109948.1; NC_000912.1. DR RefSeq; WP_010874617.1; NC_000912.1. DR ProteinModelPortal; P75514; -. DR EnsemblBacteria; AAB96221; AAB96221; MPN_260. DR GeneID; 877290; -. DR KEGG; mpn:MPN260; -. DR PATRIC; 20021845; VBIMycPne110_0279. DR KO; K02057; -. DR OMA; IGIAMMQ; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; MPNE272634:GJ6Z-267-MONOMER; -. DR Proteomes; UP000000808; 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 InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 311 Uncharacterized protein MG121 homolog. FT /FTId=PRO_0000210426. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 198 218 Helical. {ECO:0000255}. FT TRANSMEM 233 253 Helical. {ECO:0000255}. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255}. SQ SEQUENCE 311 AA; 33493 MW; B0EC5DAD03B2A33F CRC64; MSQSLISFSN LDNWLFVAPA LLLAVLSGYL SERVGIVNIA INGGMVFGGM FLSLMSYAFV PNANDSAPSW SLAISIPLSV IFASAVGFLF GIAAIKLKAD HVIVGTGVNL LGTGINFFVA QNARSLLNDT DLRVRYSFVR TGNSVSIEGI AIFAFAIIFV LLVWYLMNFT KTGLRYRAVG ENPNVIDTQG ISVYKYQWFG VMASTMVAAL AGCCFALSPQ VPSFSSGDVS GFGFIAIAIM IISMWRIIPS IVISPLFALA YVLTTGVVGN ANNTYLLRTI PFIISLLVMM VFGYLNVGPK NVGKHFDKGL R // ID Y282_MYCPN Reviewed; 166 AA. AC P75495; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MPN_282; GN OrderedLocusNames=MPN_282; ORFNames=A65_orf166, MP553; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96201.1; -; Genomic_DNA. DR PIR; S73879; S73879. DR EnsemblBacteria; AAB96201; AAB96201; MPN_282. DR PATRIC; 20021891; VBIMycPne110_0302. DR OrthoDB; EOG6JMMQZ; -. DR BioCyc; MPNE272634:GJ6Z-289-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004890; Lipoprotein_10_C. DR Pfam; PF03202; Lipoprotein_10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 166 Uncharacterized protein MPN_282. FT /FTId=PRO_0000215279. SQ SEQUENCE 166 AA; 18396 MW; 1A6B21599ED1B830 CRC64; MKTIYIYKGS IPEDKKKGDN AIWVTEKKII DALEKAANSN GESTQSNPKT IALQAAKKET KKSNKKESKT IGYTTTGYVN ADGKHIFDTD RINNERFDRK IIIGATLETL DQSSTLQSGE AIVLPAPGKY KSSDQKTVMT AQGPKIIGIH ANAKENEETQ KFVNWF // ID Y292_MYCPN Reviewed; 309 AA. AC P75485; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized RNA pseudouridine synthase MG209 homolog; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase; DE AltName: Full=RNA-uridine isomerase; GN OrderedLocusNames=MPN_292; ORFNames=H10_orf309, MP543; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96191.1; -; Genomic_DNA. DR PIR; S73869; S73869. DR RefSeq; NP_109980.1; NC_000912.1. DR RefSeq; WP_010874649.1; NC_000912.1. DR ProteinModelPortal; P75485; -. DR IntAct; P75485; 4. DR EnsemblBacteria; AAB96191; AAB96191; MPN_292. DR GeneID; 876732; -. DR KEGG; mpn:MPN292; -. DR PATRIC; 20021919; VBIMycPne110_0316. DR KO; K06180; -. DR OMA; KVCHETG; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; MPNE272634:GJ6Z-299-MONOMER; -. DR Proteomes; UP000000808; 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; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; RNA-binding. FT CHAIN 1 309 Uncharacterized RNA pseudouridine FT synthase MG209 homolog. FT /FTId=PRO_0000162740. FT DOMAIN 11 87 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 131 131 {ECO:0000250}. SQ SEQUENCE 309 AA; 35229 MW; 7F2D8135F9C75A40 CRC64; MEQTFSVTTA QRLDTFLATL LNLSRVKVAK LIVDGLVSVN GKKITKNGWL VQPEDRVHVN WSEELFEKVP VEVQPYDFPL DILYEDEQIM VVNKPNGLIS HPTSFNESES LLGAALFHCN HQPVFLVHRL DRDTSGVIML AKNQSSLLHL QKQLQQRVMK RYYLALVHFP LDSLSGTISA PLERVGNNKV MWKVGNSSNK AKNAFTKFTV LNQNEKAALI KCELLTGRTH QIRVHLQFIK HPVYNDPLYG LKSEQATEYG QYLHAQQISF IHPTLNKEMG FEAQLDKTFS DKLDNLNLKI ANSLYALFQ // ID Y294_MYCPN Reviewed; 206 AA. AC P75483; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MPN_294; GN OrderedLocusNames=MPN_294; ORFNames=H10_orf206, MP541; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96189.1; -; Genomic_DNA. DR PIR; S73867; S73867. DR RefSeq; NP_109982.1; NC_000912.1. DR RefSeq; WP_010874651.1; NC_000912.1. DR ProteinModelPortal; P75483; -. DR IntAct; P75483; 1. DR DNASU; 877198; -. DR EnsemblBacteria; AAB96189; AAB96189; MPN_294. DR GeneID; 877198; -. DR KEGG; mpn:MPN294; -. DR PATRIC; 20021923; VBIMycPne110_0318. DR OMA; PSALMCI; -. DR OrthoDB; EOG64XXT0; -. DR BioCyc; MPNE272634:GJ6Z-301-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002818; DJ-1/PfpI. DR Pfam; PF01965; DJ-1_PfpI; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 206 Uncharacterized protein MPN_294. FT /FTId=PRO_0000210658. SQ SEQUENCE 206 AA; 23219 MW; 0C8504A5C45BD85D CRC64; MDLLTTANKT PRIAKSRPVR IAIIITQKTN DLHATVPCFL WRKARYAVDL ISAEAKASIM LEMGIHVRCD NTLSKTNFNQ YTAAFIPHGN TTRLVEIDKL RKDLEKFVYK PKGPMRWLFS SGNGACVLKE FDLIAPDQLV TVQNEKEMVK LLGKNFIKQP VHVDKNIISC ANSCGLTKFS FKVIEELSGI ELARKTANLV DHIYKG // ID Y308_MYCPN Reviewed; 565 AA. AC P75472; O08088; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein MPN_308; GN OrderedLocusNames=MPN_308; ORFNames=F10_orf565, MP528; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_095 and MPN_096. {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; U00089; AAB96176.1; -; Genomic_DNA. DR EMBL; U59896; AAB52525.1; -; Genomic_DNA. DR PIR; S73854; S73854. DR RefSeq; NP_109996.1; NC_000912.1. DR RefSeq; WP_010874664.1; NC_000912.1. DR ProteinModelPortal; P75472; -. DR EnsemblBacteria; AAB96176; AAB96176; MPN_308. DR GeneID; 877171; -. DR KEGG; mpn:MPN308; -. DR PATRIC; 20021968; VBIMycPne110_0332. DR OMA; IMNIFIA; -. DR OrthoDB; EOG6G4VVV; -. DR BioCyc; MPNE272634:GJ6Z-324-MONOMER; -. DR Proteomes; UP000000808; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 565 Uncharacterized protein MPN_308. FT /FTId=PRO_0000210659. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 367 387 Helical. {ECO:0000255}. FT TRANSMEM 424 444 Helical. {ECO:0000255}. FT TRANSMEM 460 480 Helical. {ECO:0000255}. FT TRANSMEM 482 502 Helical. {ECO:0000255}. FT TRANSMEM 516 536 Helical. {ECO:0000255}. SQ SEQUENCE 565 AA; 62560 MW; ACC745B43D2184E2 CRC64; MKQQKPKISF IAAMLIVIGS SIGAGIFFKS STVLENSQAS LVLAIFNWLV ASVAVIAMAL ALIEIASVRN DNLSIISWVK VFNRRWLYHG CKNFMTYLYL PLTFFFMPLY FICSIQDGFR GLLGLETGAH FNTSVDWLIW LALALIITTY FLTIPPLYAK VGNIQNMVVS AVKFIPLVFV PIIGFIVAGT GNGELKNVKA LVQPPQINGA TASFTQLVQA GYGITRFTGI GAGMGSFISI AAIFFAYDGF YVTAGLQSEM REPKKTPWAL FLGLLITTLF YLILAVALSI NGGLFSGMEE SMGKLFNNKR AGQIVFGVVN LMIGIGVLGI INGFALWAPR FVEDLLAQGD LPFWKQVQGR LNPNKPVVGV IYCLVLSLTV QVLFTVIGAL AYLPTVADYK NYVNTEIDKL NSMQWLYSFS DLMATWTSLF TFAFIACAIF GAIVNRKTKK ITIANPKRYF LPAAWIAVVV NCISVFVTII EPFINLFLLF GYDETVAHTV LGNDFIELNE LVIGRVMLIV VLVFFAIISF LPVYVEDQYH KRKFGSLANY QQYVQQHLAH STING // ID Y329_MYCPN Reviewed; 158 AA. AC P75456; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG236 homolog; GN OrderedLocusNames=MPN_329; ORFNames=F10_orf158, MP507; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96155.1; -; Genomic_DNA. DR PIR; S73833; S73833. DR RefSeq; NP_110017.1; NC_000912.1. DR RefSeq; WP_010874685.1; NC_000912.1. DR ProteinModelPortal; P75456; -. DR IntAct; P75456; 1. DR EnsemblBacteria; AAB96155; AAB96155; MPN_329. DR GeneID; 877197; -. DR KEGG; mpn:MPN329; -. DR PATRIC; 20022012; VBIMycPne110_0353. DR OMA; NDFYIVA; -. DR OrthoDB; EOG6FBX26; -. DR BioCyc; MPNE272634:GJ6Z-346-MONOMER; -. DR Proteomes; UP000000808; Chromosome. 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 158 Uncharacterized protein MG236 homolog. FT /FTId=PRO_0000210474. SQ SEQUENCE 158 AA; 18856 MW; F6C0D2105D2C71C5 CRC64; MVLKSKGSVL DLEHDNQTLK DYISVFERNK MRLTQSRLML LQCLVQHRDW HTLAELKHHL EQNQQRTTLA SIYNNLKIFA KLKLINIFVD TNRFETYYCL RHENHKHIYF FDENQRKFLT LPLQDKEALS LIGHKSKHGK IKLNDFYIVA SGTLEDDQ // ID Y333_MYCPN Reviewed; 750 AA. AC P75445; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Uncharacterized protein MPN_333; GN OrderedLocusNames=MPN_333; ORFNames=F10_orf750, MP503; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_335. {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; U00089; AAB96151.1; -; Genomic_DNA. DR PIR; S73829; S73829. DR RefSeq; NP_110021.1; NC_000912.1. DR RefSeq; WP_010874689.1; NC_000912.1. DR EnsemblBacteria; AAB96151; AAB96151; MPN_333. DR GeneID; 877353; -. DR KEGG; mpn:MPN333; -. DR PATRIC; 20022020; VBIMycPne110_0357. DR KO; K01992; -. DR OrthoDB; EOG6RRKZQ; -. DR BioCyc; MPNE272634:GJ6Z-350-MONOMER; -. DR Proteomes; UP000000808; 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; IPR032688; ABC2_membrane_2. DR Pfam; PF12679; ABC2_membrane_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 750 Uncharacterized protein MPN_333. FT /FTId=PRO_0000210661. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 724 744 Helical. {ECO:0000255}. SQ SEQUENCE 750 AA; 85313 MW; 5CF64FD4EE600E5A CRC64; MFVLLMLALV MLFIVQSSTN VIALWTNNVF QFSLILIPLV TLLAGSITAD IFIEGYNNGI ELFLFSKPIS RDRILLIKLL VLLMYLSIVA VLSTAVVSLG YFTRNEIESY LDDLALSIFV GTILNGIIFS AVTIMLATRF SNIQSLIILL LFVSLFSFSS PIARLIFDTP AKTLSQQGYS VRQINGIAHS ESPNVERKIY VSVKKRRLTG VDREEKELWK SDEQAALRGR NLYEEAQRTS SYINSFYTNI GYLFGSLYRL GALADENNFD ASVATQNTKI RFGKLVDLDK STDIIGYRTK DRFGRFFRFH LRFPTLNFKQ SLSNSGVFFI NKRGLVKATF SAGDDAFKRD PKIMQKVFDT FLESFSWFLD KKINRRIARI YAESDNKGSP FPKEGDDENT KGDDNSSEKT DTVSVSTKLK TTADQSESTQ MSSESTATGI SSDPQSQGKM NNKSEEQKKK EKELTWQIYR DIKFLNSIYF LQVNNERLWD NVAFLNKVNA EDQNGDKNQF AQAMASLNKQ INMFYVLNEI TNKEHNLPTK YGAYSDQLKK VINENFEKIE NKKKEIEEKQ NKEFQENKNG ASNNQDTKQD AQKGDTNTQS TELKARQAQQ VQKDQQNDSK GNTATNSDTG KSDNKTDTTE DEQNTYKPLT AREKKTKIKE LTKDIFFSTA QNYLFLVQGG YNNKLFAGGL PELHQRFLSD VVVDFSEEKL VYEVQGEPIV SSVATIVITL FLTVVLLAIA FFFFKYRNVK // ID Y337_MYCPN Reviewed; 621 AA. AC P75441; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MG241 homolog; GN OrderedLocusNames=MPN_337; ORFNames=F10_orf621, MP499; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96147.1; -; Genomic_DNA. DR PIR; S73825; S73825. DR RefSeq; NP_110025.1; NC_000912.1. DR RefSeq; WP_010874693.1; NC_000912.1. DR IntAct; P75441; 1. DR EnsemblBacteria; AAB96147; AAB96147; MPN_337. DR GeneID; 877243; -. DR KEGG; mpn:MPN337; -. DR PATRIC; 20022028; VBIMycPne110_0361. DR OMA; YNDFENT; -. DR OrthoDB; EOG6HMXP6; -. DR BioCyc; MPNE272634:GJ6Z-354-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 621 Uncharacterized protein MG241 homolog. FT /FTId=PRO_0000210480. FT TRANSMEM 240 260 Helical. {ECO:0000255}. FT TRANSMEM 548 568 Helical. {ECO:0000255}. FT TRANSMEM 587 607 Helical. {ECO:0000255}. SQ SEQUENCE 621 AA; 72814 MW; 29ECFF2B3FF4C7CC CRC64; MVKKELEMYN LYTFQIDLDK KLLFEKADNQ QNYSKIRARY FKNSARNQQA VFLNKNLIKN TFNKALLNFS DFLSGSGVES IFKQVIDDQP EVLNYLKQVK KEDSCDGHSE ASQLVFNVVI NPKNTLANFF EELTIYLHFN EENNTVVGSF SLKWNIKRAD LFSETKNIAI NNLIHTFCKN NLNEVSFIQI IKCFAKTLIN KQGQIVLESC AFKQKWQNIV EQKYPFSTIH KNLKIVNSDF FDAFFVILLL ICHLNNNLLW LCEKTEHFEW KLNSKISNFK EDNTEVYLSK MLLFLKDWYF ENQAVTNEDI EKVDEVEDIG KLVEKYSANQ PQKLSSNSTV YVFEPDKKQC FLKNDDFFNT NEAKLLFLIT MQPNVFGLDD TAIANDLNLR EIGDFFKEID FTDSDVLNDF QQQKETLLVR RTFNQLLFMN SNTDVLSIVN NKFKSAIHNI VWTITYSKAI MLKAFDYSKI FEQNRTNDPS LLRSNLNSIN RLRYLSEYFR TASVKYDQLY TKVKEYMQLD QFLVDMINQV NHEDEIFGKY KERVYLSLGI VTAVVFGIIE FFNCVWTVLT VSQQTAEKSL ADPRNTVIIG IGTILVLTLL ITILTFMTRR LYLFEFNKKH K // ID Y373_MYCPN Reviewed; 204 AA. AC P75408; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MPN_373; GN OrderedLocusNames=MPN_373; ORFNames=A19_orf204, MP463; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_373 C-terminal region. 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; U00089; AAB96111.1; -; Genomic_DNA. DR PIR; S73789; S73789. DR RefSeq; NP_110061.1; NC_000912.1. DR RefSeq; WP_010874729.1; NC_000912.1. DR EnsemblBacteria; AAB96111; AAB96111; MPN_373. DR GeneID; 876791; -. DR KEGG; mpn:MPN373; -. DR PATRIC; 20022120; VBIMycPne110_0404. DR BioCyc; MPNE272634:GJ6Z-393-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 204 Uncharacterized protein MPN_373. FT /FTId=PRO_0000210666. FT TRANSMEM 160 180 Helical. {ECO:0000255}. SQ SEQUENCE 204 AA; 22588 MW; 75935B060A55C222 CRC64; MVSDGGGQTD NNAEGGNLRI ALTKNAFNPN QSTTVDIPYK IENRSVGNNK EQKTLVFDFS GLNPYEYNMI VGALFTDSSF INDAYAPIQS TFQRQLKEFL QVKYENQVGA NGSFDLFKPR SLSSQQLVQG ERSLDGFTVE LNANGGSFNF LTHVDPLVAG LTVAAIASVV VAGAVTYLVV RRYRKRNEFV DKIFASNIRA KQWR // ID Y388_MYCPN Reviewed; 128 AA. AC Q9EXD4; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 2. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MG269.1 homolog; GN OrderedLocusNames=MPN_388; ORFNames=MP449.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34751.2; -; Genomic_DNA. DR IntAct; Q9EXD4; 2. DR EnsemblBacteria; AAG34751; AAG34751; MPN_388. DR PATRIC; 20022152; VBIMycPne110_0419. DR OMA; ACYSSKI; -. DR BioCyc; MPNE272634:GJ6Z-410-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein MG269.1 homolog. FT /FTId=PRO_0000210501. SQ SEQUENCE 128 AA; 15221 MW; 600133A1B965FA17 CRC64; MSNFFEKYIN GFIETLDQID AADFQRIQHD FDPNQFPYDW VVERVSDVKD YLLNPRDFSD VETFKSTMRA KIKHFYACYS SKIPFFLFTS FVLAIFNSVG QYVKYHCDLD FTNPDAVTIF FREKALND // ID Y399_MYCPN Reviewed; 287 AA. AC P75384; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Uncharacterized protein MG280 homolog; GN OrderedLocusNames=MPN_399; ORFNames=F11_orf287, MP439; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96087.1; -; Genomic_DNA. DR PIR; S73765; S73765. DR RefSeq; NP_110087.1; NC_000912.1. DR RefSeq; WP_010874755.1; NC_000912.1. DR IntAct; P75384; 2. DR EnsemblBacteria; AAB96087; AAB96087; MPN_399. DR GeneID; 877146; -. DR KEGG; mpn:MPN399; -. DR PATRIC; 20022174; VBIMycPne110_0430. DR OMA; HEVTFRI; -. DR OrthoDB; EOG6P8TT4; -. DR BioCyc; MPNE272634:GJ6Z-422-MONOMER; -. DR Proteomes; UP000000808; 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; IPR030940; MG279/MG280. DR TIGRFAMs; TIGR04527; mycoplas_twoTM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 287 Uncharacterized protein MG280 homolog. FT /FTId=PRO_0000210507. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. SQ SEQUENCE 287 AA; 31786 MW; 1B1184005673A865 CRC64; MLLFINRFAK TIILLFGMLV FLVLLGLGGA ALYFKDNAAK LYIDTRKSID SSFDSSQAFI DTYNGSSSKF SVESINKQIE EVKKKVEEST KKLEEYEKQI NQAKGLNGYL VSPEKLKELQ EAKKSLQATK SQIEKYANTL KTANNGKTGQ NGTSSSTIPI TKISGSTISV STRDTNGKTN SALKDIQEFS TQANDIIKQY KEIKNKIPTE KQFNEYYTIG AITLVSVSGG VLAVLIVSTV MTFLGSKKLG LRTFSRLTST DQIADHVNDI LDRYPELEDA VLEELDQ // ID Y403_MYCPN Reviewed; 122 AA. AC P75381; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MG284 homolog; GN OrderedLocusNames=MPN_403; ORFNames=F11_orf122a, MP435; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96083.1; -; Genomic_DNA. DR PIR; S73761; S73761. DR RefSeq; NP_110091.1; NC_000912.1. DR RefSeq; WP_010874759.1; NC_000912.1. DR EnsemblBacteria; AAB96083; AAB96083; MPN_403. DR GeneID; 877216; -. DR KEGG; mpn:MPN403; -. DR PATRIC; 20022196; VBIMycPne110_0436. DR OMA; WNENDIN; -. DR OrthoDB; EOG6XHC67; -. DR BioCyc; MPNE272634:GJ6Z-431-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 122 Uncharacterized protein MG284 homolog. FT /FTId=PRO_0000210511. SQ SEQUENCE 122 AA; 14611 MW; E569B47AA6617158 CRC64; MSFKVKNQSK HLYSLMTKFK RSQLILKHQS NNFASELWNE EDIIRSKQFI ELIEDTLLHL KKDTVDFIYD IFIYGKKPCD ISYSNSTYYK KLNKAANSFF DHFVWEAPIY KTKELKNDNS HS // ID Y407_MYCPN Reviewed; 879 AA. AC P75377; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized protein MPN_407; GN OrderedLocusNames=MPN_407; ORFNames=F11_orf879, MP431; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96079.1; -; Genomic_DNA. DR PIR; S73757; S73757. DR RefSeq; NP_110095.1; NC_000912.1. DR RefSeq; WP_010874763.1; NC_000912.1. DR ProteinModelPortal; P75377; -. DR IntAct; P75377; 1. DR EnsemblBacteria; AAB96079; AAB96079; MPN_407. DR GeneID; 877367; -. DR KEGG; mpn:MPN407; -. DR PATRIC; 20022206; VBIMycPne110_0440. DR OMA; TEIFWAN; -. DR OrthoDB; EOG6J74Z6; -. DR BioCyc; MPNE272634:GJ6Z-436-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1110; -; 2. DR InterPro; IPR013830; SGNH_hydro. DR Pfam; PF13472; Lipase_GDSL_2; 1. DR SUPFAM; SSF52266; SSF52266; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 879 Uncharacterized protein MPN_407. FT /FTId=PRO_0000210672. FT TRANSMEM 14 34 Helical. {ECO:0000255}. SQ SEQUENCE 879 AA; 101087 MW; 3C06732BE18B72D4 CRC64; MKKRTKYRYW LNSLAFFGCG VSVGAFFTLF LMGTQSDVSP LFVKNINIQL PSSTHQQKIE PLNLPTNISK TEIASWGSEF QSKVLDFYAR DGEEHDNKIR YQLPSLSFAW TGGKELVSDF ARLHGARNFV AYFDQYWRFW SNPNWPAGQV DRVDVLCEWN SDKQTISDIN FSDQFVFASA RFEGKIANFG FAGQTMKDIN ESFQERVLSI YKPRTLVYLT SQADAERVDY YEEFVNNLTA LIKKQVGEKA EKDNFFILQL HWKTNDSAFN EKLSVLNFVA LATVKQLTDQ NRNFASKIKV VDHFEGDFVP SDWLSGNYLS EDKVSLSLQG EFAIGKQLAQ VLKATGAEPL PVEVTEPSLE AIPINEETQF DVKNYYSFGH YHDTNVINDR IDFDDPNYNL ETDFFNNAKA NLVTTSNPFT VTWKTKTKEL EIESTEVNPN GLQYQLSFAS DFNARDIKKR PTSYLRWNGT ITNKQIDISL YWKYIHKALD IKENEPLNYL LQITRTDGQG SYQVINGWIN KEKDNTPTIF DFLKDKTQAN WLFIGDSMTH GVGTDGYSSA PQLLEQSLKN DFGRYRDVVI NSAINGSNTS LELYMQNHRF KQYKNIDVYV LNLGTNDINQ LAQGVYTVEQ YKHNLTQILD LLHTQSPQAH VVLANIAPSS LLRSSEKNWK TFNDFLEGIP KDSNYSSFVH LLDQKSLFLQ LAKVSGIDIN ENKLFNTDFL KKSFYFADKF SHLSVNGNVE YMRNILTTVG FDWQNSAFAS LGYLSFGYLK KPATVVELPE VTVDDQTGVL DIKQSVPPKL KVNKQGFEPV FITFTNTNNN EQVTVVLNNW SQWETHKTDF APWLKCKHWN IDVKQIRRVK TTFRDQENAN FFELIESKQ // ID Y412_MYCPN Reviewed; 278 AA. AC Q9EXD5; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MPN_412; GN OrderedLocusNames=MPN_412; ORFNames=A05_orf278, MP426.2; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAG34749.1; -; Genomic_DNA. DR RefSeq; NP_110100.1; NC_000912.1. DR RefSeq; WP_010874768.1; NC_000912.1. DR EnsemblBacteria; AAG34749; AAG34749; MPN_412. DR GeneID; 877310; -. DR KEGG; mpn:MPN412; -. DR PATRIC; 20022220; VBIMycPne110_0447. DR OMA; DAQKDDQ; -. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-441-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF12378; CytadhesinP1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 278 Uncharacterized protein MPN_412. FT /FTId=PRO_0000210673. SQ SEQUENCE 278 AA; 30631 MW; E27C42961F7387B3 CRC64; MFGLKVKDAQ KDDQKSSEYL SGEAGSQAGG STQGTSTTTQ RRGSSNENKV KVLQVAMKKK SDSEDNGQIE LETNNLANAP IKRGSNNNQQ VQLKADDFGT TSSSESGQSG TQGSTPSNPG PWTPWLTTEQ IHNDPAKFAA SILILYDAPY ARNRTAIDRV DHLDPKVMTA NYPPSWRTPK WNHHGLWDWK ARDVLLQTTG FFNPRRHPEW FDGGQTVADN EKTGFDVDNS ENTKQGFQKE ADSDKSAPIA LPFEAYFANI GNLTWFGQAL LVFGICLS // ID Y435_MYCPN Reviewed; 395 AA. AC P75343; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MG306 homolog; GN OrderedLocusNames=MPN_435; ORFNames=A05_orf395, MP406; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96054.1; -; Genomic_DNA. DR PIR; S73732; S73732. DR RefSeq; NP_110123.1; NC_000912.1. DR RefSeq; WP_010874791.1; NC_000912.1. DR ProteinModelPortal; P75343; -. DR EnsemblBacteria; AAB96054; AAB96054; MPN_435. DR GeneID; 876874; -. DR KEGG; mpn:MPN435; -. DR PATRIC; 20022266; VBIMycPne110_0470. DR KO; K07027; -. DR OMA; TFYAESQ; -. DR OrthoDB; EOG6J74S4; -. DR BioCyc; MPNE272634:GJ6Z-464-MONOMER; -. DR Proteomes; UP000000808; 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; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 395 Uncharacterized protein MG306 homolog. FT /FTId=PRO_0000210525. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT TRANSMEM 298 318 Helical. {ECO:0000255}. FT TRANSMEM 348 368 Helical. {ECO:0000255}. SQ SEQUENCE 395 AA; 45633 MW; 9E9C1ABD25B89B16 CRC64; MSTPKSASFF TRKNILAFSF FIAFLVVVSV LVTVFFLDIK TGDVKTIINT INRTNWPWIL LIVLGIVVTL AWNIIINWWV ARRFCFHAPW WEWVLFACVV QFFQIVTPLS LGQDPFRLYW FIKKGMKKQT AVLLVTSTGA FWNLAQALIT WPSFFVLSQN YALLEQNHEG FVSYWFSFAG MIFDVVVAIL FIFIAYSKRM HVLIYSGVNQ FRKWIKRPYL TKEQIYQRFI DKAEFNKLYG LEIKRLGLTI FKLLANILIA VVGYFSVFAV FAIVKKENAT NNVIDQYSTA DIFNITNIAI TASNFIPVPS GEGATQFVMT SFLNAFKSAV GIESQVKQGV FLWRFLSVYI PAILFSLCFI GWVVQVVIEF KHPKPVLPTV NLINHHFWNN KKLHN // ID Y472_MYCPN Reviewed; 293 AA. AC P75312; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=DegV domain-containing protein MG326 homolog; GN OrderedLocusNames=MPN_472; ORFNames=MP369, P01_orf293; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and CC may play a role in lipid transport or fatty acid metabolism. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 DegV domain. {ECO:0000255|PROSITE- CC ProRule:PRU00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96017.1; -; Genomic_DNA. DR PIR; S73695; S73695. DR RefSeq; NP_110160.1; NC_000912.1. DR RefSeq; WP_010874828.1; NC_000912.1. DR ProteinModelPortal; P75312; -. DR IntAct; P75312; 1. DR EnsemblBacteria; AAB96017; AAB96017; MPN_472. DR GeneID; 877184; -. DR KEGG; mpn:MPN472; -. DR PATRIC; 20022366; VBIMycPne110_0510. DR OMA; PEKGETW; -. DR OrthoDB; EOG6HB9NH; -. DR BioCyc; MPNE272634:GJ6Z-513-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR InterPro; IPR003797; DegV. DR Pfam; PF02645; DegV; 1. DR TIGRFAMs; TIGR00762; DegV; 1. DR PROSITE; PS51482; DEGV; 1. PE 3: Inferred from homology; KW Complete proteome; Lipid-binding; Reference proteome. FT CHAIN 1 293 DegV domain-containing protein MG326 FT homolog. FT /FTId=PRO_0000209774. FT DOMAIN 3 289 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 62 62 Fatty acid. {ECO:0000250}. FT BINDING 94 94 Fatty acid. {ECO:0000250}. SQ SEQUENCE 293 AA; 32779 MW; E3A278F4A07E8C5C CRC64; MKTAIITDST ASIKEGEIQD VYVLPLQVII NGQDTYRDGK DIDYDRVYQL LKEHPQGLNI STSLPRQADL IELIEAIKDK YDRFVFLPLS KGLSGTYDMI VQAVKPLSTP KKEFVVLETS DIAISLKWLV QEVKALTDTN CPTKAIAEVV DQHKQSIFTA VTVKNLVQLR KGGRISGLKK IIATLLRVKP IIFFDKGVNT LSGKAFTFVQ ALEKIFTFVK SKFGDNFKIK RIGFCNAFTP VKAKEVKALI LDFLHTNKIT LQREIESSFI TSAIIAHTGI DAFSISLLLD KNK // ID Y474_MYCPN Reviewed; 1033 AA. AC P75310; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MG328 homolog; GN OrderedLocusNames=MPN_474; ORFNames=MP367, P01_orf1033; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96015.1; -; Genomic_DNA. DR PIR; S73693; S73693. DR RefSeq; NP_110162.1; NC_000912.1. DR RefSeq; WP_010874830.1; NC_000912.1. DR ProteinModelPortal; P75310; -. DR IntAct; P75310; 1. DR EnsemblBacteria; AAB96015; AAB96015; MPN_474. DR GeneID; 877396; -. DR KEGG; mpn:MPN474; -. DR PATRIC; 20022370; VBIMycPne110_0512. DR OMA; LMASETQ; -. DR OrthoDB; EOG6N3CNZ; -. DR BioCyc; MPNE272634:GJ6Z-515-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 1033 Uncharacterized protein MG328 homolog. FT /FTId=PRO_0000210544. SQ SEQUENCE 1033 AA; 118078 MW; B32A330BEA4869BA CRC64; MEFLEQEGQE VLTKEIKAGF CEITPSSITE QTTKPQLDET QLVDEYVHTK ELETTPIPIS FATKEVLFEE VFNTPSTQQV DESVLVNEYI ELTQQIKNAS EQVSSNHTHK FSVATEPAAT KAVSETMLLD DYVEMVEQDV QAQTALPQAA LDPTVSLTFS SPIDSNAILV YPEMKVPHVF DTVAPTTTTV PLDQTQLLDE LVEVPVLTHT VTPAPLQPKA APTNFALDQT QLVDELVTVP LTHTLVNESA PVTPVVVTSP AAEHSFSITT VDKANLTNAL SQTVVIKPAE DSAHQSAVLD KEIATKQAQL QQLQAQIELR QAQLETPPVT YMGVEEYKLL PVQDVVPVQP TVSFEMTLLQ EQLDKALKHN AALQIQLEEQ LAKPLQYDQS PVLQERIELL QNQNTNLTQE LNELQQKLFK SQNNSLLLAR LEEENRTLKQ HLQNNLPEAN QLNFVLEKQL EQLQQDKHSL TLQIEQYKFD SKKHQEQLAL IPSLRSEINS LETEVISLKQ TNQRLSLIER ENNFLKTEIK QLRETKLNDE NTKYRNLLKQ YELMRADSDA KLKELEHEQH LAHQHHQEQL AQLQRHNEAL VKELDQVKAT NFELGLAAQG FEQQKVVLEQ KNSSLLASLQ AAEENVQALG ITNSELQNQL NVLEFTHKEK TAFDSKTLTL TKQQLEQTQF DLSLTQEQLA TFKQQNQSLT DKLMASETQL NHLQQSDENL TQLQTQHELL QESYNKLQDE ANHTQQQFHQ AQNELDAAHQ QLALFKQNNE ELTDKCSNIQ NELHDLNRVK TNWENLNTEH NLLQDKYAQQ KEQMQHEHSN LAQIQAEHEL LQESYNKVKA ELNEIQITNL NEANAQYQDL LSAYELLQSN HNKLKQELQV LNQVNLEKQQ LAQKLHNTHQ SLSQTHAELT QLQAAYNNLQ ATPPVSDELL EQFNQVQLEK QRLLQQNLAL VHELQYFNEL NSSQTHEIKT KQDETVKEVI IVEKEIPVPP EKKPRLKKRD IVIENKEDAL GKLSKKERIQ AYAERLAKIN GKQ // ID Y477_MYCPN Reviewed; 209 AA. AC P75307; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MG331 homolog; GN OrderedLocusNames=MPN_477; ORFNames=MP364, P01_orf209; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96012.1; -; Genomic_DNA. DR PIR; S73690; S73690. DR RefSeq; NP_110165.1; NC_000912.1. DR RefSeq; WP_010874833.1; NC_000912.1. DR EnsemblBacteria; AAB96012; AAB96012; MPN_477. DR GeneID; 877401; -. DR KEGG; mpn:MPN477; -. DR PATRIC; 20022378; VBIMycPne110_0516. DR OMA; EANEKQW; -. DR OrthoDB; EOG6X1121; -. DR BioCyc; MPNE272634:GJ6Z-518-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 209 Uncharacterized protein MG331 homolog. FT /FTId=PRO_0000210546. FT TRANSMEM 183 203 Helical. {ECO:0000255}. SQ SEQUENCE 209 AA; 24014 MW; 5C18C6A6A0ECCCC5 CRC64; MGRLEKFRFY RQNDDNNTTV QKALLKAQKQ VASWKVELDE LSPKILSHYQ PFSELSANPV KRKSEPNQVL QSLQTLINNF QTSDFQAIAT QADALWLQIK HHDSATGYES WITDDRGMDK IDNLKRFFED NEQQFIQQTQ TFVVQLGNYN KALMALTNEK VSFTTTDLSQ PLASSYNPLF KRILLSLLVF FISSLVGLVV LLTLLFTSL // ID Y517_MYCPN Reviewed; 166 AA. AC P75270; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 70. DE RecName: Full=Uncharacterized protein MG342 homolog; GN OrderedLocusNames=MPN_517; ORFNames=G12_orf166a, MP325; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95973.1; -; Genomic_DNA. DR PIR; S73651; S73651. DR RefSeq; NP_110205.1; NC_000912.1. DR RefSeq; WP_010874873.1; NC_000912.1. DR ProteinModelPortal; P75270; -. DR IntAct; P75270; 1. DR EnsemblBacteria; AAB95973; AAB95973; MPN_517. DR GeneID; 876915; -. DR KEGG; mpn:MPN517; -. DR PATRIC; 20022488; VBIMycPne110_0571. DR OMA; PEINGYM; -. DR OrthoDB; EOG6SNDXM; -. DR BioCyc; MPNE272634:GJ6Z-558-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 166 Uncharacterized protein MG342 homolog. FT /FTId=PRO_0000210550. FT NP_BIND 117 124 ATP. {ECO:0000255}. SQ SEQUENCE 166 AA; 18869 MW; F42411A935A85401 CRC64; MSTKPLILLL ANSKNSINRK FAKALEQQLN AELIELVDYQ VDFYCEDLEK DHFPEKIKSL VRKLHDHKTL IFVTPEHNGF VPAFAKNTID WMTRDTQYGK NQFLKELDGI ICCVTPAAKS GGKTVLELLT KFFSFSGLNV KGAVLVNGYH DGFDFQPFIT DVQKLI // ID Y526_MYCPN Reviewed; 328 AA. AC P75252; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MG350 homolog; GN OrderedLocusNames=MPN_526; ORFNames=G12_orf328b, MP316; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75539:dnaB; NbExp=3; IntAct=EBI-2259783, EBI-2259786; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95964.1; -; Genomic_DNA. DR PIR; S73642; S73642. DR RefSeq; NP_110214.1; NC_000912.1. DR RefSeq; WP_010874882.1; NC_000912.1. DR IntAct; P75252; 6. DR EnsemblBacteria; AAB95964; AAB95964; MPN_526. DR GeneID; 877176; -. DR KEGG; mpn:MPN526; -. DR PATRIC; 20022520; VBIMycPne110_0585. DR OMA; DLLMINI; -. DR OrthoDB; EOG6PZXKW; -. DR BioCyc; MPNE272634:GJ6Z-569-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 328 Uncharacterized protein MG350 homolog. FT /FTId=PRO_0000210556. SQ SEQUENCE 328 AA; 39392 MW; 38C15138D689CBA7 CRC64; MENTNAKTQP AINELDKTTV QDTIKNYEQQ LQKELNEEQL KAFKKRFKYL KLTKREVIEK ESRELLLQAF RDFENCEKIK GNHCPNKGNA HLNIFREPPF WTKSNKKVLG KLIGIKMSCA KSIDKEDIFK LRYSNFIIYK PNWFKYADEF PQINQLPINK FQEESFEEIR NDLSELYENE KNHKENISFF NLQKVNFNHE GAKLLLCDFV ERGVKTALLY CEEFVSRFDR AYWKVDDYLD LINEANVIIF VSLGEESFVS KNYILFLTRL FDIINSKRKD VYFFSTEYNE KNGLIQAFQK SIHFKAKWVN SFFEQLNYFF EMKREEIK // ID Y559_MYCPN Reviewed; 235 AA. AC P75219; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MG381 homolog; GN OrderedLocusNames=MPN_559; ORFNames=H03_orf235, MP283; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95931.1; -; Genomic_DNA. DR PIR; S73609; S73609. DR RefSeq; NP_110248.1; NC_000912.1. DR RefSeq; WP_010874916.1; NC_000912.1. DR IntAct; P75219; 1. DR EnsemblBacteria; AAB95931; AAB95931; MPN_559. DR GeneID; 877278; -. DR KEGG; mpn:MPN559; -. DR PATRIC; 20022595; VBIMycPne110_0621. DR OMA; VQHHKKL; -. DR OrthoDB; EOG6D5G9X; -. DR BioCyc; MPNE272634:GJ6Z-604-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 235 Uncharacterized protein MG381 homolog. FT /FTId=PRO_0000210583. SQ SEQUENCE 235 AA; 26761 MW; 032202285D244A0B CRC64; MASASKSWLP WRKMFKLGWA SFVDPELAKT AFLEFAKQFY VTSSAGAILF DLKKSQGLDQ LQAIEKTRKV IITEQFANQT GKWILFDKEN TKRINSLAQE HITPLIKRIL RLADFKNVLI NVQHHKKLQK CLLWEINGLI CLVESLQFME NPTAIMEWFQ GLKKHCPNVA VVTISGQHKP VIEPSLTEYK AVFGSSLLSF HLDATTINNS HLVRQILEQI KIKATLKSNS KVAKS // ID Y586_MYCPN Reviewed; 347 AA. AC P75194; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 16-SEP-2015, entry version 78. DE RecName: Full=Uncharacterized protein MPN_586; GN OrderedLocusNames=MPN_586; ORFNames=D02_orf347, MP256; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-347. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95904.1; -; Genomic_DNA. DR EMBL; Z32671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S73582; S73582. DR RefSeq; NP_110275.1; NC_000912.1. DR RefSeq; WP_010874943.1; NC_000912.1. DR IntAct; P75194; 1. DR EnsemblBacteria; AAB95904; AAB95904; MPN_586. DR GeneID; 876813; -. DR KEGG; mpn:MPN586; -. DR PATRIC; 20022653; VBIMycPne110_0649. DR BioCyc; MPNE272634:GJ6Z-632-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR009003; Peptidase_S1_PA. DR Pfam; PF00949; Peptidase_S7; 1. DR SUPFAM; SSF50494; SSF50494; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 347 Uncharacterized protein MPN_586. FT /FTId=PRO_0000210734. SQ SEQUENCE 347 AA; 40216 MW; 2C457C1401861B88 CRC64; MRQTIYLTVN LMQNWVERWI LDWANILTWK TLCHQTKIGL PNGAQAFVSA QTSTIPKTAF TAHDFVDYTL PQEQKGKEQK EQQWMKNSQT KDTDVHPYAD FAVLEILLFP DSSTDRKIFN HFIQPAIRAY KQLGDSLNIF ANQTLDQPKH NRYYLLGYPF LRNKAASLFL NQTEQRKEHM DKTTQILHEK PFVVLTDPAK PTLIRNKGAN FTGNTWTSNY DLSKKSGLYH KFLGKKYQIY GKSIVISDLN LSSGSSGSLL LNDRKQIVGI YFGVDGPKDE LGFSQLLRWQ AKNNDEEKDS VAYDLIFGNK NTTKYYAQFA KEHKTHLYEQ IDRSNDQQFT FVKNQKC // ID Y589_MYCPN Reviewed; 157 AA. AC Q50338; P75192; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MPN_589; GN OrderedLocusNames=MPN_589; ORFNames=D02_orf157L, MP253; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U43738; AAC43667.1; -; Genomic_DNA. DR EMBL; U00089; AAB95901.1; -; Genomic_DNA. DR PIR; S62855; S62855. DR RefSeq; NP_110278.1; NC_000912.1. DR RefSeq; WP_010874946.1; NC_000912.1. DR EnsemblBacteria; AAB95901; AAB95901; MPN_589. DR GeneID; 877385; -. DR KEGG; mpn:MPN589; -. DR PATRIC; 20022659; VBIMycPne110_0652. DR BioCyc; MPNE272634:GJ6Z-635-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF00949; Peptidase_S7; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Uncharacterized protein MPN_589. FT /FTId=PRO_0000210735. SQ SEQUENCE 157 AA; 17607 MW; 1B0871A99428D262 CRC64; MGYPTLWTDD AKLFEWTKTE QRFNHDDFYG SMPTLTKNLR QGQPVAGSKV HTDYSNGFLN EYSLNQGIVD FGTFKSAITD YHGYEYKNHG YGLALTDTDL LGGSSGSLVF NQDKKISSIY SAATESDSVG YAQLLPVPKD VNGVSLVKYS YDLILWW // ID Y612_MYCPN Reviewed; 997 AA. AC P75183; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MG414 homolog; GN OrderedLocusNames=MPN_612; ORFNames=C12_orf997, MP230; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG414/MG415 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; U00089; AAB95878.1; -; Genomic_DNA. DR PIR; S73556; S73556. DR RefSeq; NP_110301.1; NC_000912.1. DR RefSeq; WP_010874969.1; NC_000912.1. DR IntAct; P75183; 1. DR PRIDE; P75183; -. DR EnsemblBacteria; AAB95878; AAB95878; MPN_612. DR GeneID; 877134; -. DR KEGG; mpn:MPN612; -. DR PATRIC; 20022707; VBIMycPne110_0676. DR OMA; VDGYESE; -. DR OrthoDB; EOG6W19D7; -. DR BioCyc; MPNE272634:GJ6Z-658-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 997 Uncharacterized protein MG414 homolog. FT /FTId=PRO_0000210599. SQ SEQUENCE 997 AA; 117141 MW; B8E903709A6FCBB6 CRC64; MRSYHYLPLL GFVAFPTLLA NASLDKNLVD SSLYISNSAH HNQGFTVGIK LKDSYFRKDF NFENPLIYKP NNKTTFGWNY STLWTQLADG YYDRYNQLLR ENNFNWYNNI YYIKDVNLGI ESSYTSSLAW NKTFSYPGVR NSFKSDIHDL QYFHFHNDSK SGFGPSRIND PWYPQHDKYV TLSAGRTAEE AKNAGWSIPY NLETQRLFSP VWNRNKDFKW INVFFGFMNR SLSVKSPNIN DIVQNAKWIK QGKNGNYFII FNAYAITQND GFFEDRPNNI FIATLWNNWW LESTPIYIYR VFWEVELIKT PRVFEQDNVQ WNEPVLPKET WVFSIDNKQA NAYWSSSNGF KDKVIKDRKI MEAFTRNRQV TQSILNMGKN VVVKPLTDDE EQSLFSNKWD IFKYTPIIPV NAQRFGVDFY VEQHNADLKP PISFSQLSRL WLSQLQFDPN SVVDTLSKTF NEKDLSQKDQ LQIMFKKEFT QAIAQISKLN EEIDLATDKA TALQKFDSLK SKDSNVNFAS LQYLYDLLGM EPTNKEHLIF IRNLPEMLQT IFARAKLLAK VKIGDTLQEI TLLKNNVNVF DIKTWEKYLT PQQHASNEYT INFLSLDFIV DGYESENLHF QVVDQLFGAV KNLPTINKIP EGYQYKFKYR SNFSNQQFKE KDFSVPLHKA IKSFSVGELK QRMEKLNDFE KQQIVFVIKN SFAGVDKTVL DVDANSLTFV EDPRQYKLDL GNMNENKGFF YVLADIHNSN ELFKLGSTID PEIIKGQIYF VKQNQIKPNT RTYLFKINTR KLLLDKQKLW FKPHLETQTV SFMFDEFEIG KLDIETSNIQ LIDDYEFEFQ SDFSLQDEQV LLEKLNIVLS QMNLHVETKN ARLNPVNKMA YLTVLKNNQK FNLEFHVDRY TSQLSIQAML GSQRLFAINY DLKLSQNKQM LYLINKDGLE KSVWFNIKND SQTKLAQQLA RFLKENNFQF RQKPVFDFHT QNKAFALEKL DNKDDTD // ID Y626_MYCPN Reviewed; 172 AA. AC P75169; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MG428 homolog; GN OrderedLocusNames=MPN_626; ORFNames=C12_orf172, MP216; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95864.1; -; Genomic_DNA. DR PIR; S73542; S73542. DR RefSeq; NP_110315.1; NC_000912.1. DR RefSeq; WP_010874983.1; NC_000912.1. DR ProteinModelPortal; P75169; -. DR EnsemblBacteria; AAB95864; AAB95864; MPN_626. DR GeneID; 877327; -. DR KEGG; mpn:MPN626; -. DR PATRIC; 20022735; VBIMycPne110_0690. DR OMA; ANFIKSS; -. DR OrthoDB; EOG6HB9QP; -. DR BioCyc; MPNE272634:GJ6Z-672-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; 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 Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF88659; SSF88659; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 172 Uncharacterized protein MG428 homolog. FT /FTId=PRO_0000210609. SQ SEQUENCE 172 AA; 20473 MW; 93F6430F3BF8C4AB CRC64; MKLQIFNTKL GLLAAKIYWK SWRHLGLSED EIVSIALHAE HDSKKRYDPK YGLSFETYLK LNGANFIKSS YRSLMNKVDD WIGFKDMKTL EEQNTVSYTP ENYLRSVEFR EMVHLAFKKA KNEDERQVFA LYVKGYKNLE IAKKLNLTTR RVRYLISIFK DHIKVLTKRY GY // ID Y635_MYCPN Reviewed; 352 AA. AC P75162; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 59. DE RecName: Full=Uncharacterized protein MPN_635; GN OrderedLocusNames=MPN_635; ORFNames=E30_orf352, MP207; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_633 (in the N-terminal section), CC and M.pneumoniae MPN_634 (in the C-terminal section). 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; U00089; AAB95855.1; -; Genomic_DNA. DR PIR; S73533; S73533. DR RefSeq; NP_110324.1; NC_000912.1. DR RefSeq; WP_010874992.1; NC_000912.1. DR IntAct; P75162; 1. DR EnsemblBacteria; AAB95855; AAB95855; MPN_635. DR GeneID; 877004; -. DR KEGG; mpn:MPN635; -. DR PATRIC; 20022751; VBIMycPne110_0698. DR BioCyc; MPNE272634:GJ6Z-681-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 352 Uncharacterized protein MPN_635. FT /FTId=PRO_0000210702. SQ SEQUENCE 352 AA; 41243 MW; F92D6BFFFC4DC9ED CRC64; MEVDPAEQIE KAGTLITIEG LKKDDYDKAI VNFLALREDL QLLAASPKGD VYRNTSGNGA EIFLNGMKIA TDEDFLFSYH IKEPNKKLQR SLNRENKNLP RDCYRENIIT ILKSNINNRT QTLIDELIDS RDQYDNGEWS FIDVKKLIGL NTNRNILWAD SSSKNIEKLI YSLYGMDTKK YEILALNSLQ YRSMENDDRL KKQTLMHVSE KLKQQRIEEE AEKIKVKEQK PRKRFEEEDL PIEDLNPIER EGWDWAMEKA RELCGFIRGW EKLYEEYQFV LMEKNHKYVG LCYTDQKIIK LSRGILKDEY SLLNTLVHEI CHATTNGRDG TKKFERGLTD AFHPLFKLGQ SK // ID Y643_MYCPN Reviewed; 274 AA. AC P75154; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MG440 homolog 2; DE Flags: Precursor; GN OrderedLocusNames=MPN_643; ORFNames=E09_orf302, MP199; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95847.1; 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; U00089; AAB95847.1; ALT_INIT; Genomic_DNA. DR PIR; S73525; S73525. DR RefSeq; NP_110332.1; NC_000912.1. DR RefSeq; WP_010875000.1; NC_000912.1. DR IntAct; P75154; 1. DR EnsemblBacteria; AAB95847; AAB95847; MPN_643. DR GeneID; 877148; -. DR KEGG; mpn:MPN643; -. DR PATRIC; 20022767; VBIMycPne110_0706. DR OMA; KINAKGN; -. DR OrthoDB; EOG62K24M; -. DR BioCyc; MPNE272634:GJ6Z-689-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 274 Uncharacterized lipoprotein MG440 homolog FT 2. FT /FTId=PRO_0000014051. FT LIPID 25 25 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 25 25 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 274 AA; 30675 MW; EA3F5A3AD0046F32 CRC64; MKKKIWNKTS LGALFMLFGT ALTACSNSGF EANLTSLNQL RTSASKNTNL TQNKADLVTA LKSAFENNPE GTTRVLLDAW KFTLLDAQIL EKQDFSKFSK SFGSGRSIED VEPSAGVRGL RLVERYTQDT ANIINNVIKL DKQKVEAFSI QYKDPKNFRV QVKINAKGNY KKDTVKTYLS QVGLSDGDLN DTGTLEAEII YTYMPPAASF FSASKFDKLT RAINFNTNLR IQIIGKDSVM TKLLQQSSFV KQLADQKFQD QSINLLPYVL YSIL // ID Y648_MYCPN Reviewed; 136 AA. AC P75149; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MG441 homolog; GN OrderedLocusNames=MPN_648; ORFNames=E09_orf136, MP194; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95842.1; -; Genomic_DNA. DR PIR; S73520; S73520. DR RefSeq; NP_110337.1; NC_000912.1. DR RefSeq; WP_010875005.1; NC_000912.1. DR EnsemblBacteria; AAB95842; AAB95842; MPN_648. DR GeneID; 877003; -. DR KEGG; mpn:MPN648; -. DR PATRIC; 20022777; VBIMycPne110_0711. DR OMA; LIANIHF; -. DR OrthoDB; EOG6MH5PP; -. DR BioCyc; MPNE272634:GJ6Z-694-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 136 Uncharacterized protein MG441 homolog. FT /FTId=PRO_0000210613. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 136 AA; 16157 MW; D4A8362D014F27B7 CRC64; MKSQFKANVL AILLVSLFLI NGLVFLSKTL FKLFNFRVTH SLNNYYTFNL LIKAWRSIKN DFSSLNNFVF FIERQVHNFI GLLIEQPSIE EDNQPEVIEE TPKLEIVVVI EKEVINSKLS DYFCFFKYRS LFFELR // ID Y650_MYCPN Reviewed; 101 AA. AC P75147; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 74. DE RecName: Full=Uncharacterized lipoprotein MPN_650; DE Flags: Precursor; GN OrderedLocusNames=MPN_650; ORFNames=E09_orf101, MP192; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95840.1; -; Genomic_DNA. DR PIR; S73518; S73518. DR RefSeq; NP_110339.1; NC_000912.1. DR RefSeq; WP_010875007.1; NC_000912.1. DR IntAct; P75147; 2. DR EnsemblBacteria; AAB95840; AAB95840; MPN_650. DR GeneID; 876995; -. DR KEGG; mpn:MPN650; -. DR PATRIC; 20022781; VBIMycPne110_0713. DR OrthoDB; EOG6QRW94; -. DR BioCyc; MPNE272634:GJ6Z-696-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 101 Uncharacterized lipoprotein MPN_650. FT /FTId=PRO_0000014063. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 101 AA; 11183 MW; C71F0B9EF197573D CRC64; MKFKYLSTPL LFSALLFSAC SSVNVGANLK SLIKETTDQD LDLSESVSTS EGKKNLISSL KKSYETNPSK TASVLLNAWK QSVENGQIES SETNWTNWKF P // ID Y655_MYCPN Reviewed; 204 AA. AC P75136; Q50351; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=UPF0134 protein MPN_655; GN OrderedLocusNames=MPN_655; ORFNames=E09_orf204o, MP187; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-188. RC STRAIN=ATCC 29342 / M129; RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x; RA Proft T., Herrmann R.; RT "Identification and characterization of hitherto unknown Mycoplasma RT pneumoniae proteins."; RL Mol. Microbiol. 13:337-348(1994). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95835.1; -; Genomic_DNA. DR EMBL; Z32652; CAA83573.1; -; Genomic_DNA. DR PIR; S73513; S73513. DR RefSeq; NP_110344.1; NC_000912.1. DR RefSeq; WP_010875012.1; NC_000912.1. DR ProteinModelPortal; P75136; -. DR EnsemblBacteria; AAB95835; AAB95835; MPN_655. DR GeneID; 877039; -. DR KEGG; mpn:MPN655; -. DR PATRIC; 20022795; VBIMycPne110_0720. DR OMA; RRNKIEL; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-701-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 204 UPF0134 protein MPN_655. FT /FTId=PRO_0000221613. FT CONFLICT 124 126 Missing (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 204 AA; 23787 MW; 2E0FC9C7D59E45F8 CRC64; MSNNNKYFTI TKKQYKKMRR NKIELLFNVK VLKKKNGRQK FKILHEVENK PKIPIKIIED QPESPKPLKP PKPPKPPKGP DNPEEPDSPE EPKETDQPGG PDNPNAGNKK MPTPEEYVTR KEFNEFKDSN NQRLTKIENK VDKLEVKVDK LAEIVQTQGE EIKELKVEQK AQSETLQLIL KTLQKMNDRL DRMETRLDKI DSPK // ID Y675_MYCPN Reviewed; 101 AA. AC P75117; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=UPF0134 protein MPN_675; GN OrderedLocusNames=MPN_675; ORFNames=K05_orf101a, MP167; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95815.1; -; Genomic_DNA. DR PIR; S73493; S73493. DR RefSeq; NP_110364.1; NC_000912.1. DR RefSeq; WP_010875032.1; NC_000912.1. DR ProteinModelPortal; P75117; -. DR EnsemblBacteria; AAB95815; AAB95815; MPN_675. DR GeneID; 877031; -. DR KEGG; mpn:MPN675; -. DR PATRIC; 20022841; VBIMycPne110_0743. DR OMA; GFRIQGE; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-721-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 101 UPF0134 protein MPN_675. FT /FTId=PRO_0000221614. SQ SEQUENCE 101 AA; 11939 MW; 63F5D19ED3566F8B CRC64; MGFYGNLNHM EKGKSGYVTH KQLDKKLEVF KQELLVEFDQ RYVTKAEFKE FQIEVREGFR IQGEAMNARM DRFESLVLKS LESINNTLID FGKRIDKLES K // ID Y272_MYCPN Reviewed; 93 AA. AC Q9EXD2; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MPN_272; GN OrderedLocusNames=MPN_272; ORFNames=A65_orf94, MP562.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34755.1; -; Genomic_DNA. DR RefSeq; NP_109960.1; NC_000912.1. DR RefSeq; WP_010874629.1; NC_000912.1. DR EnsemblBacteria; AAG34755; AAG34755; MPN_272. DR GeneID; 876865; -. DR KEGG; mpn:MPN272; -. DR PATRIC; 20021871; VBIMycPne110_0292. DR OMA; ITTNFEV; -. DR BioCyc; MPNE272634:GJ6Z-279-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein MPN_272. FT /FTId=PRO_0000210657. FT TRANSMEM 68 88 Helical. {ECO:0000255}. SQ SEQUENCE 93 AA; 10622 MW; 2076AA2C28BF2D98 CRC64; MNRPTPNFEA IDKKISAFVT NHDNLLDKLL KQQTELLTSE ITTNFEVTQQ IQEEVAKKTK QHSKNYKWLV TVVLANGVVS LFLLGGLIYL FSK // ID Y275_MYCPN Reviewed; 100 AA. AC P75502; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG134 homolog; GN OrderedLocusNames=MPN_275; ORFNames=A65_orf100, MP560; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96208.1; -; Genomic_DNA. DR PIR; S73886; S73886. DR RefSeq; NP_109963.1; NC_000912.1. DR RefSeq; WP_010874632.1; NC_000912.1. DR ProteinModelPortal; P75502; -. DR IntAct; P75502; 1. DR EnsemblBacteria; AAB96208; AAB96208; MPN_275. DR GeneID; 876875; -. DR KEGG; mpn:MPN275; -. DR PATRIC; 20021877; VBIMycPne110_0295. DR KO; K09747; -. DR OMA; MDINKEL; -. DR OrthoDB; EOG6DVJWP; -. DR BioCyc; MPNE272634:GJ6Z-282-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.30.1310.10; -; 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MG134 homolog. FT /FTId=PRO_0000210437. SQ SEQUENCE 100 AA; 11479 MW; 9D9F62971E7205CD CRC64; MSFKKITEMM RQAERQSKQK ALDFEQKLFE YSYKNAAIKI IIFGNLTIKS ITIDPALIDP EDKVTLEEMI TEAVNEAVGD VKAKYDQLME EAMPQMPGLF // ID Y284_MYCPN Reviewed; 794 AA. AC P75493; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized lipoprotein MPN_284; DE Flags: Precursor; GN OrderedLocusNames=MPN_284; ORFNames=A65_orf794, MP551; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; U00089; AAB96199.1; -; Genomic_DNA. DR PIR; S73877; S73877. DR RefSeq; NP_109972.1; NC_000912.1. DR RefSeq; WP_010874641.1; NC_000912.1. DR IntAct; P75493; 1. DR EnsemblBacteria; AAB96199; AAB96199; MPN_284. DR GeneID; 877107; -. DR KEGG; mpn:MPN284; -. DR PATRIC; 20021899; VBIMycPne110_0306. DR OMA; GNINIPA; -. DR BioCyc; MPNE272634:GJ6Z-291-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 794 Uncharacterized lipoprotein MPN_284. FT /FTId=PRO_0000018730. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 794 AA; 87167 MW; A2AD1AF9E5DAE7F6 CRC64; MKLKYGTIIF SGLLGVSAIL AACGARGKFD QVDDGKIVLA SSLTSKGAAN ALQTIVKKYN EVKNIDDYPI EIIQIAGGYD GGRGNLQTKL SVKDKNSFYN LILNYPDVVS VLGRVGMELP FDKVRTDKLS PRFLDFNKRI SAISKQGIYG IPVSLSTEVL VLNGPVLHYI LSSAKGSSGK TQVSQTSSGS NQQKTLQKPL KIDTSDSSTS SLWTQIENAA KNNGKKANNS KSNRRSTDQS TQTHNDQGDA SESDKKIKES WGDYEEVDGG LKGFTFKASI FDNWHDLLDF STRAAKSFKK IKDNNTKKGT DIQGILGVDS SANSLFTSVF AAGNGDYDNF FYKVANGRAD FSNFKNRGSS FQNLQSVFND YKGLIDQNGL FVNKGGSYSS NFQKFHQLAY SISSTSGFYY SFAGNSAKRL KFGDNSFIEY PQYTVPIKAP SKNGDGNSTN SNSDLLGTFT LSSVKKSTDK SKSDSQQNQG KKVEGTPNQG KKAEGAQNQG KKENNSTTIE IYKNKIPDGK NAGKDAILIK DNNLIKQLED AAKKNGAESN QKQGGESNVQ KEQIIGYTTT GNVREDGNHI FRVDKINDEQ YDRKIIVGVT VETLEQSSTL QSEEAIVLAA PGKYKSTDKK KVTITQGPNI IGIHANEKEN AETQKFVDWF LNTEVDWPAK ENSSNKQDQQ NSTKKQTAAE FFVESASYIL PLKEIFENKE KKENTSNSDK NKSSSQRKNT YAEKALELFQ QISKDEIVSY SDPSDFRSGK FRDGIGSNFN AAVSSKADFN KFVKGFIATL GSEI // ID Y295_MYCPN Reviewed; 220 AA. AC P75482; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MG210.1 homolog; GN OrderedLocusNames=MPN_295; ORFNames=H10_orf220L, MP540; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96188.1; -; Genomic_DNA. DR PIR; S73866; S73866. DR RefSeq; NP_109983.1; NC_000912.1. DR RefSeq; WP_010874652.1; NC_000912.1. DR IntAct; P75482; 1. DR EnsemblBacteria; AAB96188; AAB96188; MPN_295. DR GeneID; 876832; -. DR KEGG; mpn:MPN295; -. DR PATRIC; 20021925; VBIMycPne110_0319. DR OMA; WQIFLED; -. DR OrthoDB; EOG6GTZJH; -. DR BioCyc; MPNE272634:GJ6Z-302-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 220 Uncharacterized protein MG210.1 homolog. FT /FTId=PRO_0000210457. SQ SEQUENCE 220 AA; 25700 MW; 59259B626998CBFD CRC64; MNNTKNKSDW QLFLEDYRFY HEKEFDWITY LNHCLNSYPD FDILKFIRKY GPECEKSFLS LQSKTKADVY GVFTKQIKAG SVNEVLAQKL VQLDALRTNY LIGALYSTNK TQKKLFKQSW KNAKKQGYTK QEWLMTLVGL PFEKGEYHKQ LYAHSRQEIL DLVEAVKKLY LRPEKDDKLE FADSSKVSES KSIKVTNAVT LPSDDLDKEL FEFSGEGGDE // ID Y326_MYCPN Reviewed; 100 AA. AC P75459; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG233 homolog; GN OrderedLocusNames=MPN_326; ORFNames=F10_orf100a, MP510; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YsxB. {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; U00089; AAB96158.1; -; Genomic_DNA. DR PIR; S73836; S73836. DR RefSeq; NP_110014.1; NC_000912.1. DR RefSeq; WP_010874682.1; NC_000912.1. DR ProteinModelPortal; P75459; -. DR EnsemblBacteria; AAB96158; AAB96158; MPN_326. DR GeneID; 876952; -. DR KEGG; mpn:MPN326; -. DR PATRIC; 20022006; VBIMycPne110_0350. DR OMA; MITITFY; -. DR OrthoDB; EOG64V2GR; -. DR BioCyc; MPNE272634:GJ6Z-343-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007422; Peptidase_C108. DR Pfam; PF04327; Peptidase_C108; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 100 Uncharacterized protein MG233 homolog. FT /FTId=PRO_0000210472. FT TRANSMEM 26 42 Helical. {ECO:0000255}. SQ SEQUENCE 100 AA; 10879 MW; FDDEFEF0B0A8F63D CRC64; MIKLTVSHHK LTASGHALFA KKGQDIVCAA VSGIIFGALP WFETNSIAVQ EDATVPSLSL ELVQPTAKLI TGLSVVIMQL KTLAHSYPQF ISFEDQRKDE // ID Y336_MYCPN Reviewed; 344 AA. AC P75442; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein MG240 homolog; GN OrderedLocusNames=MPN_336; ORFNames=F10_orf291, MP500; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP SEQUENCE REVISION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SIMILARITY: Contains 1 HD 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; U00089; AAB96148.2; -; Genomic_DNA. DR PIR; S73826; S73826. DR ProteinModelPortal; P75442; -. DR EnsemblBacteria; AAB96148; AAB96148; MPN_336. DR PATRIC; 20022026; VBIMycPne110_0360. DR OMA; FHDICKE; -. DR OrthoDB; EOG6F55KJ; -. DR BioCyc; MPNE272634:GJ6Z-353-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.3210.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00244; NaMN_adenylyltr; 1. DR InterPro; IPR005249; CHP00488. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR005248; NAMN_adtrnsfrase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00482; TIGR00482; 1. DR TIGRFAMs; TIGR00488; TIGR00488; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 344 Uncharacterized protein MG240 homolog. FT /FTId=PRO_0000210478. FT DOMAIN 193 304 HD. SQ SEQUENCE 344 AA; 39341 MW; 2910A628DECEDA19 CRC64; MIFGGAFDPL HQAHIYIAKR AVQAIKAQKL YFVPTAKAFF KSPIKASNQA RLAMLRVALK ALPQMAVSNF DIKAQNGFSF NTVQHFKQRF PNAELYFLIG SDKLSELAKW HNIEQLQKLC RFVCYERFGY PIDEQLVQQF NVRLLGKCPL DLASSEMFGS HKFRQIPAKV LHYIHQHNIY LKTILQTLLD EPRMQHCLRV GQLAKTLAVA NKLDGKTAYT AGAYHDLAKQ LPQAQLEKLA KVAGVNDYPS WKVLHSYAGA YILKHWYGLN NSAVFSAIWN HTVPPQKMSQ LDMIIYLADK LEPMRVHEEW AKGIDITALV KLAKKDLKLA YQITLKYVRS LQKN // ID Y349_MYCPN Reviewed; 281 AA. AC P75429; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized protein MG246 homolog; GN OrderedLocusNames=MPN_349; ORFNames=H91_orf281, MP487; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96135.1; -; Genomic_DNA. DR PIR; S73813; S73813. DR RefSeq; NP_110037.1; NC_000912.1. DR RefSeq; WP_010874705.1; NC_000912.1. DR PDB; 1T71; X-ray; 2.10 A; A=1-281. DR PDBsum; 1T71; -. DR ProteinModelPortal; P75429; -. DR SMR; P75429; 1-281. DR IntAct; P75429; 1. DR EnsemblBacteria; AAB96135; AAB96135; MPN_349. DR GeneID; 876765; -. DR KEGG; mpn:MPN349; -. DR PATRIC; 20022058; VBIMycPne110_0376. DR KO; K09769; -. DR OMA; PTADAQI; -. DR OrthoDB; EOG68DD2S; -. DR BioCyc; MPNE272634:GJ6Z-366-MONOMER; -. DR EvolutionaryTrace; P75429; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR005235; YmdB-like. DR Pfam; PF13277; YmdB; 1. DR PIRSF; PIRSF004789; DR1281; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00282; TIGR00282; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 281 Uncharacterized protein MG246 homolog. FT /FTId=PRO_0000210486. FT STRAND 6 10 {ECO:0000244|PDB:1T71}. FT STRAND 12 14 {ECO:0000244|PDB:1T71}. FT HELIX 15 23 {ECO:0000244|PDB:1T71}. FT HELIX 26 33 {ECO:0000244|PDB:1T71}. FT STRAND 36 41 {ECO:0000244|PDB:1T71}. FT TURN 45 48 {ECO:0000244|PDB:1T71}. FT HELIX 53 62 {ECO:0000244|PDB:1T71}. FT STRAND 66 68 {ECO:0000244|PDB:1T71}. FT TURN 71 74 {ECO:0000244|PDB:1T71}. FT HELIX 77 79 {ECO:0000244|PDB:1T71}. FT HELIX 80 83 {ECO:0000244|PDB:1T71}. FT TURN 100 103 {ECO:0000244|PDB:1T71}. FT STRAND 104 112 {ECO:0000244|PDB:1T71}. FT STRAND 117 124 {ECO:0000244|PDB:1T71}. FT HELIX 137 145 {ECO:0000244|PDB:1T71}. FT STRAND 151 158 {ECO:0000244|PDB:1T71}. FT HELIX 162 172 {ECO:0000244|PDB:1T71}. FT TURN 173 175 {ECO:0000244|PDB:1T71}. FT STRAND 176 186 {ECO:0000244|PDB:1T71}. FT STRAND 199 202 {ECO:0000244|PDB:1T71}. FT STRAND 206 208 {ECO:0000244|PDB:1T71}. FT HELIX 219 226 {ECO:0000244|PDB:1T71}. FT STRAND 241 249 {ECO:0000244|PDB:1T71}. FT TURN 252 254 {ECO:0000244|PDB:1T71}. FT STRAND 259 267 {ECO:0000244|PDB:1T71}. FT HELIX 270 272 {ECO:0000244|PDB:1T71}. SQ SEQUENCE 281 AA; 31431 MW; 909EE2FC9141C2CD CRC64; MMNSIKFIFL GDVYGKAGRN IIKNNLAQLK SKYQADLVIV NAENTTHGKG LSLKHYEFLK EAGVNYITMG NHTWFQKLDL AVVINKKDLV RPLNLDTSFA FHNLGQGSLV FEFNKAKIRI TNLLGTSVPL PFKTTNPFKV LKELILKRDC DLHIVDFHAE TTSEKNAFCM AFDGYVTTIF GTHTHVPSAD LRITPKGSAY ITDVGMCGPG FGSVIGANPE QSIRLFCAGS REHFEVSKCG AQLNGVFFEV DVNTKKVIKT EAIRIVEDDP RYLKQDYFNL I // ID Y376_MYCPN Reviewed; 1140 AA. AC P75405; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MPN_376; GN OrderedLocusNames=MPN_376; ORFNames=A19_orf1140, MP460; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_375 (in the N-terminal section), CC M.pneumoniae MPN_374 (in the central section) and M.pneumoniae CC MPN_373 (in the C-terminal section). {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; U00089; AAB96108.1; -; Genomic_DNA. DR PIR; S73786; S73786. DR RefSeq; NP_110064.1; NC_000912.1. DR RefSeq; WP_010874732.1; NC_000912.1. DR ProteinModelPortal; P75405; -. DR IntAct; P75405; 1. DR EnsemblBacteria; AAB96108; AAB96108; MPN_376. DR GeneID; 876818; -. DR KEGG; mpn:MPN376; -. DR PATRIC; 20022126; VBIMycPne110_0407. DR OMA; ENDEGFL; -. DR OrthoDB; EOG6BS8ND; -. DR BioCyc; MPNE272634:GJ6Z-396-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 1140 Uncharacterized protein MPN_376. FT /FTId=PRO_0000210669. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 1098 1118 Helical. {ECO:0000255}. SQ SEQUENCE 1140 AA; 130384 MW; 8FA9406C57DD8886 CRC64; MKRLQYRFLL FGFALGSFGW FVASSAFTSV VKSNNETLSS DGGVHMRYLK GKGDVLSILK SKSPAITQRF DLKWNNGKKT EVYLNNVNNY ISESLYAQEA LKQIERTAQL SIQNGELPDV KVYTNSGASF GLVGWHTDNG RTWAFRHENK YDKNVHFSWN QTYYKYSNRE RTASNPYYWK WVAWFDLGYA NQRIGLVEND EYHIDKRVPE PTPRKWDKNK PLWGDIRSKI LYSAERLDPD KGIFIWFNQT GFNTKGTKGW ANSGFFTDFW DTNNNPNAFT TNITSEGGNS NWHSPDWGSH TTDTRFFLKL EPYSKLFYKE NGQERSITVS DYIRKAKSTK TNYQWVNKNQ IKTLVRKTRS IDLGLGSAVR QTYTTKSDIA SNQQLKYKLK DSTFSIDTYN NFKLDKLLVP KTNEDATAIK NGVFVKQPTL SFDFNPVLTN AIVNIHNLFA QTLDLKEHLK SDQPYNESDK AAINKVIEQI KNKEVDYIQV ADFIGKLKNW SQNPGSIESK GENTAQWYAD AKREFGLNLN DDVNTWTQLS SLIASYFSKD IFANVKLNGA KERRMKVWDG AKFEFIPIEN TEKQSEQLAN ENRAEIAVSA IGFQDEGGLR DASFINKVAL TPKSSKTKIA NGDASKIEKA ANEISYKYHY RQNFKQASWD KQNSQTKSIV VQSTDLNDER ERFQKDINNY LKVQGISETE IKVNAVHKVD AMLNARKSDD PKLASVQSTA NKYGLNLRSN PYTGQFYVVV DVTNANDLGN QRRANNAKSY FYYIEGLDKG AQSSYLVRFE NKQKLYSLES LAVDSRGLYV KNVSKDAIIQ AKQNQNLYLD THNWNAALKA NLTNAELTLP TASADNSAKL STPNAENDEG FLSENVSGSI LGYVERMTGK KLFLKERVSF NKEDKNNLKL RLTSNFTLDK KGNLEVKDPS VINQIVEEAK GYNVLVSEEK GDDPESDKNI FKITLTTNPE QSTVIKLPYW IVTKKSKTNK DGTVREQKNL VFDFSNLNNF EYNTVVSLLF TDSSFIKNAY APLQTEFRKQ LKTVLEHKYQ APIKTGQLPL LTKVQLANNQ KQIDNFTFDL HKNIFNKEDI NKINWPLIAI TFTGSAALLS TIIASGVVLH RWRKSRKHFW EQMLKARKVK // ID Y377_MYCPN Reviewed; 74 AA. AC Q9EXD3; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Uncharacterized protein MPN_377; GN OrderedLocusNames=MPN_377; ORFNames=A19_orf74, MP459.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SIMILARITY: To U.parvum UU416. {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; U00089; AAG34753.1; -; Genomic_DNA. DR RefSeq; NP_110065.1; NC_000912.1. DR RefSeq; WP_010874733.1; NC_000912.1. DR IntAct; Q9EXD3; 1. DR EnsemblBacteria; AAG34753; AAG34753; MPN_377. DR GeneID; 876815; -. DR KEGG; mpn:MPN377; -. DR PATRIC; 20022130; VBIMycPne110_0408. DR OMA; FEPRTRI; -. DR BioCyc; MPNE272634:GJ6Z-398-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 74 Uncharacterized protein MPN_377. FT /FTId=PRO_0000210670. SQ SEQUENCE 74 AA; 9108 MW; 63B50EDAE707F28E CRC64; MSKDKKNKVE QLEPVDLFER TKLEDTQVLN DVELDDIKKL EELKKELENT FEPRTRIEIK REIKELERKL RRNR // ID Y398_MYCPN Reviewed; 218 AA. AC P75385; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MG279 homolog; GN OrderedLocusNames=MPN_398; ORFNames=F11_orf218, MP440; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96088.1; -; Genomic_DNA. DR PIR; S73766; S73766. DR RefSeq; NP_110086.1; NC_000912.1. DR RefSeq; WP_010874754.1; NC_000912.1. DR EnsemblBacteria; AAB96088; AAB96088; MPN_398. DR GeneID; 877137; -. DR KEGG; mpn:MPN398; -. DR PATRIC; 20022172; VBIMycPne110_0429. DR OMA; REPINNY; -. DR OrthoDB; EOG69SKHS; -. DR BioCyc; MPNE272634:GJ6Z-421-MONOMER; -. DR Proteomes; UP000000808; 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; IPR030940; MG279/MG280. DR TIGRFAMs; TIGR04527; mycoplas_twoTM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 218 Uncharacterized protein MG279 homolog. FT /FTId=PRO_0000210505. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. SQ SEQUENCE 218 AA; 24899 MW; EF19EEC1F5B98C1E CRC64; MFKFLKKLST FLIVLIGILL VGGITAAGYF AFENREPINN YYKEGYNKVK QYNEEIKKVS KSLSSNELVK TLGDVESSIK EGKELTKLLG DSALESSFNQ LEDSLSKVNN FSKGSTFTEV KNTIEKINQY VDEILKRFPN PNENDQFKEY VTNISQIVFY VGVSIIGTFV VSGALLFIFT KRVYGVRVSR FNPQRLLKKH LVLLLQKNQD VYDEVFES // ID Y404_MYCPN Reviewed; 346 AA. AC P75380; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MG285 homolog; GN OrderedLocusNames=MPN_404; ORFNames=F11_orf346, MP434; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96082.1; -; Genomic_DNA. DR PIR; S73760; S73760. DR RefSeq; NP_110092.1; NC_000912.1. DR RefSeq; WP_010874760.1; NC_000912.1. DR IntAct; P75380; 1. DR EnsemblBacteria; AAB96082; AAB96082; MPN_404. DR GeneID; 877206; -. DR KEGG; mpn:MPN404; -. DR PATRIC; 20022198; VBIMycPne110_0437. DR OrthoDB; EOG66TG4V; -. DR BioCyc; MPNE272634:GJ6Z-432-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 346 Uncharacterized protein MG285 homolog. FT /FTId=PRO_0000210513. SQ SEQUENCE 346 AA; 40350 MW; 7D6AC8B1655E4BE1 CRC64; MTILTVRQIQ NNYYTEYYMG PVRNFADKKE VYFDAKVNNI ESKVNKDKAL LHITLALKYD SNFPSNMFQA QFKLGNWSSE KIPLQKAPDK KSDLENKIHY FYATLEVPRT ALIKREINRI SEYIREELTI AFRLNDSSDR YHWSNYNLFD TVAADMYQTV IKETVTFGNM IRLNQLEGEK EGNIQQSELK YGWTMLDYRN MGPLEEVNNL INIKFNQPVK VVSVGVTVSY TAPDGKRQEL KDQAEYQHTL NPNEEFKLNF PRRLSFNRVT KKLDFDPNGS AVFLPQGGFG SYEIKLEANV GNQFYTIVAT NSFEYAHPFD DPKTNDFFLV QYAPVYSLFN FSDLIQ // ID Y411_MYCPN Reviewed; 252 AA. AC P75373; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized lipoprotein MPN_411; DE Flags: Precursor; GN OrderedLocusNames=MPN_411; ORFNames=A05_orf252, MP427; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB96075.1; -; Genomic_DNA. DR PIR; S73753; S73753. DR RefSeq; NP_110099.1; NC_000912.1. DR RefSeq; WP_010874767.1; NC_000912.1. DR EnsemblBacteria; AAB96075; AAB96075; MPN_411. DR GeneID; 877378; -. DR KEGG; mpn:MPN411; -. DR PATRIC; 20022218; VBIMycPne110_0446. DR OMA; ITYSANE; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-440-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 252 Uncharacterized lipoprotein MPN_411. FT /FTId=PRO_0000014058. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 252 AA; 29196 MW; 69707347B3312DCB CRC64; MRKKKFLSRF AFGSLFLLCG TILSACTGIQ ADLRNLIKEA TGKDIDLSKS IKTTDGKKNI ITSSKKSYEV NPKDTTKLLL EAWKQSFEEG KLGIAELAFD QATNPTKNSD FKMERKVEYF NMEYKSFSDF SVNARLSYIF NWYGSYFGEK SFTANNGGKH NFDLFLSIKS HSKKQFTEKS FIVKDENFQD QDKSQQIITE WIQLDLSLIW SLKGQDELSR KSLDKIFLKD YITYSANEKQ INLFTYLQHL IK // ID Y450_MYCPN Reviewed; 314 AA. AC Q50362; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MG315 homolog; GN OrderedLocusNames=MPN_450; ORFNames=H08_orf314, MP391; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L38997; AAA61694.1; -; Genomic_DNA. DR EMBL; U00089; AAB96039.1; -; Genomic_DNA. DR PIR; S73717; S73717. DR RefSeq; NP_110138.1; NC_000912.1. DR RefSeq; WP_010874806.1; NC_000912.1. DR ProteinModelPortal; Q50362; -. DR IntAct; Q50362; 1. DR EnsemblBacteria; AAB96039; AAB96039; MPN_450. DR GeneID; 877048; -. DR KEGG; mpn:MPN450; -. DR PATRIC; 20022298; VBIMycPne110_0486. DR KO; K02340; -. DR OMA; TIHQVIS; -. DR OrthoDB; EOG6CS03S; -. DR BioCyc; MPNE272634:GJ6Z-479-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR030934; Intein_C. DR SUPFAM; SSF48019; SSF48019; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 314 Uncharacterized protein MG315 homolog. FT /FTId=PRO_0000210531. SQ SEQUENCE 314 AA; 35704 MW; 39B00E9553BA5655 CRC64; MGCGACCILW VQSFTMTVVY GADIGLIHQQ LNQLLNPAAC KQVWFQDVNK LYDVVLNQNL FAEDTKPILI HNCSFLEKNN LTKAELHCLK TLKDTDVVVT IYSDSPANAL INDRAITKYA CKPVTAKTIH QVISKAAKTL KLNLNPDLID HLATILPFNL GVIEQELRKL TLLSPAELQD KKMLEAVLCD YQTSQILQLT DAMVRLQTAK ALKLIERLFL PKQLTPPQFL EFLANELLLA LMVKGVKPQA VFQLQWNVNP FRLKAIQSQY RFWSTNQLTA LINAIWQLDI KIKRNDGLAI HLLKHFVLRF FAQK // ID Y460_MYCPN Reviewed; 565 AA. AC P75323; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized cation transporter MG322 homolog; GN OrderedLocusNames=MPN_460; ORFNames=H08_orf565, MP381; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TrkH potassium transport 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; U00089; AAB96029.1; -; Genomic_DNA. DR PIR; S73707; S73707. DR RefSeq; NP_110148.1; NC_000912.1. DR RefSeq; WP_010874816.1; NC_000912.1. DR EnsemblBacteria; AAB96029; AAB96029; MPN_460. DR GeneID; 877065; -. DR KEGG; mpn:MPN460; -. DR PATRIC; 20022340; VBIMycPne110_0497. DR OMA; TTNAGFD; -. DR OrthoDB; EOG6HTNT6; -. DR BioCyc; MPNE272634:GJ6Z-499-MONOMER; -. DR Proteomes; UP000000808; 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:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003445; Cat_transpt. DR Pfam; PF02386; TrkH; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 565 Uncharacterized cation transporter MG322 FT homolog. FT /FTId=PRO_0000070482. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 262 282 Helical. {ECO:0000255}. FT TRANSMEM 315 335 Helical. {ECO:0000255}. FT TRANSMEM 364 384 Helical. {ECO:0000255}. FT TRANSMEM 393 413 Helical. {ECO:0000255}. FT TRANSMEM 461 481 Helical. {ECO:0000255}. FT TRANSMEM 526 546 Helical. {ECO:0000255}. SQ SEQUENCE 565 AA; 62498 MW; 069B3144A3B49E2E CRC64; MTAAHKQKAK LLAWLKLILW GDSISQRIFH FYIYCILLGA VLLFLPFALK TDYQKVISYE VDLQGHTISK QTASYGFLDA LFLAVSAFSD TGLSTTVVSE TYSVFGQTVL AILLQLGGIG FVVIAFLVWR LFKLHKKGKY SFYEKLMLQS ERGGSKLGTT SEMIVVSVLF LFMVELLYGF LYTILFYFIP AFESASVFQS SGKVSNQLKA LIVDSTKRLP VVHNLNLAFQ YGFFHSLSAV NNAGIDLLGA NSFAPYRTNW GIVIQWLAIS QIIFGGIGYP VLFDAYEAIK KRRLYGKYYK HQFSLFTKLA VLTNLIVTAW CFLMLLMVEF IVITSLTNTI AHLNVEKAYL VEGLKNKSNQ ELQSLIFGPI PAASRVMQLW FGVISSRSAG FSVFPWSAES DIIKGIMVIA MFIGGSPSST AGGIRTTTLA VIFLTLKAKF RGQKEVKVFK RSIDGQTVIN AFLVAVFGLV SVVLIAILLP LSMQQPLSFV DSLFETTSAF GTVGLSSGAT KIMALEPTRN LFNYLTLGLL MIMGQVGVSS SVLTFVKKHP QGNSFSYPRE DVKVG // ID Y484_MYCPN Reviewed; 103 AA. AC P75301; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0134 protein MPN_484; GN OrderedLocusNames=MPN_484; ORFNames=MP358, P02_orf103b; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96006.1; -; Genomic_DNA. DR PIR; S73684; S73684. DR RefSeq; NP_110172.1; NC_000912.1. DR RefSeq; WP_010874840.1; NC_000912.1. DR ProteinModelPortal; P75301; -. DR EnsemblBacteria; AAB96006; AAB96006; MPN_484. DR GeneID; 876760; -. DR KEGG; mpn:MPN484; -. DR PATRIC; 20022394; VBIMycPne110_0524. DR OMA; IQTQGET; -. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-525-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 103 UPF0134 protein MPN_484. FT /FTId=PRO_0000221609. SQ SEQUENCE 103 AA; 11936 MW; 0766A83FAE7F12F9 CRC64; MGFYGNLNHM EKRKSGYVTQ KQFNDFKNSN NQRLIKIENT LVSQGEQISQ LIKVSILQGE QINKLTETVE KQGEQIQTQG ETLKLILETL QVINKRLDRL ESK // ID Y485_MYCPN Reviewed; 316 AA. AC P75300; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MPN_485; GN OrderedLocusNames=MPN_485; ORFNames=MP357, P02_orf316; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96005.1; -; Genomic_DNA. DR PIR; S73683; S73683. DR EnsemblBacteria; AAB96005; AAB96005; MPN_485. DR PATRIC; 20022396; VBIMycPne110_0525. DR OMA; NDKHHYL; -. DR BioCyc; MPNE272634:GJ6Z-526-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 316 Uncharacterized protein MPN_485. FT /FTId=PRO_0000210685. SQ SEQUENCE 316 AA; 33653 MW; 3CBBFA8C199F9000 CRC64; MEGKDAVAIR SIVSRAKIAM TDQTPGFKVD PAFVKVKQNN QTDAFYTTQR KLSGGQTNGG SNNSNDKHHY LQDAVRLTSS QAMAAASTGA GSSSGTNVGG SSGGNSVLIP LPRSAALTHT QQQVQQTTST LQTPVYARGD DGTYALAIDG GDYFLANNKR DFTKQADILL YRYLQAKSNN FKENGVEFSL NLLESGSLFQ TWAQTGLTAK LYGALVAMMG SGQGTQVKGS VQGSSRAASV SVQTTQQSRQ QSTDTQESEV VKLAKALLKS SADLAKPFTD NPTFKKALTD IQSEYKDYLA AAGKLSEFKK DLGEVS // ID Y491_MYCPN Reviewed; 474 AA. AC P75295; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MPN_491; GN OrderedLocusNames=MPN_491; ORFNames=MP351, P02_orf474; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95999.1; -; Genomic_DNA. DR PIR; S73677; S73677. DR RefSeq; NP_110179.1; NC_000912.1. DR RefSeq; WP_010874847.1; NC_000912.1. DR ProteinModelPortal; P75295; -. DR EnsemblBacteria; AAB95999; AAB95999; MPN_491. DR GeneID; 877215; -. DR KEGG; mpn:MPN491; -. DR PATRIC; 20022408; VBIMycPne110_0531. DR OMA; TEDNEAW; -. DR OrthoDB; EOG63RGP1; -. DR BioCyc; MPNE272634:GJ6Z-532-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.60.10.10; -; 2. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR SUPFAM; SSF56219; SSF56219; 2. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 474 Uncharacterized protein MPN_491. FT /FTId=PRO_0000210687. FT TRANSMEM 3 23 Helical. {ECO:0000255}. SQ SEQUENCE 474 AA; 52974 MW; 62D0B3E69B485E9D CRC64; MKLTLWLVLG AVGVGAVGTG VGFGTKYFLD HKAKSNVDVA FKQRSLRKQV NVGFWNALNF LGSERSFGNQ NSKVKTKGIA EIINLLKYDI VGLAEIQPST ESTAERFVDQ LNEYADPYTS WSYDLSPVTT SKTASEGQKE RILIVYNSQS VKMEGQGWFY DNPEMDISNY VSDGSSSKTR TPKKTKTSKK KPIKKKSSKS KSSKGSKKQK TTNESESETL ELKLEQRRVT TRSQSKQQKG QEQATDQTDS EGVTTEEGAD NTDTELVETT AETTEQEATT KSTKDTKETK DRTKVDWSRP PYSAEFSTQK GKVVVAFGHF DSPGANTKRG EKIAKMGKGQ GAHEYFEAQT TFKAMDSIKQ HFNNENILFM ADTNIKFGNQ AAAFGESKDY TFLTEDNEAW KSSLGTKSGY ANPYDKIITS NSFKNKVLDQ AETYWNYFDR YLKTKGHNSY LFDLASWGTK PRTISDHAPV GVLF // ID Y504_MYCPN Reviewed; 126 AA. AC P75282; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 68. DE RecName: Full=UPF0134 protein MPN_504; GN OrderedLocusNames=MPN_504; ORFNames=MP338, P02_orf126; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75454:tig; NbExp=1; IntAct=EBI-2260286, EBI-2260094; CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95986.1; -; Genomic_DNA. DR PIR; S73664; S73664. DR RefSeq; NP_110192.1; NC_000912.1. DR RefSeq; WP_010874860.1; NC_000912.1. DR ProteinModelPortal; P75282; -. DR IntAct; P75282; 1. DR EnsemblBacteria; AAB95986; AAB95986; MPN_504. DR GeneID; 877271; -. DR KEGG; mpn:MPN504; -. DR PATRIC; 20022450; VBIMycPne110_0552. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; MPNE272634:GJ6Z-545-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR InterPro; IPR000727; T_SNARE_dom. DR Pfam; PF01519; DUF16; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 126 UPF0134 protein MPN_504. FT /FTId=PRO_0000221611. SQ SEQUENCE 126 AA; 14988 MW; 8DB52D86973A549C CRC64; MKEKISEKEY KALIRKTGKE HFDGEKEEYG DGTVGVWTYE LRKYKLKPPV KVKYVTQEQF QEYKDSNNQR LIKIENKVDK LVEIVQIHGE QIKAQGETLQ LILQTLQKMS DRLDKMEKRI DKLESK // ID Y512_MYCPN Reviewed; 154 AA. AC P75274; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAY-2015, entry version 57. DE RecName: Full=Uncharacterized protein MPN_512; GN OrderedLocusNames=MPN_512; ORFNames=F04_orf154, MP330; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95978.1; -; Genomic_DNA. DR PIR; S73656; S73656. DR RefSeq; NP_110200.1; NC_000912.1. DR RefSeq; WP_010874868.1; NC_000912.1. DR EnsemblBacteria; AAB95978; AAB95978; MPN_512. DR GeneID; 876819; -. DR KEGG; mpn:MPN512; -. DR PATRIC; 20022474; VBIMycPne110_0564. DR BioCyc; MPNE272634:GJ6Z-553-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 154 Uncharacterized protein MPN_512. FT /FTId=PRO_0000215259. SQ SEQUENCE 154 AA; 17574 MW; 48493AB66799236E CRC64; MRYSFVIQWD FETVYTGVNS TTNLAFSVKA MTTNFANLQE LQDSLVLRGQ NLTTQLFWKP TVKRLVLGNN NDLTTVAKAA VGDNLFTTQA NLTKSVLDQT VLKEAESRFE ATVLKPFIEA RQKALAEHQA HQKVLEEQRQ KQLEELKQKQ KEAE // ID Y527_MYCPN Reviewed; 225 AA. AC P75251; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MG350.1 homolog; GN OrderedLocusNames=MPN_527; ORFNames=G12_orf225, MP315; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95963.1; -; Genomic_DNA. DR PIR; S73641; S73641. DR RefSeq; NP_110215.1; NC_000912.1. DR RefSeq; WP_010874883.1; NC_000912.1. DR ProteinModelPortal; P75251; -. DR EnsemblBacteria; AAB95963; AAB95963; MPN_527. DR GeneID; 877189; -. DR KEGG; mpn:MPN527; -. DR PATRIC; 20022524; VBIMycPne110_0586. DR OMA; LITPLYW; -. DR OrthoDB; EOG60SCM1; -. DR BioCyc; MPNE272634:GJ6Z-571-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 225 Uncharacterized protein MG350.1 homolog. FT /FTId=PRO_0000210558. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. SQ SEQUENCE 225 AA; 25952 MW; 25805A37EF18FCBB CRC64; MNGARIAFWP KKEQHQLFNL SFSAMMLALA LIASFVSHFI SIPFLSALKL TIDISSVFLI ACAFFVSYSW ALVITVALSL CSFIWDGNNW IGILTLTIAN FAIVSFTRLY FHIFAQIKLR WLWVFSLATL SNTLLLTTLN GLLITPLYWY WFGYVPTANF VEVAKIYNKT PYFHFFLFGV PNYWGGIFAL YSLFNVIKFT LVSLIGVPVM RAFQKFYWKK AQIVY // ID Y529_MYCPN Reviewed; 109 AA. AC P75249; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MG353 homolog; GN OrderedLocusNames=MPN_529; ORFNames=G12_orf109, MP313; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95961.1; -; Genomic_DNA. DR PIR; S73639; S73639. DR RefSeq; NP_110218.1; NC_000912.1. DR RefSeq; WP_010874886.1; NC_000912.1. DR ProteinModelPortal; P75249; -. DR EnsemblBacteria; AAB95961; AAB95961; MPN_529. DR GeneID; 876723; -. DR KEGG; mpn:MPN529; -. DR PATRIC; 20022533; VBIMycPne110_0590. DR KO; K03530; -. DR OMA; IRNARYQ; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; MPNE272634:GJ6Z-574-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 4.10.520.10; -; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR Pfam; PF00216; Bac_DNA_binding; 1. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein MG353 homolog. FT /FTId=PRO_0000210560. SQ SEQUENCE 109 AA; 12410 MW; 3FF862745F3C5316 CRC64; MEKTTTSSKP LSRSEINKII AVATGVKEAK IKEIFKYLNT LLLNELVSRS VCILPENLGK LRITIRNARI QKDMKTGEMK HIPPKPLVRY SPSKTIKETA AKVRWKYAD // ID Y544_MYCPN Reviewed; 664 AA. AC P75234; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MG366 homolog; GN OrderedLocusNames=MPN_544; ORFNames=G12_orf664, MP298; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95946.1; -; Genomic_DNA. DR PIR; S73624; S73624. DR RefSeq; NP_110233.1; NC_000912.1. DR RefSeq; WP_010874901.1; NC_000912.1. DR IntAct; P75234; 2. DR EnsemblBacteria; AAB95946; AAB95946; MPN_544. DR GeneID; 877411; -. DR KEGG; mpn:MPN544; -. DR PATRIC; 20022565; VBIMycPne110_0606. DR OMA; YANLEED; -. DR OrthoDB; EOG6TN42C; -. DR BioCyc; MPNE272634:GJ6Z-589-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR021301; DUF2779. DR Pfam; PF11074; DUF2779; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 664 Uncharacterized protein MG366 homolog. FT /FTId=PRO_0000210568. SQ SEQUENCE 664 AA; 76770 MW; ADA1E46D56FC2935 CRC64; MLTKAFFLKN FDRSKELIPL SYADVFGAAS QLLKKHHKQV DTEIDVQEDL IEDPVFEIDI LELLNEAPEL LFDSKNPRVK EAQIIIEKAK KDIASYFHLD NILDTDNLGL KATVTEKIQF TEKQIEAAVQ NKKAAIIFKP VFTVNQCLIQ PDAVVVHANG LCEFVVIKAT TNTKRKFILE IIYDFLLFEK LGKYKLVNYY FCIVNYELKN KHNVSFFLNT EIKTAKNSST SKTKEEQVLY GHLPFNDPKK IAYIHSKKSG GVNGFLLVKL VDNIIRSGVT NLEQIISFVF RELNAPSIRS LKQIISEVAK VQLDFWNIID DVKQHQELQD NQITFNYSDA FNSFWNNYLL RNLIKLVFAY KYSEIFRLSG KLAKWDEVVE AYKENKSVKI DGFLYELNQG KMKKTKNPAT SQFNKIHFFL RAWNDKKGIA VGNKFKSVWQ KLKEKKVYFD FETISSAVRV IDKSLPFTQI VTQCSLIVDD NTESDKSKLV CQNLIFDPLT IGIEDFKTVV DALYQKQCDQ YSFVVYNKSF EKNRLLEMAT FINEAPYQQR VQAIIENLFD LADIFGLEND CLAFKQLDGF SSIKKVLPMI DQRFLDASRT VSYQSLKVQK GDVAQELTLA RFLNCLDEQQ WAQTALELKQ YCENDVRAMI AIELFIKDFI TNQL // ID Y611_MYCPN Reviewed; 372 AA. AC P75184; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized lipoprotein MG412 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_611; ORFNames=C12_orf385, MP231; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95879.1; 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; U00089; AAB95879.1; ALT_INIT; Genomic_DNA. DR PIR; S73557; S73557. DR RefSeq; NP_110300.1; NC_000912.1. DR ProteinModelPortal; P75184; -. DR EnsemblBacteria; AAB95879; AAB95879; MPN_611. DR GeneID; 877112; -. DR KEGG; mpn:MPN611; -. DR PATRIC; 20022703; VBIMycPne110_0674. DR KO; K02040; -. DR OMA; CANINLI; -. DR OrthoDB; EOG6HB9P1; -. DR BioCyc; MPNE272634:GJ6Z-657-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR024370; PBP_domain. DR Pfam; PF12849; PBP_like_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 372 Uncharacterized lipoprotein MG412 FT homolog. FT /FTId=PRO_0000014041. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 372 AA; 40977 MW; 608D661025BA662B CRC64; MLRVARLSRL ALLSLTAVIF SGCANINLIS AVGSSSVQPL LSKLSSHYVL NHNDKDNLVE ISVQAGGSSA GVKAITKGLA DIGNVSKNTK SYAEENKQLW MDKKLKTITL GKDAIAVIYK APSEFKGKLV LTKDNLNDLY DLFAGSKSVD INKFVENGQT TKNSNHNLIG FPRTGGAFAS GTAEAFLKFS GLTQTKTLDK DSKEILEGQR NYGPNARPTS ETNIEAFNTF VTTLRQPNLY GMVYLSLGFV NNNMNLIKSE GFEVLKVKYD NNAVTPSSQA VSSNTYKWVR PLNSVVSLLP KQKTLPSIQR FFNWLLFSNN SEIKKIYDDF GVLELTADEK KKMFKTGNAE MSNIANFWVD DYSLNNQTFG AL // ID Y633_MYCPN Reviewed; 247 AA. AC P75164; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 76. DE RecName: Full=Uncharacterized protein MPN_633; GN OrderedLocusNames=MPN_633; ORFNames=C12_orf247, MP209; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_635 N-terminal region. 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; U00089; AAB95857.1; -; Genomic_DNA. DR PIR; S73535; S73535. DR ProteinModelPortal; P75164; -. DR IntAct; P75164; 1. DR EnsemblBacteria; AAB95857; AAB95857; MPN_633. DR PATRIC; 20022749; VBIMycPne110_0697. DR OrthoDB; EOG68H83T; -. DR BioCyc; MPNE272634:GJ6Z-679-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR SUPFAM; SSF55874; SSF55874; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 247 Uncharacterized protein MPN_633. FT /FTId=PRO_0000210700. SQ SEQUENCE 247 AA; 28095 MW; B9C82D8F1B38CEFE CRC64; MRYLDLNIKS ILADWEIADA IRELIANAID EHRLSNTAFP VIELQKGFLN SSLVIKDYGR GIKSNHFIQN ESREKVQSEK TIGKFGIGLK DAIAVLFRHN VKVSFTSSEG TFTPVERMKE GMKDGTKTIQ ITVDETKKID KGTDILISKI SRSDYEKAIA IFLELRTGYQ KLASSKKGDI YRSENGSEIF LNGMKIGTDE NFLFSYDIKE PNKKLQKSLN RERKTLSRDS YRDNIISILK SSINKNT // ID Y634_MYCPN Reviewed; 181 AA. AC P75163; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 55. DE RecName: Full=Uncharacterized protein MPN_634; GN OrderedLocusNames=MPN_634; ORFNames=C12_orf181o, MP208; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_635 C-terminal region. 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; U00089; AAB95856.1; -; Genomic_DNA. DR PIR; S73534; S73534. DR EnsemblBacteria; AAB95856; AAB95856; MPN_634. DR BioCyc; MPNE272634:GJ6Z-680-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 181 Uncharacterized protein MPN_634. FT /FTId=PRO_0000210701. SQ SEQUENCE 181 AA; 21358 MW; 6E22B4BDC60A65D3 CRC64; MQNTNRKILW TSNESSDIAA PAYQTWAQEE GYEIISIGSS QYQSMENDAE FKSYTLNDFG DRFVNEFQTE EVPFHKLTEI EKDNWNWVMA KVKELTRVWS NWKNLYKHYE FSIIKKHPNA EGLHSNGRIQ IVRKILNERS HLFNTIMHEI CHATSFSPDV SQRFEQGLTS AFYPVMKLKP E // ID Y641_MYCPN Reviewed; 276 AA. AC P75156; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized lipoprotein MG440 homolog 3; DE Flags: Precursor; GN OrderedLocusNames=MPN_641; ORFNames=E09_orf276, MP201; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95849.1; -; Genomic_DNA. DR PIR; S73527; S73527. DR RefSeq; NP_110330.1; NC_000912.1. DR RefSeq; WP_010874998.1; NC_000912.1. DR EnsemblBacteria; AAB95849; AAB95849; MPN_641. DR GeneID; 876993; -. DR KEGG; mpn:MPN641; -. DR PATRIC; 20022763; VBIMycPne110_0704. DR OrthoDB; EOG62K24M; -. DR BioCyc; MPNE272634:GJ6Z-687-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 276 Uncharacterized lipoprotein MG440 homolog FT 3. FT /FTId=PRO_0000014052. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 276 AA; 31073 MW; D4EFD093A43DA6C0 CRC64; MNKKRLLPKA SLGALFMLFG TALTACSNSD FQTNLTSLNQ LREGVNQNTS LTQDKKAFVE SLQKAFENNP EGTTKVLLDA WKFTLLDSKI LESKDPSRFV KAFGSGKSNE DVEPNASVKG LRLDKRFEPS TANIINNVIS LNEQKVEAFN IQYKSRTSFK VQVKLNAQGK YQKSQVQSYL QQIGLNDGDL KQESGTLSAD LIFTYTVPES NLFSRKNFDT LMKKINFNTT LKIDMVGKDE IMKKILQSTT FTNNLSSQTF QDQSIDLLPY LLYSIL // ID Y657_MYCPN Reviewed; 401 AA. AC P75134; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MG443 homolog; GN OrderedLocusNames=MPN_657; ORFNames=K05_orf401, MP185; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95833.1; -; Genomic_DNA. DR PIR; S73511; S73511. DR RefSeq; NP_110346.1; NC_000912.1. DR RefSeq; WP_010875014.1; NC_000912.1. DR EnsemblBacteria; AAB95833; AAB95833; MPN_657. DR GeneID; 877009; -. DR KEGG; mpn:MPN657; -. DR PATRIC; 20022799; VBIMycPne110_0722. DR OMA; LVDENHN; -. DR OrthoDB; EOG6XDGRN; -. DR BioCyc; MPNE272634:GJ6Z-703-MONOMER; -. DR Proteomes; UP000000808; 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; IPR019264; DUF2179. DR InterPro; IPR003740; YitT. DR Pfam; PF10035; DUF2179; 1. DR Pfam; PF02588; YitT_membrane; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 401 Uncharacterized protein MG443 homolog. FT /FTId=PRO_0000210617. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TRANSMEM 246 266 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. SQ SEQUENCE 401 AA; 45571 MW; A8F8945C51611253 CRC64; MDWLKRWFTR KDQDKTETTS ASKRAKITSS LLMFSALYEA KKPLKYTIVY ILALVNAFFL LVFIQQTGLY SFGISSLTQG FARLLFVLLK NLEDGQRNLV FNIFYWLFYV IVNIPLIIFS YKKIGKRFTI LSTHYVVASN VFGFIFSIIP GANQLPSMLS AVHHTEFWED AKKAEGVDQS ALFVPFLWND TSQGNVIIST FIYAGIYGFV NGTSLAILYI LGSCAGGADF LTQYFARKKN RSVGPILFYV NTFILIIAIL MGSFVAGSIV LQDIPDYKKS AWQVNLFFSP NLIATFFSVL FTGTVVSHLF PRYNFAEIKV FTDKIEEVRL ALLNDKATHS LSIQETMGGY SLAKKRMIVS VTMYVEIPNL IRIIRKIDKD CLVSITRIRG IDGYIYLRSQ D // ID Y666_MYCPN Reviewed; 251 AA. AC P75125; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MG452 homolog; GN OrderedLocusNames=MPN_666; ORFNames=K05_orf251, MP176; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95824.1; -; Genomic_DNA. DR PIR; S73502; S73502. DR RefSeq; NP_110355.1; NC_000912.1. DR RefSeq; WP_010875023.1; NC_000912.1. DR EnsemblBacteria; AAB95824; AAB95824; MPN_666. DR GeneID; 877029; -. DR KEGG; mpn:MPN666; -. DR PATRIC; 20022817; VBIMycPne110_0731. DR OMA; YSPARSI; -. DR OrthoDB; EOG6CVVDQ; -. DR BioCyc; MPNE272634:GJ6Z-712-MONOMER; -. DR Proteomes; UP000000808; 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; IPR011631; DUF1600. DR Pfam; PF07667; DUF1600; 1. DR PIRSF; PIRSF006834; UCP006834; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 251 Uncharacterized protein MG452 homolog. FT /FTId=PRO_0000210624. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 205 225 Helical. {ECO:0000255}. SQ SEQUENCE 251 AA; 28750 MW; 18A27EEE01CC5838 CRC64; MEQNNCKIRT WFAKLALAQK VFLGVIPLFF ICFVFVIADI VISLQNKGHI IEEIDKFTNQ SNVMLLIYAC WYVSKPKSHY LKNQQFFLSA FAYIIFTFLG YNVILAASQQ AYSDKDAYSL ASSVFLHVLA PIAFLVAGIV KMKTDKDVTF NHFWKSLGYF MIYPLVYGLY LATIPYVRGH YVSDDGKSTT YVVYGEITNT KDNPIVAWPV VICFLFIYFP LSFLAVYALQ CKLLNRPLKA QFKCATNKCP K // ID Y685_MYCPN Reviewed; 284 AA. AC Q50316; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Putative ABC transporter ATP-binding protein MG468.1 homolog; GN OrderedLocusNames=MPN_685; ORFNames=K05_orf284, MP157; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34816; AAC43649.1; -; Genomic_DNA. DR EMBL; U00089; AAB95805.1; -; Genomic_DNA. DR PIR; S62839; S62839. DR RefSeq; NP_110374.1; NC_000912.1. DR RefSeq; WP_010875042.1; NC_000912.1. DR ProteinModelPortal; Q50316; -. DR IntAct; Q50316; 3. DR EnsemblBacteria; AAB95805; AAB95805; MPN_685. DR GeneID; 877042; -. DR KEGG; mpn:MPN685; -. DR PATRIC; 20022859; VBIMycPne110_0752. DR OMA; GVEITAH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-731-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 284 Putative ABC transporter ATP-binding FT protein MG468.1 homolog. FT /FTId=PRO_0000093252. FT DOMAIN 53 284 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 89 96 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 284 AA; 32242 MW; E2275C81CFE295E0 CRC64; MSLNAKNKRS LDYCLQWPDF CQSKKASKLI VKLNKKHPKR RHYKDPEAKH YDVLFKGVCK AVTNGITNQL ICDHIDLKIA PGEFVVILGK SGSGKTSLLS LISALDRPTS GVSFVCGRST ICCNDAQLTS LRNKNVGYIF QQYGLLRDLN VDDNIKLAVP FKKRHNNNLE ELLERLELKE HRNKKITKLS GGQQQRVAIA RALIKEPRIL FGDEPTGAVN VDISKKILQF FVEYNRDKGT TIVLVTHNEK IVELAKRVIK IHDGKIVADY LNQRPKTINE INWV // ID Y312_MYCPN Reviewed; 218 AA. AC P75469; O08090; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MPN_312; GN OrderedLocusNames=MPN_312; ORFNames=F10_orf218, MP524; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=9098066; RA Krause D.C., Proft T., Hedreyda C.T., Hilbert H., Plagens H., RA Herrmann R.; RT "Transposon mutagenesis reinforces the correlation between Mycoplasma RT pneumoniae cytoskeletal protein HMW2 and cytadherence."; RL J. Bacteriol. 179:2668-2677(1997). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96172.1; -; Genomic_DNA. DR EMBL; U59896; AAB52529.1; -; Genomic_DNA. DR PIR; S73850; S73850. DR RefSeq; NP_110000.1; NC_000912.1. DR RefSeq; WP_010874668.1; NC_000912.1. DR EnsemblBacteria; AAB96172; AAB96172; MPN_312. DR GeneID; 877352; -. DR KEGG; mpn:MPN312; -. DR PATRIC; 20021976; VBIMycPne110_0336. DR OMA; ATSEAHD; -. DR BioCyc; MPNE272634:GJ6Z-328-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MPN_312. FT /FTId=PRO_0000210660. SQ SEQUENCE 218 AA; 24208 MW; EF717BA6A4FC752C CRC64; MKDSALTLKR VRIGKFSESM VEERPTLNLF EKVEFNPVPT ALVDQLPTEP LVEATLLEKE AITFVDTYAT SEAHDQIATF VLEQSMETEV VEKEAIETAI VAPAPDLVEE KAVLVEEVLV EPTATEAVTT EENQVSTTSV TKIKTKRSNT KKVTSETLVA SKSVKTKKLI TPNRVSSGNV NITLWQVDKK STNLTKTKTD LFGKKHQFKG PQLISYKK // ID Y319_MYCPN Reviewed; 503 AA. AC P75462; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MG226 homolog; GN OrderedLocusNames=MPN_319; ORFNames=F10_orf503, MP517; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG225. {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; U00089; AAB96165.1; -; Genomic_DNA. DR PIR; S73843; S73843. DR RefSeq; NP_110007.1; NC_000912.1. DR RefSeq; WP_010874675.1; NC_000912.1. DR ProteinModelPortal; P75462; -. DR EnsemblBacteria; AAB96165; AAB96165; MPN_319. DR GeneID; 876937; -. DR KEGG; mpn:MPN319; -. DR PATRIC; 20021990; VBIMycPne110_0342. DR OMA; FFQGWNQ; -. DR OrthoDB; EOG6F55D5; -. DR BioCyc; MPNE272634:GJ6Z-336-MONOMER; -. DR Proteomes; UP000000808; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 503 Uncharacterized protein MG226 homolog. FT /FTId=PRO_0000210470. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 106 126 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 166 186 Helical. {ECO:0000255}. FT TRANSMEM 215 235 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TRANSMEM 301 321 Helical. {ECO:0000255}. FT TRANSMEM 359 379 Helical. {ECO:0000255}. FT TRANSMEM 405 425 Helical. {ECO:0000255}. FT TRANSMEM 443 463 Helical. {ECO:0000255}. FT TRANSMEM 468 488 Helical. {ECO:0000255}. SQ SEQUENCE 503 AA; 54960 MW; 4BC1BFDE036985B2 CRC64; MSHQEQLHKP NRQQFSEKQF IAFAFNYVAG FGFISVVLTM FKLGPFSYLI LGLAALGILG VMLSFSRLSI ICGSKAYGGS YLIAKKALGV KTITARFFTF LSGWNVSLTG PFNGLIVPAV LVLSFADIKA VKDNNGALIG LLVGGFVLFG ALNFISLFGL KMNKNAILFF AIVKWVVVLG GLILGIYLIG TNHGHGFVEN NTLGEHIEDL SFLKVISTTV GMLVAFAGTE DLTAITPDVK SKNIRKCFLL MFGAVTLLYL IGFVIISGIS GLNGYGLDGK EKNEKAINTF GSIYFQAGGK YLGIPLLVIF GLGFLLNSLA SRLGMTITTA RKYVALAQDG FLPSFINEQN KHHEYHKAVW ASNIMTLAVM VLMIIVPFLP NDENPGKQLV MFDAISVLVE VAIELAVLIS LIQYFITYIF FFMILAKKEG SASVSWWEIA SYGVSFAIIT VLLFVNLFPI TAWKNTNTFK LSILAAFFAL GIGFFIHSEI KHKGQLVKSV ECN // ID Y339_MYCPN Reviewed; 224 AA. AC P75439; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MG243 homolog; GN OrderedLocusNames=MPN_339; ORFNames=H91_orf224, MP497; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96145.1; -; Genomic_DNA. DR PIR; S73823; S73823. DR RefSeq; NP_110027.1; NC_000912.1. DR RefSeq; WP_010874695.1; NC_000912.1. DR IntAct; P75439; 1. DR EnsemblBacteria; AAB96145; AAB96145; MPN_339. DR GeneID; 876778; -. DR KEGG; mpn:MPN339; -. DR PATRIC; 20022032; VBIMycPne110_0363. DR OMA; HELFLWV; -. DR OrthoDB; EOG67MF17; -. DR BioCyc; MPNE272634:GJ6Z-356-MONOMER; -. DR Proteomes; UP000000808; 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; IPR010432; RDD. DR Pfam; PF06271; RDD; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 224 Uncharacterized protein MG243 homolog. FT /FTId=PRO_0000210484. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. SQ SEQUENCE 224 AA; 25613 MW; 56ACE3DC715A7845 CRC64; MQVKVIDENS NTTAVLNCAK AKTRALAWLC DTVLLAILLA IIYGISSIFI KEQSSVFLIM TVSQAVLWLT YFVILPGLWK GKTLFRALLG LSLLIFKKRF WNLLVHELFL WVWYSVIFLA LAIYFFVNRD DPKILQAFFD NQNSNLSWIF VKILLSVISV LQLVFVVYFC FSSQKQALQD LLSKSFMVQK AIKVKDCKSE LKSTNTIKTH SDLPGDIDLE QLGD // ID Y355_MYCPN Reviewed; 242 AA. AC P75424; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase MG252 homolog; DE EC=2.1.1.-; GN OrderedLocusNames=MPN_355; ORFNames=H91_orf242a, MP481; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH 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; U00089; AAB96129.1; -; Genomic_DNA. DR PIR; S73807; S73807. DR RefSeq; NP_110043.1; NC_000912.1. DR RefSeq; WP_010874711.1; NC_000912.1. DR ProteinModelPortal; P75424; -. DR EnsemblBacteria; AAB96129; AAB96129; MPN_355. DR GeneID; 876924; -. DR KEGG; mpn:MPN355; -. DR PATRIC; 20022070; VBIMycPne110_0382. DR KO; K03218; -. DR OMA; WIYYASE; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; MPNE272634:GJ6Z-372-MONOMER; -. DR Proteomes; UP000000808; 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; 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; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 242 Uncharacterized tRNA/rRNA FT methyltransferase MG252 homolog. FT /FTId=PRO_0000159834. FT BINDING 198 198 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 218 218 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000250}. FT BINDING 227 227 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 242 AA; 27775 MW; C117F83D8B6AA7A0 CRC64; MKRMQETSFL FGSKAFLEAL DNQLQIKKVN LSDKHQKLLG LIKKRGLRYE MHSSQWFHQQ FRHINHQEFV CVINPNQMLK TIEQLIQITD SKSTSTLVML HEIQDPHNFG AILRTCMAAE VDGIIFKKHN QAPINSTVIR TSMGTVFYQN LVQVTNLSYA ITTLQKHGFW TVATTLDERL KPKDYRQVDF DKRILLVGNE DKGLNALLLK NADLKVKIPM NPKLNSLNVS VAVGIILFGW KS // ID Y374_MYCPN Reviewed; 229 AA. AC P75407; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_374; GN OrderedLocusNames=MPN_374; ORFNames=A19_orf229V, MP462; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_376 central region. {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; U00089; AAB96110.1; -; Genomic_DNA. DR PIR; S73788; S73788. DR RefSeq; NP_110062.1; NC_000912.1. DR RefSeq; WP_010874730.1; NC_000912.1. DR EnsemblBacteria; AAB96110; AAB96110; MPN_374. DR GeneID; 877395; -. DR KEGG; mpn:MPN374; -. DR PATRIC; 20022122; VBIMycPne110_0405. DR OrthoDB; EOG6BS8ND; -. DR BioCyc; MPNE272634:GJ6Z-394-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 229 Uncharacterized protein MPN_374. FT /FTId=PRO_0000210667. SQ SEQUENCE 229 AA; 26513 MW; 11DE39A2ACB2639D CRC64; MKEVIDTNTT GTNFKFENRN YKLQNQSFSF VRYKNFNLDK LLIPKTNANL NSTRNGVLTQ APTLDFVLNP VFVNAITNVY NLSEQVKDLE QRLESKSNES EKAGINSVLT QIKNKQVDYL KVKEYISSLD KDTNKVSTPI NSTGWVKWYQ EANKELGLNL NQEPKDWDQF LKLVASYFSM AIYANVTLGQ KVTKEVKVWD GQNFQFLAIE NNEDQAQCFS KRKQSWNYC // ID Y410_MYCPN Reviewed; 148 AA. AC P75374; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=UPF0134 protein MPN_410; GN OrderedLocusNames=MPN_410; ORFNames=F11_orf148o, MP428; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB96076.1; -; Genomic_DNA. DR PIR; S73754; S73754. DR RefSeq; NP_110098.1; NC_000912.1. DR RefSeq; WP_010874766.1; NC_000912.1. DR ProteinModelPortal; P75374; -. DR EnsemblBacteria; AAB96076; AAB96076; MPN_410. DR GeneID; 877313; -. DR KEGG; mpn:MPN410; -. DR PATRIC; 20022216; VBIMycPne110_0445. DR OrthoDB; EOG6PZX78; -. DR BioCyc; MPNE272634:GJ6Z-439-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 148 UPF0134 protein MPN_410. FT /FTId=PRO_0000221608. SQ SEQUENCE 148 AA; 17391 MW; 01E31C79869ACAAC CRC64; MKEKIPFYNE KEFNEMMKKT KKGTFSGWYI INPENNSVEF SGSFNRQFKL NKPIIPVNTE YVTRKEFNEY KDSNDQRLIK IETTLTAQGE QINKLTQTVE KQGEQIRELQ VEQKAQGEQI KAQGETLKLI LQTLQKMSDR LDKIDPPK // ID Y424_MYCPN Reviewed; 102 AA. AC P75363; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=UPF0122 protein MPN_424; GN OrderedLocusNames=MPN_424; ORFNames=A05_orf102, MP417; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: Might take part in the signal recognition particle (SRP) CC pathway. This is inferred from the conservation of its genetic CC proximity to ftsY/ffh. May be a regulatory protein (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UPF0122 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; U00089; AAB96065.1; -; Genomic_DNA. DR PIR; S73743; S73743. DR RefSeq; NP_110112.1; NC_000912.1. DR RefSeq; WP_010874780.1; NC_000912.1. DR ProteinModelPortal; P75363; -. DR EnsemblBacteria; AAB96065; AAB96065; MPN_424. DR GeneID; 876863; -. DR KEGG; mpn:MPN424; -. DR PATRIC; 20022244; VBIMycPne110_0459. DR KO; K09787; -. DR OMA; FQARTRI; -. DR OrthoDB; EOG6TTVWB; -. DR BioCyc; MPNE272634:GJ6Z-453-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003677; F:DNA binding; 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 Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00245; UPF0122; 1. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR007394; UPF0122. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04297; UPF0122; 1. DR SUPFAM; SSF88659; SSF88659; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 102 UPF0122 protein MPN_424. FT /FTId=PRO_0000211873. SQ SEQUENCE 102 AA; 12478 MW; 950B6906302AB4E0 CRC64; MNQTKLNQRL KQQQLFDIYG ELLTKRQACY FNEYINLDLS MQEIADKYQV KKSSIHQHIK TCNLIFNRFE AKLQLFKKQQ LRLKLYEKIT DPQLREQLIK LR // ID Y427_MYCPN Reviewed; 290 AA. AC P75360; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative phosphatase MPN_427; DE EC=3.1.3.-; GN OrderedLocusNames=MPN_427; ORFNames=A05_orf290, MP414; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-2261609, EBI-2261609; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; U00089; AAB96062.1; -; Genomic_DNA. DR PIR; S73740; S73740. DR RefSeq; NP_110115.1; NC_000912.1. DR RefSeq; WP_010874783.1; NC_000912.1. DR ProteinModelPortal; P75360; -. DR EnsemblBacteria; AAB96062; AAB96062; MPN_427. DR GeneID; 876743; -. DR KEGG; mpn:MPN427; -. DR PATRIC; 20022250; VBIMycPne110_0462. DR KO; K07024; -. DR OMA; PKENIKA; -. DR OrthoDB; EOG6K13W0; -. DR BioCyc; MPNE272634:GJ6Z-456-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 290 Putative phosphatase MPN_427. FT /FTId=PRO_0000054441. FT REGION 53 54 Phosphate binding. {ECO:0000250}. FT ACT_SITE 16 16 Nucleophile. {ECO:0000250}. FT METAL 16 16 Magnesium. {ECO:0000250}. FT METAL 18 18 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 239 239 Magnesium. {ECO:0000250}. FT METAL 240 240 Magnesium. {ECO:0000250}. FT BINDING 17 17 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 216 216 Phosphate. {ECO:0000250}. FT BINDING 242 242 Phosphate. {ECO:0000250}. SQ SEQUENCE 290 AA; 33216 MW; FCA0416EDEEE48CA CRC64; MTKTSKASGL SWFFCDLDGT LLRYQNNQHL IEPTTKRAVA QLVESGANFV VATGRKPSDV RNIYKELGIE QASPYLIANN GAVVWDLKRN SYLNKQTLSL SDFDLIDHIN QTLNQLNHEY GCILYGLNDQ VYFYHIHAPD SQAFKQYFAF YEGEFVQNQY LEIDGLKTEY NLVKAIWFFK EVHQQKAVIA QHFTNQERLV ITSAHSFELV PLNVSKGHAI NLIKQQVKIT DNQIMVLGDS YNDLPMFQHG VVKVTNHLAP DNLKQLATRV YELPASLFVG QALNDYFKFD // ID Y439_MYCPN Reviewed; 237 AA. AC P75339; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized lipoprotein MPN_439; DE Flags: Precursor; GN OrderedLocusNames=MPN_439; ORFNames=H08_orf237, MP402; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor, GPI- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96050.1; -; Genomic_DNA. DR PIR; S73728; S73728. DR EnsemblBacteria; AAB96050; AAB96050; MPN_439. DR PATRIC; 20022276; VBIMycPne110_0475. DR OMA; RKRSSYC; -. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MPNE272634:GJ6Z-468-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 237 Uncharacterized lipoprotein MPN_439. FT /FTId=PRO_0000014059. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 237 AA; 26668 MW; B89C7B454A7C6F53 CRC64; MKSFLRKPKF WLLLLGGLST SSIILSACAT PSNSALQAVF KPTSNQFFNG EHGTIQSALN TALRDPETNK KFVAAPLLKA LEAWYENNQD KNITQFLKDT KTNVDNQYKT VVDKVVSAPR NKSLFVQQDL LDSSGGSEAT WKARKLFEQL ISDFASRVFQ KNYLSYKENG KVSAGPFLYD TISKNSNWQN IVFDAVNFPE TNDDFFAKIQ SEVFDQWAEY TDPTIISSVT LKYSAPN // ID Y441_MYCPN Reviewed; 102 AA. AC P75337; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 51. DE RecName: Full=Uncharacterized protein MPN_441; GN OrderedLocusNames=MPN_441; ORFNames=H08_orf102, MP400; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96048.1; -; Genomic_DNA. DR PIR; S73726; S73726. DR RefSeq; WP_010874797.1; NC_000912.1. DR RefSeq; YP_009121730.1; NC_000912.1. DR IntAct; P75337; 1. DR EnsemblBacteria; AAB96048; AAB96048; MPN_441. DR GeneID; 877073; -. DR KEGG; mpn:MPN441; -. DR BioCyc; MPNE272634:GJ6Z-470-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 102 Uncharacterized protein MPN_441. FT /FTId=PRO_0000210678. SQ SEQUENCE 102 AA; 11012 MW; B0CE5606F539D015 CRC64; MLSTAAKSAA SNWSTMLVAS TTFLVSLVSD KLNGKSITWP LSVPRTYLVR PSFWTPFVWL PSCCCFGFSS IASSPLTSCF QRLLPTFWLP AISSAAAKNG KA // ID Y466_MYCPN Reviewed; 140 AA. AC P75317; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_466; GN OrderedLocusNames=MPN_466; ORFNames=MP375, P01_orf140; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB96023.1; -; Genomic_DNA. DR PIR; S73701; S73701. DR EnsemblBacteria; AAB96023; AAB96023; MPN_466. DR PATRIC; 20022350; VBIMycPne110_0502. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-505-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MPN_466. FT /FTId=PRO_0000210684. SQ SEQUENCE 140 AA; 16218 MW; 1F5FB1483204402F CRC64; MERKIEHFQM TYQSFKDLSV EAKLSYTFNW FGDYSSGGFT AKKGDKHYFD LFLKIKPDAK KSFTIANFKT EEDNSTTIGG KETTRNLEWI EFSASLKFSL KGKDDVSQKS VNKFLSTFAN NTEGYSSNIN LFIYLEYLIK // ID Y500_MYCPN Reviewed; 527 AA. AC P75287; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Putative adhesin P1-like protein MPN_500; GN OrderedLocusNames=MPN_500; ORFNames=MP343, P02_orf527V; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95990.1; -; Genomic_DNA. DR PIR; S73669; S73669. DR RefSeq; NP_110188.1; NC_000912.1. DR RefSeq; WP_010874856.1; NC_000912.1. DR EnsemblBacteria; AAB95990; AAB95990; MPN_500. DR GeneID; 877245; -. DR KEGG; mpn:MPN500; -. DR PATRIC; 20022436; VBIMycPne110_0545. DR OMA; NANDTKF; -. DR BioCyc; MPNE272634:GJ6Z-541-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 527 Putative adhesin P1-like protein MPN_500. FT /FTId=PRO_0000210716. SQ SEQUENCE 527 AA; 55346 MW; 647560CD8087A0F5 CRC64; MDDITAPQTS AGSSSGTSTN TSGSRSFLPT FSNVGVGLKA NVQGTLGGRQ TTTTGNNIPK WATLDQANLQ LWTGAGWRND KTTSGSTGNA NDTKFTSATG SGSGQGSSSG TNTSAGNPDG LQADKVDQNG QVKTSVQEAT SGDNLTNYTN LPPANLTPTA DWPNALSFTN KNNAQRAQLF LRGLLGSIPV LVNKSGQDDN SKFKAEDQKW SYTDLQSDQT KLNLPAYGEV NGLLNPALVE TYFGNTRASG SGSNTTSSPG IGFKIPEQSG TNTTSKAVLI TPGLAWTPQD VGNIVVSGTS FSFQLGGWLV TFTDFIKPRA GYLGLQLTGL DVSEATQREL IWAKRPWAAF RGSWVNRLGR VESVWDFKGV WADQAQLAAQ AATSSTTTTA TGATLPEHPN ALAYQISYTD KDSYKASTQG SGQTNSQNNS PYLHFIKPKK VESTTQLDQG LKNLLDPNQV RTKLRQSFGT DHSTQPQPQS LKTTTPVFGR SSGNLSSVFS GGGAGGGSSG SGQSGVDLSP VERVSGH // ID Y510_MYCPN Reviewed; 458 AA. AC P75276; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_510; GN OrderedLocusNames=MPN_510; ORFNames=MP332, P02_orf458; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95980.1; -; Genomic_DNA. DR PIR; S73658; S73658. DR RefSeq; NP_110198.1; NC_000912.1. DR RefSeq; WP_010874866.1; NC_000912.1. DR EnsemblBacteria; AAB95980; AAB95980; MPN_510. DR GeneID; 876817; -. DR KEGG; mpn:MPN510; -. DR PATRIC; 20022468; VBIMycPne110_0561. DR OMA; KLANWIT; -. DR BioCyc; MPNE272634:GJ6Z-551-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 458 Uncharacterized protein MPN_510. FT /FTId=PRO_0000215257. SQ SEQUENCE 458 AA; 53085 MW; 5FFA80772532241E CRC64; MLTVPKVPEN FFSFFQEDYF PRLTPRGLNI ADNVASLFND YNLNSIDFTG FNLKLLRQND IVLKNKVRYN FALQMGFDTV YAGKNTTILK FSLQAQTINF TSLQELRDSF ENNGNTLSTH LFWKPVVEQL TTDGGNDLTN IAKTAIGESL FNLKVNLTDS IIDQSVLQQA QKSFEDKILD PFHAERVEAK RIHDEEARRL EAERKRIAAE LKAKEDEARR IREEHWAFYQ STRDVKSFKE FWAKRGKNVA DKKQLIEALK LSFQAKQNPT FELLTNAFRN AINWYYNHKK HDEEAKRTAF GSGGISFAQS GLNGIFMPNW LRWELINRAN IQLQLQNVKV RENNFEVNGW GVPVSINWND HNNGINYRAT TPWTYGFEIT MNYKGSYGLK GIYWTLANWG LGGIPPEWSG DMELKFQIDG KLANWITQKQ DYPGSLFQFQ NDKLLFTLHV VQRITVKD // ID Y530_MYCPN Reviewed; 136 AA. AC P75248; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MG354 homolog; GN OrderedLocusNames=MPN_530; ORFNames=G12_orf136, MP312; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95960.1; -; Genomic_DNA. DR PIR; S73638; S73638. DR RefSeq; NP_110219.1; NC_000912.1. DR RefSeq; WP_010874887.1; NC_000912.1. DR ProteinModelPortal; P75248; -. DR SMR; P75248; 1-136. DR EnsemblBacteria; AAB95960; AAB95960; MPN_530. DR GeneID; 876728; -. DR KEGG; mpn:MPN530; -. DR PATRIC; 20022535; VBIMycPne110_0591. DR OMA; ICSTRES; -. DR OrthoDB; EOG64R67M; -. DR BioCyc; MPNE272634:GJ6Z-575-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR015271; DUF1951. DR Pfam; PF09188; DUF1951; 1. DR SUPFAM; SSF110009; SSF110009; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 136 Uncharacterized protein MG354 homolog. FT /FTId=PRO_0000210562. SQ SEQUENCE 136 AA; 15584 MW; 602FC1AD0DA69F94 CRC64; MEPNNLKEEL VSVFEKACSS HKERLDFICS VRESDTFSNV DVPLAPIKTI IEIAKNEENQ TEILKLAIEN IKTLSTVGSG QYIASHFSTH NEVAIIFCIS YFLYHFNFLH DENKKQLLKR AFEAVAEKIA DYLNEN // ID Y548_MYCPN Reviewed; 326 AA. AC P75230; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized RNA pseudouridine synthase MG370 homolog; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase; DE AltName: Full=RNA-uridine isomerase; GN OrderedLocusNames=MPN_548; ORFNames=G12_orf326, MP294; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95942.1; -; Genomic_DNA. DR PIR; S73620; S73620. DR RefSeq; NP_110237.1; NC_000912.1. DR RefSeq; WP_010874905.1; NC_000912.1. DR ProteinModelPortal; P75230; -. DR EnsemblBacteria; AAB95942; AAB95942; MPN_548. DR GeneID; 877406; -. DR KEGG; mpn:MPN548; -. DR PATRIC; 20022573; VBIMycPne110_0610. DR KO; K06179; -. DR OMA; GVFDKPP; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; MPNE272634:GJ6Z-593-MONOMER; -. DR Proteomes; UP000000808; 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 InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; RNA-binding. FT CHAIN 1 326 Uncharacterized RNA pseudouridine FT synthase MG370 homolog. FT /FTId=PRO_0000162742. FT DOMAIN 15 76 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 147 147 {ECO:0000250}. SQ SEQUENCE 326 AA; 37267 MW; D87BED622FD680F3 CRC64; MSTAKFVVPK AVENVRIEKF CLKLLPNIKL SQFFKLLRLG KVLLNNTKAK LGQRVSSGDT IVFQFAIEPY LHNHSEVVDL TQVQDDLQVI FEDEQLIVVD KPAGVVCQPD AKHELFNLAN SLLKHCGYNQ YFKNSLSFIP RFAHRIDRNT CGLVIGAKTN QALQELEAVF RHNLLMKQYQ GLVFGPFNFK GTQKAYWAKD AYQALVTVKA KPFPNAKPIT TIFENSKYLT KLDLSLLTIR LVSGKTHQIR ACLNLLNTQL VGDRKYQLLQ FKNRNRDFKH QALHATNLSF AQLDKQKFPL LANYSQRQFK SQLVPWFASL IKGVSI // ID Y549_MYCPN Reviewed; 325 AA. AC P75229; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MG371 homolog; GN OrderedLocusNames=MPN_549; ORFNames=G12_orf325, MP293; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the mgp1/MG371 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; U00089; AAB95941.1; -; Genomic_DNA. DR PIR; S73619; S73619. DR RefSeq; NP_110238.1; NC_000912.1. DR RefSeq; WP_010874906.1; NC_000912.1. DR ProteinModelPortal; P75229; -. DR IntAct; P75229; 1. DR EnsemblBacteria; AAB95941; AAB95941; MPN_549. DR GeneID; 877409; -. DR KEGG; mpn:MPN549; -. DR PATRIC; 20022575; VBIMycPne110_0611. DR KO; K06881; -. DR OMA; KKRVDFN; -. DR OrthoDB; EOG6FBX0G; -. DR BioCyc; MPNE272634:GJ6Z-594-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 325 Uncharacterized protein MG371 homolog. FT /FTId=PRO_0000210573. SQ SEQUENCE 325 AA; 36767 MW; C685932F94E24474 CRC64; MINIDPHFIH NLTNKLKTFD NFSLYVHVNP DFDAFGAAFA FKAFLAVYFP HKKAYVMGSH NIKADGKDLF PFEAAPIDDA FVKNSLAIIF DTSNQERVLT QKHKLAKETV RIDHHPKTES FADLEWIDPA FSAAAEMVGY LILQMGYELN AEMAAYIYAG IITDTQRFSS SATTPQTFAL TAKLLETGFN RNKVHDAVYL KPLLEHKYFS YVLNKAKITP NGLAYALLKK GTYKQFGVVS PLPMVHALNN IKGVKIWTTC YFNEDIKKWI GSIRSRSIPI NNFAQMFGGG GHKYAAAFVL DDKRQFMKLV EIMDDFLAKQ KHVNS // ID Y554_MYCPN Reviewed; 104 AA. AC P75224; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG376 homolog; GN OrderedLocusNames=MPN_554; ORFNames=G12_orf104, MP288; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95936.1; -; Genomic_DNA. DR PIR; S73614; S73614. DR RefSeq; NP_110243.1; NC_000912.1. DR RefSeq; WP_010874911.1; NC_000912.1. DR PDB; 2HQL; X-ray; 2.00 A; A/B/C/D/E/F=1-104. DR PDBsum; 2HQL; -. DR ProteinModelPortal; P75224; -. DR SMR; P75224; 1-104. DR EnsemblBacteria; AAB95936; AAB95936; MPN_554. DR GeneID; 877308; -. DR KEGG; mpn:MPN554; -. DR PATRIC; 20022585; VBIMycPne110_0616. DR OMA; YVIYAND; -. DR OrthoDB; EOG6K6VCZ; -. DR BioCyc; MPNE272634:GJ6Z-599-MONOMER; -. DR EvolutionaryTrace; P75224; -. DR Proteomes; UP000000808; Chromosome. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR024506; DUF3217. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF11506; DUF3217; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MG376 homolog. FT /FTId=PRO_0000210579. FT STRAND 3 16 {ECO:0000244|PDB:2HQL}. FT STRAND 21 33 {ECO:0000244|PDB:2HQL}. FT STRAND 36 47 {ECO:0000244|PDB:2HQL}. FT HELIX 48 58 {ECO:0000244|PDB:2HQL}. FT STRAND 62 75 {ECO:0000244|PDB:2HQL}. FT TURN 76 79 {ECO:0000244|PDB:2HQL}. FT STRAND 80 90 {ECO:0000244|PDB:2HQL}. SQ SEQUENCE 104 AA; 12470 MW; BAC327512A2A1F9B CRC64; MLNRVFLEGE IESSCWSVKK TGFLVTIKQM RFFGERLFTD YYVIYANGQL AYELEKHTKK YKTISIEGIL RTYLERKSEI WKTTIEIVKI FNPKNEIVID YKEI // ID Y571_MYCPN Reviewed; 660 AA. AC P75207; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Putative ABC transporter ATP-binding MG390 homolog; GN OrderedLocusNames=MPN_571; ORFNames=D02_orf660, MP271; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00362, ECO:0000255|PROSITE- CC ProRule:PRU00434}. CC -!- SIMILARITY: Contains 1 peptidase C39 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00362}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95919.1; -; Genomic_DNA. DR PIR; S73597; S73597. DR RefSeq; NP_110260.1; NC_000912.1. DR RefSeq; WP_010874928.1; NC_000912.1. DR ProteinModelPortal; P75207; -. DR IntAct; P75207; 3. DR EnsemblBacteria; AAB95919; AAB95919; MPN_571. DR GeneID; 877236; -. DR KEGG; mpn:MPN571; -. DR PATRIC; 20022621; VBIMycPne110_0633. DR OMA; NECGICV; -. DR OrthoDB; EOG6H1PW2; -. DR BioCyc; MPNE272634:GJ6Z-617-MONOMER; -. DR Proteomes; UP000000808; 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:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011527; ABC1_TM_dom. 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 SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Protease; Reference proteome; Thiol protease; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 660 Putative ABC transporter ATP-binding FT MG390 homolog. FT /FTId=PRO_0000093248. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 265 285 Helical. {ECO:0000255}. FT TRANSMEM 290 310 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. FT TRANSMEM 402 422 Helical. {ECO:0000255}. FT DOMAIN 6 126 Peptidase C39. {ECO:0000255|PROSITE- FT ProRule:PRU00362}. FT DOMAIN 464 660 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00362, ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 494 501 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00362, ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT ACT_SITE 12 12 {ECO:0000255|PROSITE-ProRule:PRU00362}. SQ SEQUENCE 660 AA; 76015 MW; B2A97A32F7F993A7 CRC64; MKIIYQEQPN ECGICVLGML ANELHEDKYA HDELLEQINL PASGLSFFEL ETYGKKFGLE IASYQLTLEE LKQLEGKYFI VHFPKHFVVV HKKQDNLWEV FDPAKGKYLL NDEELKKQWT GYAATVQKSF KEIPPINKRN FFKHFFDLNL IIFYVFIELI IIGISTLLAT ASKTMIANTV DFGTSVNIVV FVVFFLVLKG LYLLLYALLQ MVRNVLFWKQ YRGYLGWIMQ TLQTKSFVYF SNKSPNQLTE RQFYLKEVLS FFNVHIPNLI ISCTVALIIG TLIGINQMEF LWIAIVQIVV NCAIFLYDFF FTKRITKQAI PQMELQNKVS LQLDGNLRDE QNGKRFNYLM MQLRKALIKN QNISNQKEVN HLASDGVKSF AQQVFDFLIL ALGIIGIIEQ RYTLAFLFYI FSIQALFSAY ATRIIQFGAA VNLYQFCKDK LVTLFEDKVN DCNFKVSWKC PKVINLNNCS ITLNQNLDLA NLNLNLTNGM VISGENGSGK STLLKILTGR GLSYQGQIKL DELDLKDFSA SQLFHNVYYL TGQLTAYNDI TDFGYSEALL NCKNPQVYQL LADTGIHNQI KLSSGQKQIL QLFLLQNLKD KVILLDETLN AIATELKPRV YQLLIKPLTY NNFVLMVEHD LRFVNSEQDL INLSPYLQQT // ID Y575_MYCPN Reviewed; 128 AA. AC P75204; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MPN_575; GN OrderedLocusNames=MPN_575; ORFNames=D02_orf128, MP267; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95915.1; -; Genomic_DNA. DR PIR; S73593; S73593. DR RefSeq; NP_110264.1; NC_000912.1. DR RefSeq; WP_010874932.1; NC_000912.1. DR EnsemblBacteria; AAB95915; AAB95915; MPN_575. DR GeneID; 876795; -. DR KEGG; mpn:MPN575; -. DR PATRIC; 20022629; VBIMycPne110_0637. DR OMA; NIFQIAG; -. DR BioCyc; MPNE272634:GJ6Z-621-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 128 Uncharacterized protein MPN_575. FT /FTId=PRO_0000210694. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. SQ SEQUENCE 128 AA; 13736 MW; 3FF8702F348717A8 CRC64; MLQNLALSFP FITRFFQKQM LGSQNSSGKT PGFNEAEGIT SNIFQIAGGI SLLVILLLII GFLSCLLGGI FLHKHKYAEV GSPAHAKTKN LFVAFFVVGS LLLLVAVVML IAFGVLDASL PLPKENNS // ID Y580_MYCPN Reviewed; 140 AA. AC P75200; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 75. DE RecName: Full=Uncharacterized protein MPN_580; GN OrderedLocusNames=MPN_580; ORFNames=D02_orf140, MP262; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75349:MPN_126; NbExp=1; IntAct=EBI-2260425, EBI-2260422; CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95910.1; -; Genomic_DNA. DR PIR; S73588; S73588. DR RefSeq; NP_110269.1; NC_000912.1. DR RefSeq; WP_010874937.1; NC_000912.1. DR IntAct; P75200; 1. DR EnsemblBacteria; AAB95910; AAB95910; MPN_580. DR GeneID; 877394; -. DR KEGG; mpn:MPN580; -. DR PATRIC; 20022637; VBIMycPne110_0641. DR BioCyc; MPNE272634:GJ6Z-626-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF00949; Peptidase_S7; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MPN_580. FT /FTId=PRO_0000210730. SQ SEQUENCE 140 AA; 16104 MW; 37E646BB8BEF34D6 CRC64; MTAQYYQLDE KFNQQTYEQY GKGLALNDLY IRRGASGSLV FNQDQQISGI FFAVASHSDP KPGEKTLVQL LRLPVDESTT ATVKDNCVPY DLIFGNRNTT HYYTQFAKQH HTHLYEQIQQ SNDQLIKFID RKNVSCSMVS // ID Y582_MYCPN Reviewed; 439 AA. AC P75198; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized lipoprotein MPN_582; DE Flags: Precursor; GN OrderedLocusNames=MPN_582; ORFNames=D02_orf439, MP260; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95908.1; -; Genomic_DNA. DR PIR; S73586; S73586. DR RefSeq; NP_110271.1; NC_000912.1. DR RefSeq; WP_010874939.1; NC_000912.1. DR IntAct; P75198; 1. DR EnsemblBacteria; AAB95908; AAB95908; MPN_582. DR GeneID; 876808; -. DR KEGG; mpn:MPN582; -. DR PATRIC; 20022641; VBIMycPne110_0643. DR OMA; EIDHANY; -. DR OrthoDB; EOG6N9469; -. DR BioCyc; MPNE272634:GJ6Z-628-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 3. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 439 Uncharacterized lipoprotein MPN_582. FT /FTId=PRO_0000018740. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 439 AA; 50357 MW; 1587A9EEEE9D5D29 CRC64; MWVALKRFGF LSGLLALTVL SACSAFRKPD KFEGYYINNI PGSAEIDHAN YDLTFFLGFF NRIEKTEKDK SQIDFGSIHG TGWLIDWKEV DKKDKKANKF TVYLATNLHV IQALKNREDH PPYNQFDINF VRTVDFRIGK YTDVKQFVAP SKLGLPNSTQ AFVAAQPTVL PKTAFIAHDF VNYTLSKDQK NKKQREQQWK VQIKPNKDEV HPYADSAVLE LPLFLNNSSD RQIFDHFIQP AIRAYKQLGD SLNIFAYPTL DQFKHSHYYV LGYPYIAKKL PTLFVNQTGK EKTVPGETAQ IPNDQPFVST INEEGPHLGR IKSDKFNGGT WAWNHDNTKN FPFNRQFRGK EYQMYGKGIG ITNGSLSRGA SGSLVLNNKR QIVAIYFASR ITETQEWGLA QLLRWKPRSV LNEEKDSVAY DLIFGNSNTK KYYAQFAKK // ID Y588_MYCPN Reviewed; 531 AA. AC Q50339; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized lipoprotein MPN_588; DE Flags: Precursor; GN OrderedLocusNames=MPN_588; ORFNames=D02_orf531, MP254; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U43738; AAC43668.1; -; Genomic_DNA. DR EMBL; U00089; AAB95902.1; -; Genomic_DNA. DR PIR; S62796; S62796. DR RefSeq; NP_110277.1; NC_000912.1. DR RefSeq; WP_010874945.1; NC_000912.1. DR EnsemblBacteria; AAB95902; AAB95902; MPN_588. DR GeneID; 876794; -. DR KEGG; mpn:MPN588; -. DR PATRIC; 20022657; VBIMycPne110_0651. DR OMA; TGWLFDW; -. DR OrthoDB; EOG6N9469; -. DR BioCyc; MPNE272634:GJ6Z-634-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 531 Uncharacterized lipoprotein MPN_588. FT /FTId=PRO_0000018743. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 531 AA; 60142 MW; 0A3A089261B3C998 CRC64; MRLQFKLLGF LTLLGTSTIL SACAATQPNF EPNNIEESGP ITPTTPTTDV PKPTAEVVPV NRGFHFQTNK VPSESDVFKH NYDLTFSLNF TNKSNDIYGT GWLFDWKGDE KALGIDGSFV PSITSNIDNS LLKDDQFTVY LATNLHVADA LRNDQDYEPY KKDQNKQDFT ENTKTEFFSL GKYLEGEQLK QYISKEENQS ANQTDKALVS IQASNIPKTA YTATDFVDMN SYSYNNITTS LPGNYADFAV IEVNLNLKNQ RDQQILHDFV KPAIKAYKAL GDTLELFSAK PLNQFIEQNY YLLGYPVINK GNNTANLLLA QQKSFDHNNS DHNQKSQWFT KDQSYINKLD RIPVLTNNYR AYNESTGSQL FANQQNESWL NGVVIQDKGV VNFASFSNFT LKYHEKRFQQ YGYGLMLNDT NFPGGSSGSP LIGKDNKLNS IYFGVLEIYQ SGSLARNDIG MSQILRTPQN DKGSSISKGS YDLIFGDKNT KNYYAKFAKD HQTHLYQKIK ESKDEQFRFV ETQETTNNLG N // ID Y591_MYCPN Reviewed; 353 AA. AC Q50336; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MPN_591; GN OrderedLocusNames=MPN_591; ORFNames=D02_orf353V, MP251; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U43738; AAC43665.1; -; Genomic_DNA. DR EMBL; U00089; AAB95899.1; -; Genomic_DNA. DR PIR; S62854; S62854. DR RefSeq; NP_110280.1; NC_000912.1. DR RefSeq; WP_010874948.1; NC_000912.1. DR EnsemblBacteria; AAB95899; AAB95899; MPN_591. DR GeneID; 877103; -. DR KEGG; mpn:MPN591; -. DR PATRIC; 20022663; VBIMycPne110_0654. DR OrthoDB; EOG6PGK11; -. DR BioCyc; MPNE272634:GJ6Z-637-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF00949; Peptidase_S7; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 353 Uncharacterized protein MPN_591. FT /FTId=PRO_0000210736. SQ SEQUENCE 353 AA; 40492 MW; 8B97C1E1D0535873 CRC64; MANSLRNVND YDPFKYRPSY FDLEAPTESF ALGKFVDAIE VKQMALDAFS ESSMVSIATS QLPKTAYTAT SFIESEYYSF PYLFNDQKYY WDYFDYKIPA ADFAVLELEL DLNNQQDQQI KDHFIDPAIK AYKQLGDSTG LFATKPLTEY QNDTHYLLGY PVVPTDHTQL WECKQGAERF SYGYFYSNMA RLTKNLRQGD PNAGSKTHIE YSNELLDKDS MDQGIVRFST FLGANINYHD YDYRQQGYGL TLTDTNLPGG SSGSLVFNQD KKISSIYSAA TESDSVGYAQ LLRTPRDVNG ISVVSQSYDL IFGDSNTKRY YAMFAKKQQT HLYSEILKST DEQYRYVVDK QFN // ID Y592_MYCPN Reviewed; 521 AA. AC Q50335; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized lipoprotein MPN_592; DE Flags: Precursor; GN OrderedLocusNames=MPN_592; ORFNames=D02_orf521, MP250; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U43738; AAC43664.1; -; Genomic_DNA. DR EMBL; U00089; AAB95898.1; -; Genomic_DNA. DR PIR; S62794; S62794. DR RefSeq; NP_110281.1; NC_000912.1. DR RefSeq; WP_010874949.1; NC_000912.1. DR IntAct; Q50335; 1. DR EnsemblBacteria; AAB95898; AAB95898; MPN_592. DR GeneID; 877053; -. DR KEGG; mpn:MPN592; -. DR PATRIC; 20022665; VBIMycPne110_0655. DR OMA; FRFVEND; -. DR OrthoDB; EOG6PGK11; -. DR BioCyc; MPNE272634:GJ6Z-638-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 4. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 521 Uncharacterized lipoprotein MPN_592. FT /FTId=PRO_0000018745. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 521 AA; 59501 MW; 0E706CDEC8CEEBDA CRC64; MGFKLKGFGF LTLFASQAFL TACSATLTVA NTNHKNESDK FVIFEPQPPL SQTIPKPEAE PVIEPDAVAT PPVQNAEVQI KPDSSKGVYS PGFKFNTNFI PKVNTKYRPG YDLSFALKFG TSWKEAYGTG WLIDWKDVKQ DNKFTAYLAT NLHVADSLRN KDDYKPYNKD GNQKEFLPGD ITTEFSLGKY IDAQTVQKLT PEYQNLKHLN NRNSDALVSI QTSKLPKTAY TATDFIKTAQ YKYNHIVSNT VYELDLFQNA VSYADFAVLE LELNLANNRD QQIFDSFINP AVTAYEKLGN SLGLFSNLQL DQYVDDTHYL LGYPLLKREK TSYWNLPQKG YSSPLYENSN KEVSRITRNI RKDDEIPGSR LVQNQINYLP FAQNDPKGVM DFSKYLNYVF NYHEKQYQHH GYGLLLEDTD FPGGSSGSPL FNQNKQINSI YFAALPSKSY GVSQILRATQ NKDKSKNYDL IFGDSNTKKY YAQFAKEHKT HLYHQILQSN DEQFRFVEND QTVTSQTPFK S // ID Y593_MYCPN Reviewed; 122 AA. AC Q50334; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUN-2015, entry version 70. DE RecName: Full=Uncharacterized protein MPN_593; GN OrderedLocusNames=MPN_593; ORFNames=D02_orf122b, MP249; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43738; AAC43663.1; -; Genomic_DNA. DR EMBL; U00089; AAB95897.1; -; Genomic_DNA. DR PIR; S62853; S62853. DR RefSeq; NP_110282.1; NC_000912.1. DR RefSeq; WP_010874950.1; NC_000912.1. DR IntAct; Q50334; 1. DR EnsemblBacteria; AAB95897; AAB95897; MPN_593. DR GeneID; 877147; -. DR KEGG; mpn:MPN593; -. DR PATRIC; 20022667; VBIMycPne110_0656. DR BioCyc; MPNE272634:GJ6Z-639-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 122 Uncharacterized protein MPN_593. FT /FTId=PRO_0000210697. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. SQ SEQUENCE 122 AA; 14114 MW; 8F2CB5F0EA1A919E CRC64; MNKKESTTTK KQWFKKCSFK KLKAEICNML PTTPHNTKRT LIWVIVFSFI TFLSFIFAYV CFNYAPVSTG FLYFLGAVFL LIGFAFAILS FVAMVKFVAD YFANRFSNTQ LKMDCDCAKT KK // ID Y620_MYCPN Reviewed; 839 AA. AC P75175; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MG422 homolog; GN OrderedLocusNames=MPN_620; ORFNames=C12_orf839, MP222; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95870.1; -; Genomic_DNA. DR PIR; S73548; S73548. DR RefSeq; NP_110309.1; NC_000912.1. DR RefSeq; WP_010874977.1; NC_000912.1. DR EnsemblBacteria; AAB95870; AAB95870; MPN_620. DR GeneID; 877410; -. DR KEGG; mpn:MPN620; -. DR PATRIC; 20022723; VBIMycPne110_0684. DR OMA; WFLGFNA; -. DR OrthoDB; EOG6MM1S3; -. DR BioCyc; MPNE272634:GJ6Z-666-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 839 Uncharacterized protein MG422 homolog. FT /FTId=PRO_0000210603. SQ SEQUENCE 839 AA; 99913 MW; 3E3523E18BCDFECC CRC64; MLKQISTTTK KEPWVNLSLL MVHNSFLDIN YFWTTNLSIH KYGNYLVNNL NKAQWNTLSS VLQLKKAPHS GFLWTDQHNY IPLHRVKTNL CEKIELAAVQ QSHPFHQTIH DFLRQSTCPK KRQRLIEKLQ IPNELRWFLG FNALKKLSQF VVFELDNTNK LTSETLSQFF TTKFVNKVYF NQIQFEYNNF VGLLEDHERD LVEFSTHFFN SFFEQPDHLT KSFFEQYYAL TRQRERLLHN LKVQSYETKH GVNTYFENLQ ITRAQQQANQ LKRAFKKQQR NSVQLINRFM SSLWWSQTKI KFKSIFNFYK TRILEKRIVA KRIQIKIWLL KELKQMRLLN PDLLVSTIAE SERLVEQLMS NIQRLYQQIL QLKPGQSLNW KYQAISFELE KLTKPIVLTH DAVIGFLIKS RLAFLQEYAK GLNRCEQHNK LVNELKQNVL LNQNQYKGEV SQSYSVVNQK AVFKGFIQTV KAALNYTKLK HTLDPFNLMN IVQERCFEQL LTTYEKLDWT KYELNQLYFV CRALWTNLHK QTQHFFTKYQ FITHGVVDFV FNQGRNQTQF ASLKANLNRD WNSPKWKLLV NKTVNKYFEA NLHHPQAYLL LPNRNATTLT EANTTTINQL NLKTQLKQWR AHYHLLLQDI RLIQWLYKKE IKQKQQQIKA LLKNYGTLNK LLNTQISKVN NVVRKTFFVD SEECDLNRLQ ASNKLHFNLL NAMVNVISFC LKKCRQNPKK LNRTANLKML LDNTFKNGIP SWMIFSDLNK INTKQRFKLY LLFKLLLHPQ LVLVDSFVNF NKHTYNFTRG LLIAHQNQQG IAYLFNDPHN NLVKDFFTQT INFETRAKN // ID Y621_MYCPN Reviewed; 561 AA. AC P75174; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Uncharacterized protein MG423 homolog; GN OrderedLocusNames=MPN_621; ORFNames=C12_orf561, MP221; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95869.1; -; Genomic_DNA. DR PIR; S73547; S73547. DR RefSeq; NP_110310.1; NC_000912.1. DR RefSeq; WP_010874978.1; NC_000912.1. DR ProteinModelPortal; P75174; -. DR EnsemblBacteria; AAB95869; AAB95869; MPN_621. DR GeneID; 876764; -. DR KEGG; mpn:MPN621; -. DR PATRIC; 20022725; VBIMycPne110_0685. DR KO; K12574; -. DR OMA; PWLLMKI; -. DR OrthoDB; EOG6PCPSF; -. DR BioCyc; MPNE272634:GJ6Z-667-MONOMER; -. DR Proteomes; UP000000808; 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:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR004613; RNase_J. DR PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00649; MG423; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 561 Uncharacterized protein MG423 homolog. FT /FTId=PRO_0000210605. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. SQ SEQUENCE 561 AA; 63358 MW; 5A3B5588FEABA3DA CRC64; MAKINFFAFG GQDERGKNCF VLEINNDVFI FNVGSLTPTT AVLGVKKIIP DFSWIQENQA RIKGIFIGNP VTENIGSLEF LFHTVGFFPI YTSTIGAVVI KTKIHENKLN IPHDELEIHE LKPLETVKIG HHNITPFKVS SSIPSSFGFA LHTDDGYIVY VDDFIVLNDK NIAFENQLNQ IIPQVANKTL LLITGVGLVG RNTGFTTPKH KSLEQLNRII ASAKGRVFAA CYDSNAYSVM TLAQIARMQN RPFVIYSHSF VHLFNAIVRQ KLFNNTHLNT ISIEEINNST NAIVVLTAPP DKLYAKLFKI GTNEDERVRY RKTDSFIFMI PRIAGYEELE AQILDDVARN EVSYYNLGRE ILSINASDED MKFLVTSLKP KYIIPTSGLY RDFINFTMVM KQAGVEQSQV LIPFNGEVLA INHKQIDNKK RELKLNPKCV DSAGLQEIGA SIMFERDQMS EAGVVTIIIY YDSKKSEFLN EITYSFLGVS LDSNNQVKLK TKMEELIRKQ INDIKDFTTI KRRLGKDTSK ELKVSIKRAV MNLFTKMTAK APLILSTIIS I // ID Y644_MYCPN Reviewed; 283 AA. AC P75153; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 3; DE Flags: Precursor; GN OrderedLocusNames=MPN_644; ORFNames=E09_orf283b, MP198; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95846.1; -; Genomic_DNA. DR PIR; S73524; S73524. DR RefSeq; NP_110333.1; NC_000912.1. DR RefSeq; WP_010875001.1; NC_000912.1. DR IntAct; P75153; 1. DR EnsemblBacteria; AAB95846; AAB95846; MPN_644. DR GeneID; 877001; -. DR KEGG; mpn:MPN644; -. DR PATRIC; 20022769; VBIMycPne110_0707. DR OMA; VTENDFN; -. DR OrthoDB; EOG69PQBN; -. DR BioCyc; MPNE272634:GJ6Z-690-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 283 Uncharacterized lipoprotein MG439 homolog FT 3. FT /FTId=PRO_0000014045. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 283 AA; 31359 MW; F8A6491BF329EBEE CRC64; MNKKRLLFRT PLDALFLLFG TALSACSSTA TNVISSLSSA QKYFDAHKSE LIKKNVINLL KEGYSTDSKA TVNSLFAGWK YTLMDQKILE RNLDASRFTK AFGTNKGKDD VIPSISEKGL FLDETYSGVS QQIAKVLGVQ SQKVTGFSYS WSSTTNFKVV ISFMMQGIVG SGEESNSLIK SFLSSGNNGN VTENDFNNGN ANFDGTFIFT FTPPTDGRRF AFSNFDPITG TINFPANLQI DASTTHEKLN ILMQNNEHVK KIKSRSFTGK SFDLLPFYFY ALL // ID Y645_MYCPN Reviewed; 283 AA. AC P75152; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 2; DE Flags: Precursor; GN OrderedLocusNames=MPN_645; ORFNames=E09_orf290, MP197; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95845.1; -; Genomic_DNA. DR PIR; S73523; S73523. DR RefSeq; NP_110334.1; NC_000912.1. DR RefSeq; WP_010875002.1; NC_000912.1. DR IntAct; P75152; 1. DR EnsemblBacteria; AAB95845; AAB95845; MPN_645. DR GeneID; 877007; -. DR KEGG; mpn:MPN645; -. DR PATRIC; 20022771; VBIMycPne110_0708. DR OMA; NTLMEAN; -. DR OrthoDB; EOG69PQBN; -. DR BioCyc; MPNE272634:GJ6Z-691-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 22 283 Uncharacterized lipoprotein MG439 homolog FT 2. FT /FTId=PRO_0000014044. FT LIPID 22 22 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 22 22 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 283 AA; 31355 MW; 3A55F5BB85E5B005 CRC64; MKLKLKFLLI SLLGSSLLLS ACSSAATQVI SSLSSAQKYF ESSQGELNKK NVIKILKEGY ESDANKAVHA LLAGWKYTLM DQQLLSKEVD SRFIKAFGSG RDKGDVTPSV SEKGLYLNET YTGFSSQIAK VLGVQSQTVK QFNYKWSSNS DFKVQIQISM KGKVGSDSES QQLIKSFLSS DNNGSNQNGG VKETDFNGDS ANFDGFFTFT YTPPTQSRKF GATSFDPLTT KINFPADLQI DVSTTHQKLN TLMEANEQVK QIKSRKFTGK TFDLLPFFYY ALL // ID Y663_MYCPN Reviewed; 234 AA. AC P75128; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MG449 homolog; GN OrderedLocusNames=MPN_663; ORFNames=K05_orf234, MP179; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00209}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95827.1; -; Genomic_DNA. DR PIR; S73505; S73505. DR RefSeq; NP_110352.1; NC_000912.1. DR RefSeq; WP_010875020.1; NC_000912.1. DR ProteinModelPortal; P75128; -. DR IntAct; P75128; 6. DR EnsemblBacteria; AAB95827; AAB95827; MPN_663. DR GeneID; 877008; -. DR KEGG; mpn:MPN663; -. DR PATRIC; 20022811; VBIMycPne110_0728. DR KO; K06878; -. DR OMA; NTHLKRC; -. DR OrthoDB; EOG6CCH1J; -. DR BioCyc; MPNE272634:GJ6Z-709-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002547; tRNA-bd_dom. DR Pfam; PF01588; tRNA_bind; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1 234 Uncharacterized protein MG449 homolog. FT /FTId=PRO_0000210622. FT DOMAIN 103 211 tRNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00209}. SQ SEQUENCE 234 AA; 26155 MW; CBC6FDD2FC0085FD CRC64; MRYGFFDISQ DFITIFCPKK TLKNCMFGLI GSRTQATLRQ EKNQNFSFFV NEANEIAGFN FFDIKKSFRR GLISHHFTAG LNYPSLKLVK KISELLNYDL TPLAKKVPFV VCEVISAIPI PNTHLKRCKV NTGSNKSLDV VCGADNVRVG LKTVLVHVGG VLPDGTIIKK AKIAGYDSMG MLCSEKELNL KPKNQGIIEI KSHIKIGKSF LDVYLNNSEK FSAWVSTKKR VTGN // ID Y684_MYCPN Reviewed; 1882 AA. AC P75109; Q50317; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized ABC transporter permease MG468 homolog; GN OrderedLocusNames=MPN_684; ORFNames=K05_orf1882, MP158; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1848. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95806.1; -; Genomic_DNA. DR EMBL; U34816; AAC43650.1; -; Genomic_DNA. DR PIR; S73484; S73484. DR RefSeq; NP_110373.1; NC_000912.1. DR RefSeq; WP_010875041.1; NC_000912.1. DR IntAct; P75109; 1. DR EnsemblBacteria; AAB95806; AAB95806; MPN_684. DR GeneID; 877036; -. DR KEGG; mpn:MPN684; -. DR PATRIC; 20022857; VBIMycPne110_0751. DR OMA; YPKLANI; -. DR OrthoDB; EOG69GZN1; -. DR BioCyc; MPNE272634:GJ6Z-730-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR Pfam; PF02687; FtsX; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1882 Uncharacterized ABC transporter permease FT MG468 homolog. FT /FTId=PRO_0000210632. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 987 1007 Helical. {ECO:0000255}. FT TRANSMEM 1037 1057 Helical. {ECO:0000255}. FT TRANSMEM 1080 1100 Helical. {ECO:0000255}. FT TRANSMEM 1154 1174 Helical. {ECO:0000255}. FT TRANSMEM 1759 1779 Helical. {ECO:0000255}. FT TRANSMEM 1807 1827 Helical. {ECO:0000255}. FT TRANSMEM 1828 1848 Helical. {ECO:0000255}. FT TRANSMEM 1851 1871 Helical. {ECO:0000255}. SQ SEQUENCE 1882 AA; 209443 MW; 03CFA4D99A7120ED CRC64; MFSFFKQIFK SLKKFFFLLF GIIFVLFSII FLETSILQLS NNLVNTYTAL VQKTNSSDIV APAIFKESSP VYKTELKEEK RHFSKIKLTE KKINFIWPYQ ESDFGSDSEK KDSTTKSSDN NPRKGDVNDK DKLFLARKRG ILKAYGEANI AEKRIYKGLA VSFQNTYSFT GTDQESNNLN QNTVSDPQNL IYDKEGNLLG YFVDGLILDG IPLRAGIARF PGDKGKGEDK KTTKKKSEIK QASSATTVLQ PLAAQAKMTD AKETTNNEEP KKDSNVEEQY TTNNKDKVWF KSDETQAGSS SGESETSKLS TSYLFTGGQE AANWFPNLYA NVPIVLPISP GSQFWLETNP FKEIIEVFQK EKEEKEKQSF SLTFTLDTSK LSHLDKEEFD WLEKQAETIS SGSSFGDYNL KKKINSLKSF ELNINKDWLK NKVKAEKETI LDSLPGFSNS DKNTIFSTQS GDAKSGTQSN PSSLIALRSS VSFKPQLQQT NVALAQQQQD KQESSADDGV KDPTFSDVQT EFDKIGTENH TPQKNLNNVY AALLHQWKSI FQEDLVKKVT ALLEKYRDAF LKAKALKELE FSRQNLAIAT NVSSEESASF LVSNKDSQKY NDLSIIEGIN FKSWLAKEKS NPLDMVYGGK SNSEGFLEKV EYEFKPTQTD EKKKAAAKTT QGTTDSLTQL ADASSSSSSS STGDTKSTST KFQIYPKLAN ILAQAQLPEA SSIPDTLTNA IKQWSTLDKK GFEALDDTGK SKAANNYVAL LSYFTPEFQD PNELVVTNRQ KLDIPIIFKN GVNPLTLPTD QQSLVVQTPE AHGAVVSQQW LFKHDKEVLP LEGEYSWKEA LENPKNLPNW LNDLPDKYKF SINGLTFAIL GVGESVETGY PVLSTNSPLP NSQDEGLIFL NEQGYRSVLF AVPAASEENY YAFKSDDIKA KFPGQDPIQV VASKLKGYLN VPDSDLAFNV KDISKFQYLT TARNYFPDLV QNYLAIASVV IAAFLSILAL YLTILLIKSF IKKNQTEFSI IRAGGFSTAK FIAGMSVFAG IVALASSFFG VLFAFLLERQ VKGIISRYWF IALPANSFNW ISFFGSMLLI FVIFQFISWI AFKQLFSKPV NVLIDQGNET KFSVFLHLLK RKSYTMTPLG KFRVSLIISR LSRLFTYVGL SSIALLLIGI AGTIPQKFGA AQSNTVLNRN FNYRLNLQTP TEQSGWYAIQ PYSRFGQTDD SLGIKALYKD KGDQIQQQQQ QQQQQGNDKE HPYNLKELKI SDRGGNPIKH NGKEIELGNL LLPSFGGAQQ LNTDENFFRH ASLSKWLIDF PIRVGGANIN PWEIVEKSIP KQITQLLSAS SDQFLIAVLT DDYFNNLNNN GFLTRNPRTN FIQLDAARVL TQINVFNPGG VKFNEQFLKF LTKVYGDPEL SYQDSKLTYG IVPVDPQIEE TYTYVQGPFG FKETELNPDS PYTLTGISPD SKFVNLTDSG GNSLRSLISS DSEMNVIVNA GFQYANNTKI GDFIFIQPKN TATRYSEKFL KSPPKTPTVK FRVVGVSTDA FGQELYINQN IANRLLKLNG FDGRGVIKDV VKDGQSTDDS GGTSSGGGSC GGGSTSSTTK DKYKIEYVKP TGYVPFNGVF SKELNPSLVS KALVLNSNIG VWGNFTDFGN NFTNLVKGKE NKIITSILPS DPDILKQLAK EKGENGVDSM TYENLRKKVI EKYTSEWSST QSLASGARGI FGDNIMVPAL KLDAAGASAQ IIRNNAEVLF NTVNQVDGFL LGTIIPFIFI TCVVLGISML EEMKRIFISL KSIGYKDSQN LVSLLCFFIP AFVLSLLISI AILAGLLVGV QALVFGVAQV FLTNVFEFLP YMVGIVLFGA TIFVIGSYFW IKLRSAELKE GF // ID YCHF_MYCPN Reviewed; 362 AA. AC P75088; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944}; GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; GN OrderedLocusNames=MPN_026; ORFNames=B01_orf362, MP128; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S CC ribosomal subunit in a nucleotide-independent manner. CC {ECO:0000255|HAMAP-Rule:MF_00944}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. YchF/OLA1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00944}. CC -!- SIMILARITY: Contains 1 OBG-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; U00089; AAB95776.1; -; Genomic_DNA. DR PIR; S73454; S73454. DR RefSeq; NP_109714.1; NC_000912.1. DR RefSeq; WP_010874383.1; NC_000912.1. DR ProteinModelPortal; P75088; -. DR EnsemblBacteria; AAB95776; AAB95776; MPN_026. DR GeneID; 876898; -. DR KEGG; mpn:MPN026; -. DR PATRIC; 20021327; VBIMycPne110_0025. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR BioCyc; MPNE272634:GJ6Z-28-MONOMER; -. DR Proteomes; UP000000808; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; Complete proteome; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 362 Ribosome-binding ATPase YchF. FT /FTId=PRO_0000122459. FT DOMAIN 2 258 OBG-type G. FT NP_BIND 11 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00944}. FT METAL 15 15 Magnesium. {ECO:0000250}. FT METAL 35 35 Magnesium. {ECO:0000250}. SQ SEQUENCE 362 AA; 40607 MW; 7C79B46C84D5FF83 CRC64; MLSAGIVGLP NVGKSTLFSA ITNLQVEIAN YPFATIEPNA GIVNVIDERL DKLASLIKPD KVTHTTFRFV DIAGLVKGAS KGEGLGNQFL ANIREVDLIC HVVRCYEDKK IVHVNNQVDP VFDFEIIVNE LIQADIEVVN TRIGKIKRKA ESGDKQSKEE YQLLAPVLQG LQQNQMVLHL VNEVDLKKLK SLNLLTAKPI LVVANVSEAD LSNLDHNPHL TQLNQFLKQH NLPHAIPVCA LLENELSSLD ANGRQDWLKE LGLSDYQGLN QLIKTAYDAI GLWSFFTFGK QEVRAWAFKK GWLAPQCAGE IHTDFERGFI KVEVISWNQL YELKSLQEAK KQGLVRLRGQ GLRDARWWCV SL // ID Y346_MYCPN Reviewed; 115 AA. AC P75432; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=Uncharacterized protein MPN_346; GN OrderedLocusNames=MPN_346; ORFNames=H91_orf115, MP490; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96138.1; -; Genomic_DNA. DR PIR; S73816; S73816. DR RefSeq; NP_110034.1; NC_000912.1. DR RefSeq; WP_010874702.1; NC_000912.1. DR IntAct; P75432; 1. DR REBASE; 6705; MpnIIP. DR EnsemblBacteria; AAB96138; AAB96138; MPN_346. DR GeneID; 877416; -. DR KEGG; mpn:MPN346; -. DR PATRIC; 20022048; VBIMycPne110_0371. DR OrthoDB; EOG6JDWGW; -. DR BioCyc; MPNE272634:GJ6Z-363-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 115 Uncharacterized protein MPN_346. FT /FTId=PRO_0000210663. SQ SEQUENCE 115 AA; 13468 MW; 95E6E8BEFE9F054B CRC64; MSDALDDENV LCFRYKSYYI KDDGSRIDTL NEERIKHIVD FTLDKYLDAT QNTPKFDNFE NPVKEGFNSI FACESKEAAI EYYKEFKKQI EQKKLPIKIA SIIAQTKVVM NKKLV // ID Y358_MYCPN Reviewed; 534 AA. AC P75422; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG255 homolog; GN OrderedLocusNames=MPN_358; ORFNames=H91_orf534, MP478; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96126.1; -; Genomic_DNA. DR PIR; S73804; S73804. DR RefSeq; NP_110046.1; NC_000912.1. DR RefSeq; WP_010874714.1; NC_000912.1. DR EnsemblBacteria; AAB96126; AAB96126; MPN_358. DR GeneID; 876886; -. DR KEGG; mpn:MPN358; -. DR PATRIC; 20022078; VBIMycPne110_0385. DR OMA; QWPILTT; -. DR OrthoDB; EOG66XBNF; -. DR BioCyc; MPNE272634:GJ6Z-376-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 534 Uncharacterized protein MG255 homolog. FT /FTId=PRO_0000210491. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. SQ SEQUENCE 534 AA; 62644 MW; 08B95C4D515FAF6C CRC64; METQNQIETL RYIFNQLNNQ DKPQIIWFSG EGEDEKINFL IRLDNYFQPT FVQDLTINFL PAFVKRNKKN PPNTLAKGNF VNIANKLLAV LARSLSWKQL NKPQQKWLLW LLVPFLLLRQ LWLKKKVSKI FQFVNERGIL SFIKEQWPIL TTLVTVGTTL GTPIFSITIS QQKAILENAG HGAFVFLVIF SVFAIALGLV SSLIFLVSSL FSIRQKKSLQ QLHQILSRLI NKYFCFANSE QNQTGRYQLK NTGVCFFYGF DFEEKEYITQ AMNLLLLLKQ TNCFVLVGCK ESNMLLIKNK VEPDINLKQS SLYLDLKSQI SPLAQISKYN LLFEELALDA DMFYLEDFFA LLKTPRQIVN FLFRIKQNLK EFHQPQTLWF DYLALWALVI ATDFEFNNVL WSFNDYLSLT NKQKEDYASV NLTAFFNRSL KNHKDNSLLF KPELFNTHAY IPETYTQVTL ENIDSDKRAQ LVPLNWFSQQ KFSDFIEEKI NFWQTQQAEN KVFYLTLGER IFFLVLVNKK FKQIKLEAAL KYLN // ID Y367_MYCPN Reviewed; 322 AA. AC P75414; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 59. DE RecName: Full=Putative MgpC-like protein MPN_367; GN OrderedLocusNames=MPN_367; ORFNames=H91_orf322, MP469; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96117.1; -; Genomic_DNA. DR PIR; S73795; S73795. DR IntAct; P75414; 2. DR EnsemblBacteria; AAB96117; AAB96117; MPN_367. DR PATRIC; 20022100; VBIMycPne110_0394. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-387-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 322 Putative MgpC-like protein MPN_367. FT /FTId=PRO_0000210723. SQ SEQUENCE 322 AA; 33174 MW; 951918E361300E9B CRC64; MVGSGAAGSA SSLQGNGSNS SGLKSLLRSA PVSVPPSSTS NQTLSLSNPA PVGPQAVVSQ PAGGATAAVS VNRTASDTAT FSKYLNTAQA LHQMGVIVPG LEKWGGNNGT GVVASRRDAT STNLPHAAGA SQTGLGTGSP REPALTATSQ RAVTVVAGPL RAGNSSETDA LPNVITQLYH TSTAQLAYLN GQIVVMSSAR VPSLWYWVVG EDQESGKATW WAKTELNWGT DKQKQFVENQ LGFKDDSNSD SKNSNLKTQG LTQPAYLIAG LDVVADHLVF AAFKAGAVGY DMTTDSNAST YNQALVWSTT AGLDSDGGTR LW // ID Y369_MYCPN Reviewed; 253 AA. AC P75412; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized lipoprotein MPN_369; DE Flags: Precursor; GN OrderedLocusNames=MPN_369; ORFNames=H91_orf253, MP467; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB96115.1; -; Genomic_DNA. DR PIR; S73793; S73793. DR RefSeq; NP_110057.1; NC_000912.1. DR RefSeq; WP_010874725.1; NC_000912.1. DR EnsemblBacteria; AAB96115; AAB96115; MPN_369. DR GeneID; 876871; -. DR KEGG; mpn:MPN369; -. DR PATRIC; 20022108; VBIMycPne110_0398. DR OMA; ERKIEYF; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-389-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 253 Uncharacterized lipoprotein MPN_369. FT /FTId=PRO_0000014057. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 253 AA; 28978 MW; 00081B12D48966C4 CRC64; MRKKKFLSKV SFGSLFLLCG TVLSACTGIQ ADLRNLIKEA TGKDIDVYKA IKTTEGKKNM ITSLKKSYKV NPKDTTKLLL DAWKQSAEKG ELGIPDFDFD DVIYPASKDP FTMERKIEYF QMTYQSFKDL SIEAKLSYTF NWFGDYSSGD FTAKKGDKHY FDLFPKIKSN SDPGKQFTTE KFLTKEEKIK VNGKEITRNL EWIEFSASLS FSLKGKDDVS EKSVNKFLST FANNTEGYSS DINLFIYLEY LIK // ID Y375_MYCPN Reviewed; 129 AA. AC P75406; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MPN_375; GN OrderedLocusNames=MPN_375; ORFNames=A19_orf129, MP461; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_376 N-terminal region. 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; U00089; AAB96109.1; -; Genomic_DNA. DR PIR; S73787; S73787. DR RefSeq; NP_110063.1; NC_000912.1. DR RefSeq; WP_010874731.1; NC_000912.1. DR EnsemblBacteria; AAB96109; AAB96109; MPN_375. DR GeneID; 877397; -. DR KEGG; mpn:MPN375; -. DR PATRIC; 20022124; VBIMycPne110_0406. DR BioCyc; MPNE272634:GJ6Z-395-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MPN_375. FT /FTId=PRO_0000210668. SQ SEQUENCE 129 AA; 15202 MW; 43CC9E7A5CD389DB CRC64; MSFGLVGTVN NNGWKSPFRH ETKYRAGYDK FKYYKTHYRG AKKAGTNDDR WRWTAWFDLD FAHQKIVLIE RGELHRQADL KKSDPATNET SKTVWGSIKE KLLQNVNNLH SEKGVFLWFR QSGFTTTRN // ID Y396_MYCPN Reviewed; 971 AA. AC P75387; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MG277 homolog; GN OrderedLocusNames=MPN_396; ORFNames=F11_orf887, MP442; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP SEQUENCE REVISION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34750.1; -; Genomic_DNA. DR PIR; S73768; S73768. DR RefSeq; NP_110084.1; NC_000912.1. DR RefSeq; WP_010874752.1; NC_000912.1. DR ProteinModelPortal; P75387; -. DR EnsemblBacteria; AAG34750; AAG34750; MPN_396. DR GeneID; 877104; -. DR KEGG; mpn:MPN396; -. DR PATRIC; 20022168; VBIMycPne110_0427. DR KO; K12257; -. DR OMA; ALTFEYK; -. DR OrthoDB; EOG6HTNSM; -. DR BioCyc; MPNE272634:GJ6Z-419-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 971 Uncharacterized protein MG277 homolog. FT /FTId=PRO_0000210503. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 516 536 Helical. {ECO:0000255}. FT TRANSMEM 547 567 Helical. {ECO:0000255}. FT TRANSMEM 569 589 Helical. {ECO:0000255}. FT TRANSMEM 615 635 Helical. {ECO:0000255}. FT TRANSMEM 651 671 Helical. {ECO:0000255}. FT TRANSMEM 727 747 Helical. {ECO:0000255}. FT TRANSMEM 763 783 Helical. {ECO:0000255}. FT TRANSMEM 795 815 Helical. {ECO:0000255}. FT TRANSMEM 817 837 Helical. {ECO:0000255}. FT TRANSMEM 878 898 Helical. {ECO:0000255}. FT TRANSMEM 900 920 Helical. {ECO:0000255}. FT TRANSMEM 923 943 Helical. {ECO:0000255}. SQ SEQUENCE 971 AA; 108245 MW; 3B5D96DC58108B96 CRC64; MGLKKRVSFD WLLKIGIILV LAFLGLFGII FGSYKLLNDS RLGVVFNGST TTTVYFLNHK SKDANKELDP TQKKDGNGSG NNTEMITDVN GFLNNIEKSY ANSLYAQGFS SVNITKNSHD TSAKELSDKG VFDSSWLVND GLPSISVTFE QRREEARTRA RKRQIDAQVK RNALSAIEHN YKLSLETTDG IVLFDSFDKE FIRNSLTAVV PQTTNTNSAL TFEYKLSKNV ITKESLHNDF LDFIKSKSLT DSDYNTGNGQ KSVEGSGKWF KDKANGSAQN GNKTLVLWKD KEGAVQYVRN IFNVPKGGTD YLTFNEREKN LWDFLHAEGN FSSGDNLFLQ KNNNGNSPIT KASDITLKNI YYIYAAPTHF SQVATKDNNN KDAADVVAVA NSADTRKLRS GDATGFSGLF SNYILAEIRT EDPVAKNGDP VKVNATLQSF LDSNNQRLEH GGNIKFQVAN FVNNDGSYVP ASYLEASRVK VLLSNGFPET ATIAAANTKL VNAPLSNTLA RDVSNFASSF IALGVIILLA TIALGIRYKL LGLYKALALA LSAISSLAFF SAVGGVVDVF SFVGIFFVVA VNIINLITLA ELFLRNIKNN ASIVESWKLC LKRSFFTMIE THICWLLSAL VVIYLSNYQV QQLGTLMAVS AITSYFLNYG LGVILVWLFV SSHSGLEWRF FLYKKDAQAL TKTSSNYSIL TENNDIQTDF FISKNQHDFF GKKKWSLLFI WLTVLAFGVV MLGLYLGAPQ LLGNFLAADI ESSTGIMLGV GVISLLYLLY SLPRYGVAYG ISYLIALILL AAGLFGAMYL ANFIFRIDQS TIQLIIFVYL FWLFFQARIG QTTIWTYCYW FKRSLKDRVF VKNLFNDNVN SQWRLDLIGS SVLILLFIVY AAFNFGGING TINLVIFYLI AIVALFSVFV NGLPLFSFGL INGWLSPYNY VQIHITLRHK KQMFKEVDQI EEQLISGINS F // ID Y405_MYCPN Reviewed; 197 AA. AC P75379; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MG286 homolog; GN OrderedLocusNames=MPN_405; ORFNames=F11_orf197, MP433; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96081.1; -; Genomic_DNA. DR PIR; S73759; S73759. DR RefSeq; NP_110093.1; NC_000912.1. DR RefSeq; WP_010874761.1; NC_000912.1. DR EnsemblBacteria; AAB96081; AAB96081; MPN_405. DR GeneID; 877191; -. DR KEGG; mpn:MPN405; -. DR PATRIC; 20022200; VBIMycPne110_0438. DR OMA; SKRKLIC; -. DR OrthoDB; EOG6QRW9S; -. DR BioCyc; MPNE272634:GJ6Z-433-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 197 Uncharacterized protein MG286 homolog. FT /FTId=PRO_0000210515. FT TRANSMEM 11 31 Helical. {ECO:0000255}. SQ SEQUENCE 197 AA; 23189 MW; 370443D8BF0B75AB CRC64; MIFSISKRKL ICGFSLVALT IAGIVGGVYL VTKNNQQTTP QTNHFNVADP VNKVPNWRKL GPETQRELRD LLYPLDDTGY FIYKYGAISR YLQSQKELDE LVDYRTVLPS TQKHFKYDSF NQSVLESKLR KWLMKAIKQH PYFQHFEFDP VLKAQYNINI PAQKITVNAV WFYKKDNDLT TGKPIRYWDQ FEIKLKQ // ID Y409_MYCPN Reviewed; 533 AA. AC P75375; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Putative adhesin P1-like protein MPN_409; GN OrderedLocusNames=MPN_409; ORFNames=F11_orf533L, MP429; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96077.1; -; Genomic_DNA. DR PIR; S73755; S73755. DR RefSeq; NP_110097.1; NC_000912.1. DR RefSeq; WP_010874765.1; NC_000912.1. DR EnsemblBacteria; AAB96077; AAB96077; MPN_409. DR GeneID; 877293; -. DR KEGG; mpn:MPN409; -. DR PATRIC; 20022212; VBIMycPne110_0443. DR OMA; GTENSTQ; -. DR BioCyc; MPNE272634:GJ6Z-438-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004940; Adhesin_P1_dom. DR Pfam; PF03257; Adhesin_P1; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 533 Putative adhesin P1-like protein MPN_409. FT /FTId=PRO_0000210714. SQ SEQUENCE 533 AA; 56824 MW; E93816A1204A2465 CRC64; MDYVPWIGNG YRYGKNHRGV DDITAPKTGA GSSSGTSTNT SGSRSFLPTF SNVGVGLKAN VQATLGGSQT TTTGGSKWPT LDQANLLLWT GSGWRNDKNG QSDENHTTFK SATGSGQQGG SSGTSAGNPD SLKQDKISKS GDSLSVVDTG QGDDTHYANL PPSITPTSDW PNALSFTNKN NAQRVQLFLR GLLDSIPVLV NKSGQDDNSK FKAEHQKWKY SDFKSDQTKL NLPAYGEVNG LLNPALVETY FGTTRAGGSG NQNRTTVPGI GFKIPEQNND SKAVLITPGL AWTPQDVGNL VVSGTTVSFQ LGGWLVTFTD FVKPRSGYLG LQLTGLDVSE ATQRELIWAP RPWAAFRGSW VNRLGRVESV WDFKGVWADQ AHSAVSESQA ATSGTTTATG AALPEHPNAL AFQVSVVEAS AYKPNTSSGQ TQSTNSSPYL HLIQPKKVTQ SDKLDDDLKN LLDPNEVRAR MLQSFGTENS TQAQPQSLKT TTPVFGAMSG TSAVCLVVGV PRRAQAQVNL AWISPPLNGW VGH // ID Y414_MYCPN Reviewed; 493 AA. AC P75372; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 64. DE RecName: Full=Putative MgpC-like protein MPN_414; GN OrderedLocusNames=MPN_414; ORFNames=A05_orf493, MP426; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96074.1; -; Genomic_DNA. DR PIR; S73752; S73752. DR RefSeq; NP_110102.1; NC_000912.1. DR RefSeq; WP_010874770.1; NC_000912.1. DR EnsemblBacteria; AAB96074; AAB96074; MPN_414. DR GeneID; 877297; -. DR KEGG; mpn:MPN414; -. DR PATRIC; 20022224; VBIMycPne110_0449. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-443-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 493 Putative MgpC-like protein MPN_414. FT /FTId=PRO_0000210724. SQ SEQUENCE 493 AA; 52836 MW; 535607770E515304 CRC64; MKPTSLPKNF TNNPAPKAVT GFKLDNGRAY RKLNEAWPVY EPLDSTKDGK GKDKDGWTTS GASEPKGDAP LVSSTGSQMS AVTDSQQSGH NSGLVSLAQR STTVAVQKSD SSGFQGQGTT DNKFQKYLNT AQALHQMGVI VPSLETWPGK PSTGIATRAG GGVSVQAATR QSSSTNEDLP NVITQLYHTS TSQLAYLNGQ IVVMGSNAVP SLWYWVVDER TTSGSATWWA KTHLNFGTEV QKSFVENQLG FKDDSNSDSK NSNLKAQDLT QPAYLITGLD VVQDHLVFAA FKAGAVGYDM TTDSNASTKD QALAWSTTAG LDSAGGYNNL VENTAGLNGP INDLFTLLDT FAYVTPVSGM KGGSQNNEEV QTKYPVKDDS KASAKIASLI NASPLNSYGD DGVTVFDALG LNFNFKLDEA RLPSRTDQLL VYGIVNESEL KSARENAQST SDDNSNTKVK WTKPPRTTSP CRITTVPISP KRVTEEERSS GNH // ID Y438_MYCPN Reviewed; 345 AA. AC P75340; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 53. DE RecName: Full=Uncharacterized protein MPN_438; GN OrderedLocusNames=MPN_438; ORFNames=H08_orf345, MP403; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96051.1; -; Genomic_DNA. DR PIR; S73729; S73729. DR IntAct; P75340; 1. DR EnsemblBacteria; AAB96051; AAB96051; MPN_438. DR PATRIC; 20022274; VBIMycPne110_0474. DR OrthoDB; EOG628F7R; -. DR BioCyc; MPNE272634:GJ6Z-467-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 345 Uncharacterized protein MPN_438. FT /FTId=PRO_0000210676. SQ SEQUENCE 345 AA; 37472 MW; 59A66EF6DC103DB0 CRC64; MPSPFFAEEK DIPENQNVGN KRWKKLIKGE GSDDGKEKSS DDDDSSSSTK GLFGWRGDTS SGNLFDFPNT LTDVGETKQI VDATTIVDQL EAADLGAALN LKLSFLKQDF DELPVIKKLP DNLNDTIVAK SDNLEKTSKT NSTFYKDNGD SSEKQGSAES KNSPKTQLKE IFNGQNGDSG NLGKLAEQLQ KTDSTKMEAR SQTWQLRNAV SLKTTNMAQS DENYLLLDAA IPAFETSSQS PQSSGTISGS GALVNLTSTS VNLTQQKSST TPLNQRIVRN STGVKLLALE GLLYYVVGSS NKQQSSSSTI ATSLAQNQSN NNQEQEINSS LQKNLLKFRA FQAKN // ID Y455_MYCPN Reviewed; 287 AA. AC P75328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG320 homolog; GN OrderedLocusNames=MPN_455; ORFNames=H08_orf287, MP386; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96034.1; -; Genomic_DNA. DR PIR; S73712; S73712. DR RefSeq; NP_110143.1; NC_000912.1. DR RefSeq; WP_010874811.1; NC_000912.1. DR ProteinModelPortal; P75328; -. DR EnsemblBacteria; AAB96034; AAB96034; MPN_455. DR GeneID; 877110; -. DR KEGG; mpn:MPN455; -. DR PATRIC; 20022310; VBIMycPne110_0492. DR OMA; NFEANDI; -. DR OrthoDB; EOG61CM8D; -. DR BioCyc; MPNE272634:GJ6Z-484-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 287 Uncharacterized protein MG320 homolog. FT /FTId=PRO_0000210537. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 205 225 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. SQ SEQUENCE 287 AA; 32464 MW; 8821A9136BC7D1F9 CRC64; MINQANNQVN FSEQQFVHHK RFSVIRLTFS VAAIGILFIF LIGFGVQQLL TNTTSLGTLA SDIRTLGTIA FVASLVSLIL YFVTAFKLRN RNTTLAWFWG LIIADVISYG ITLGVLLTLA TTQLRELIDF KFSDIVFAFL GAALVYGTVW GLSALPSQQR RYQQTQTLFR IFIWAFFISI IASLLTFVLN FTVFRGGRTN ILDLLFPGLS LIVGGIFSLL SVYFVCLQIR NEQDLVKLYE SQDPALAKAQ MWRSALFFGA WLVSSFMNLV YFILRIILLT RNLSRAF // ID Y456_MYCPN Reviewed; 1005 AA. AC P75327; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized lipoprotein MG321 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_456; ORFNames=H08_orf1005, MP385; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96033.1; -; Genomic_DNA. DR PIR; S73711; S73711. DR RefSeq; NP_110144.1; NC_000912.1. DR RefSeq; WP_010874812.1; NC_000912.1. DR EnsemblBacteria; AAB96033; AAB96033; MPN_456. DR GeneID; 876971; -. DR KEGG; mpn:MPN456; -. DR PATRIC; 20022316; VBIMycPne110_0493. DR OMA; AQLNRFN; -. DR OrthoDB; EOG6SFP68; -. DR BioCyc; MPNE272634:GJ6Z-487-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 1005 Uncharacterized lipoprotein MG321 FT homolog. FT /FTId=PRO_0000014035. FT LIPID 25 25 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 25 25 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1005 AA; 110512 MW; 59E608AD8975FC2B CRC64; MKFQRKYWGL LSTLGVSSAV ALSACAAQAR DVYVTSSASD LLKNNSVPMS MFNVSPTSSF FGSKYAGLTT YIATGSNKDD GVNVATQTQE KLVLELATSV KGYKKKDKAT SSQKTSTNSS CTTTSSGTST SGEDDWECIG EIKRQSSSNG QNNQQSKSIT EEEKFQEISQ KATRYEFAID TGIKWVDNNG KPVKDASGND VKLSSKDFER GFEAYILSSE LRFNRNGYFI DLMGLDVKKT VGMTKKNGAQ VQMKVASSDE KDGEEKTVKI TDDAYNPEDY QSTDDSKFNV YLTSPFPFLL SMMSKEFFFP IPHTHPKVKA IKVGKDSPLV YNEKNGSKIL DQTKTNFDGI YGGGVNAWRD TWSVGPYYVE SFNQSQIVFK RNSEYDTHIT PNLPKTREDN EKPIPTMINY FQPGATPEVF YSNYIAGGLS SAEVPYSQQE DARSRFAGTG DLRWVKVQKT AQSAQITYSS RPYVVEGETV KTNSNITETE AKFLYNSESE EALTIRAGIN GLINWQNLAI ILLPNSGDLN YSIVPFGIFK EKGKNGASVQ QKAVSTTEGS DLMNDYYYKI EKEQRLGLIP QREGNYEKNK NVLESATVKI NYYSSKATSG QAGAAASAAF AKNNNTSDNT QQNQTSSVEA KSVNVTKHSF VQALKKVGFS GSNPLHFNMK LGNSSLSANG VDYYNAVKQA LTELGTADNG EKLIVPEIIL GDAQGPTRNE WYIGLSSVLG FSSWSPDYDG VGTWLDAATQ LNDQGGGDVI TYSSGAHIVR TLLLAASQKD VHSKFTQKID QQNTASTTSD VTVKKADSSQ DSSKSNTEEE KWDDVTSADL FKDDPYVLKN FGDAKAQAAQ RSTGSTTSGN GTQASLEFTK KALSLLKFLV DNGILDKEKV KEAIKDPNKY LGKRDKIENG TNKPSKNEDF IGYELKDIYK KAAQLNRFNS IWAEKDTDNA KFLITVVDSY FPVLPVPAAG LNETSPTLLK PWFQFRSAPS GNGTIRDYGF IPENK // ID Y458_MYCPN Reviewed; 157 AA. AC P75325; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MPN_458; GN OrderedLocusNames=MPN_458; ORFNames=H08_orf157b, MP383; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_456 and M.genitalium MG321 central CC region. {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; U00089; AAB96031.1; -; Genomic_DNA. DR PIR; S73709; S73709. DR EnsemblBacteria; AAB96031; AAB96031; MPN_458. DR PATRIC; 20022322; VBIMycPne110_0495. DR BioCyc; MPNE272634:GJ6Z-490-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Uncharacterized protein MPN_458. FT /FTId=PRO_0000210680. SQ SEQUENCE 157 AA; 17452 MW; BBE58C06CB795A2A CRC64; MFKLNKKTLD KHPKVQIWWT ITTIRFKFEK EQRLGLIPQR EGQYEKNKNV LTSATVKVNH YSSKQGQTQS ASKAAVAVKA NKAAGDSTTT SSQTPSVEAK KVEVTKQSFV QALRKVGFTG NNPLHFNMKL GNSSLSANGV DYYNAVKQAL TELGTCW // ID Y462_MYCPN Reviewed; 270 AA. AC P75321; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MPN_462; GN OrderedLocusNames=MPN_462; ORFNames=H08_orf270, MP379; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAB96027.1; -; Genomic_DNA. DR PIR; S73705; S73705. DR RefSeq; NP_110150.1; NC_000912.1. DR RefSeq; WP_010874818.1; NC_000912.1. DR IntAct; P75321; 1. DR EnsemblBacteria; AAB96027; AAB96027; MPN_462. DR GeneID; 877044; -. DR KEGG; mpn:MPN462; -. DR PATRIC; 20022344; VBIMycPne110_0499. DR OMA; PWTPWLA; -. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-501-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF12378; CytadhesinP1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 270 Uncharacterized protein MPN_462. FT /FTId=PRO_0000210681. SQ SEQUENCE 270 AA; 29795 MW; 5D54A3A47F7B49E9 CRC64; MFGLKVKDAT VDSSKQSTES LKGEESSSSS TTSSTSTTQR GGSSGDTKVK ALQVAVKKKS DSEDNGQIEL ETNNLANAPI KRGSNNNQQV QLKADDFGTS PSSSESGQSG TPTPWTPWLA TEQIHKDLPK WSASILILYD APYARNRTAI DRVDHLDPKV MTANYPPSWR TPKWNHHGLW DWKARDVLVQ TTGFFNPRRH PDWFDQGQAV AENTQTGFDT DDTDNKKQGF RKQGEQSPAP IALPFEAYFA NIGNLTWFGQ ALLVFGICLS // ID Y482_MYCPN Reviewed; 73 AA. AC Q9EXD7; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2003, sequence version 2. DT 13-APR-2016, entry version 84. DE RecName: Full=UPF0154 protein MG335.1 homolog; GN OrderedLocusNames=MPN_482; ORFNames=MP359.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0154 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG34745.1; 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; U00089; AAG34745.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_110170.1; NC_000912.1. DR EnsemblBacteria; AAG34745; AAG34745; MPN_482. DR GeneID; 877161; -. DR KEGG; mpn:MPN482; -. DR PATRIC; 20022388; VBIMycPne110_0521. DR KO; K09976; -. DR OMA; KQIRQIM; -. DR OrthoDB; EOG6J753J; -. DR BioCyc; MPNE272634:GJ6Z-523-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR HAMAP; MF_00363; UPF0154; 1. DR InterPro; IPR005359; UPF0154. DR Pfam; PF03672; UPF0154; 1. DR ProDom; PD048972; UPF0154; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 73 UPF0154 protein MG335.1 homolog. FT /FTId=PRO_0000214970. FT TRANSMEM 6 26 Helical. {ECO:0000255}. SQ SEQUENCE 73 AA; 8231 MW; B594DF7F6991BD90 CRC64; MNDLALALGL GIPLSLLVGV IIGYFISIKI FKKQIRDNPP ITENQIKAMY AKMGRKLSET QVKEIMRSIK NQK // ID Y486_MYCPN Reviewed; 147 AA. AC P75299; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 52. DE RecName: Full=Uncharacterized protein MPN_486; GN OrderedLocusNames=MPN_486; ORFNames=MP356, P02_orf147; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96004.1; -; Genomic_DNA. DR PIR; S73682; S73682. DR IntAct; P75299; 1. DR EnsemblBacteria; AAB96004; AAB96004; MPN_486. DR BioCyc; MPNE272634:GJ6Z-527-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MPN_486. FT /FTId=PRO_0000210686. SQ SEQUENCE 147 AA; 16257 MW; 0C15A7285A8B14C2 CRC64; MAIFARETMD LIATASFPSI KKLSSGFWLD LFESTLTSGN ELVLLPPTRY SYWSIMAVAN PTPLKAPRRL DLVTKSLLAA PLLFHLVCQS NNPVREDVLD CWVWPFFCSG NTALMKSPKF WALLGVGSKV VLPWLCPLLG SRNAGKA // ID Y488_MYCPN Reviewed; 140 AA. AC P75297; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MG337 homolog; GN OrderedLocusNames=MPN_488; ORFNames=MP354, P02_orf140; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96002.1; -; Genomic_DNA. DR PIR; S73680; S73680. DR RefSeq; NP_110176.1; NC_000912.1. DR RefSeq; WP_010874844.1; NC_000912.1. DR ProteinModelPortal; P75297; -. DR EnsemblBacteria; AAB96002; AAB96002; MPN_488. DR GeneID; 877224; -. DR KEGG; mpn:MPN488; -. DR PATRIC; 20022400; VBIMycPne110_0527. DR OMA; MDIRART; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; MPNE272634:GJ6Z-529-MONOMER; -. DR Proteomes; UP000000808; 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; IPR002871; NIF_FeS_clus_asmbl_NifU_N. DR Pfam; PF01592; NifU_N; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MG337 homolog. FT /FTId=PRO_0000210548. SQ SEQUENCE 140 AA; 15911 MW; 0641B62568B16BD5 CRC64; MDRKIREQII AIYSNLQHKQ DLTQFAHCLT TKADDNCEDF FNLGLQFQNN QLTALGFNGE GCIISTIASE LTLSALEGKT IKEAIVLLEQ FMEAVQTGSL STPLPQALQL LWDFQIDQKR LNCLLLTPQN LLQWLKDFSH // ID Y502_MYCPN Reviewed; 422 AA. AC P75285; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MPN_502; GN OrderedLocusNames=MPN_502; ORFNames=MP341, P02_orf422V; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the adhesin P1 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; U00089; AAB95988.1; -; Genomic_DNA. DR PIR; S73667; S73667. DR RefSeq; NP_110190.1; NC_000912.1. DR RefSeq; WP_010874858.1; NC_000912.1. DR EnsemblBacteria; AAB95988; AAB95988; MPN_502. DR GeneID; 876750; -. DR KEGG; mpn:MPN502; -. DR PATRIC; 20022442; VBIMycPne110_0548. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MPNE272634:GJ6Z-543-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF12378; CytadhesinP1; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 422 Uncharacterized protein MPN_502. FT /FTId=PRO_0000210689. SQ SEQUENCE 422 AA; 46142 MW; 03BE7D381C7CC298 CRC64; MRDNIAKGIT AGSNTQQTTY DPTRTEATLT TATTFALRRY DLAGRALYDL DFSKLNPQTP TRDQTGQITF NPFGGFGLSG AAPQQWNEVK DKVPVEVAQD PSNPYRFAVL LVPRSVVYYE QLQRGLALPN QGSSSGSGQQ NTTIGAYGLK VKNAEADTAK SNEKLQGYES KSSNGSSSTS TTQRGGSSNE NKVKALQVAV KKKSGSQGNS GDQGTEQVEL ESNDLANAPI KRGSNNNQQV QLKADDFGTA PSSSGSGTQD GTPTPWTPWL TTEQIHNDPA KFAASILILY DAPYARNRTA IDRVDHLDPK VMTANYPPSW RTPKWNHHGL WDWKARDVLL QTTGFFNPRR HPEWFDGGQT VADNEKTGFD VDNSENTKQG FQKEADSDKS APIALPFEAY FANIGNLTWF EQALLVFGIC LS // ID Y505_MYCPN Reviewed; 253 AA. AC P75281; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MPN_505; GN OrderedLocusNames=MPN_505; ORFNames=MP337, P02_orf253; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95985.1; -; Genomic_DNA. DR PIR; S73663; S73663. DR RefSeq; NP_110193.1; NC_000912.1. DR RefSeq; WP_010874861.1; NC_000912.1. DR IntAct; P75281; 1. DR EnsemblBacteria; AAB95985; AAB95985; MPN_505. DR GeneID; 877169; -. DR KEGG; mpn:MPN505; -. DR PATRIC; 20022452; VBIMycPne110_0553. DR OMA; SEPFKFE; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; MPNE272634:GJ6Z-546-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 253 Uncharacterized protein MPN_505. FT /FTId=PRO_0000210690. SQ SEQUENCE 253 AA; 29454 MW; 37849B1A081B60E3 CRC64; MRKKRLLSRI SFSSLFLLCG TVLSAYTGIQ ADLRNLIKET TKKDIDVYKA IKTTEGKKNI ITSLKKSYEV NPKDTTKLLL DAWKQSFEKG ELGIPDLDFE DVIYPKTSEP FKFERKVDHF QMTYQSFKDL SIEAKLSYNF NWFGDYSLGG FTAKKGDKHY FDLFLKIKSN SDPKKQFTTE KFLTKEEKNK VNGKEITRNL EWIEFSASLS WLIKGKDDVS QKSVKQFLSS YANNTSGYSR DINLFIYLEY LIK // ID Y508_MYCPN Reviewed; 509 AA. AC P75278; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 62. DE RecName: Full=Uncharacterized protein MPN_508; GN OrderedLocusNames=MPN_508; ORFNames=MP334, P02_orf509; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- INTERACTION: CC P75361:p115; NbExp=1; IntAct=EBI-2258562, EBI-2258558; CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95982.1; -; Genomic_DNA. DR PIR; S73660; S73660. DR RefSeq; NP_110196.1; NC_000912.1. DR RefSeq; WP_010874864.1; NC_000912.1. DR IntAct; P75278; 2. DR EnsemblBacteria; AAB95982; AAB95982; MPN_508. DR GeneID; 877284; -. DR KEGG; mpn:MPN508; -. DR PATRIC; 20022460; VBIMycPne110_0557. DR OMA; WSGEMNL; -. DR BioCyc; MPNE272634:GJ6Z-549-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 509 Uncharacterized protein MPN_508. FT /FTId=PRO_0000215255. SQ SEQUENCE 509 AA; 57626 MW; 8CDC95BB941A6987 CRC64; MNQLQAEINA ANAVFPVSDS TKIPKVSQKL FGLLGDGFFP QLHPKGLKIA DNIAALFDQY NLKSIALKNF DLNLERKNDI VIQGKVCYSF SIKMDFATIY EGDGSTIDLQ FALNASTTNF ANLTDLQDSF WQSGKDLNTQ LFWKPSVHKL ISNGTNDLTT LAQTALGDSL FDTKVNLTES VIEINNQTDV ATKFREKVLN SFKQEREKAH AEHVEKLRKL EEERKLQEAE AKAKAEEVKK LEAEREAFNK SLTAASEFKQ YWSKKNKDVT DKKQLAEALK ISLEADRNRT FSFLIAGFRT AIDWYYNAKK ENNDAKQKAF GSQGIQFPKD GLNGIYMPDW LRGELTSKSN INLKIKELKV QNKIESPTIN WIDGVGIKQD KANPFNYRFE VDIKYTGGYQ LYGFYAFAAL FTKFPSSWSG EMNLKFIVDG SIPVYTVAKK DYPGSLFQFN DKDELLFTLY VKEQISVADP NFMNLLRGQN LHDLELVTGA TKPPVVDLAS YLHFVLLSA // ID Y532_MYCPN Reviewed; 282 AA. AC P75246; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG356 homolog; GN OrderedLocusNames=MPN_532; ORFNames=G12_orf282b, MP310; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95958.1; -; Genomic_DNA. DR PIR; S73636; S73636. DR RefSeq; NP_110221.1; NC_000912.1. DR RefSeq; WP_010874889.1; NC_000912.1. DR ProteinModelPortal; P75246; -. DR EnsemblBacteria; AAB95958; AAB95958; MPN_532. DR GeneID; 877361; -. DR KEGG; mpn:MPN532; -. DR PATRIC; 20022539; VBIMycPne110_0593. DR OMA; ANMARES; -. DR OrthoDB; EOG628F4J; -. DR BioCyc; MPNE272634:GJ6Z-577-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR011009; Kinase-like_dom. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; SSF56112; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 282 Uncharacterized protein MG356 homolog. FT /FTId=PRO_0000210564. SQ SEQUENCE 282 AA; 33296 MW; 5662F03B9E06A89A CRC64; MNKGDAIDFL CEKLNLQPTA VAHVEQIHSG FTNFSFFTEL KDGSKYQVRL ARKDVPLNRR NEQIILDLVT PIFGNPFVYF DVTAGNAIKK WIEGKQPKRP TRLFLEQLVA SLKKVHAVEW KQFANEIWIF DPLIYFNQTK LPDFYKKLYV ELTDKHKAIP KTLCHHDSTF DNLVYTPKKQ VVLIDFEWSC VDNPYYEIAN IIREELTIET ANQIIDLYGS LDKKLVFETV IYVLLFAFQW TEIMPQTQQI IDYKKWVQKR LNYFLKALFP NTWKIAKTIP LY // ID Y537_MYCPN Reviewed; 412 AA. AC P75241; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MG360 homolog; GN OrderedLocusNames=MPN_537; ORFNames=G12_orf412, MP305; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 umuC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00216}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95953.1; -; Genomic_DNA. DR PIR; S73631; S73631. DR RefSeq; NP_110226.1; NC_000912.1. DR RefSeq; WP_010874894.1; NC_000912.1. DR ProteinModelPortal; P75241; -. DR IntAct; P75241; 1. DR EnsemblBacteria; AAB95953; AAB95953; MPN_537. DR GeneID; 877274; -. DR KEGG; mpn:MPN537; -. DR PATRIC; 20022551; VBIMycPne110_0599. DR KO; K02346; -. DR OMA; GTANDIT; -. DR OrthoDB; EOG6FZ4D8; -. DR BioCyc; MPNE272634:GJ6Z-582-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1490.100; -; 1. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. 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; Reference proteome. FT CHAIN 1 412 Uncharacterized protein MG360 homolog. FT /FTId=PRO_0000173985. FT DOMAIN 20 199 UmuC. {ECO:0000255|PROSITE- FT ProRule:PRU00216}. SQ SEQUENCE 412 AA; 47051 MW; ED1114DD5898DB2E CRC64; MIGTFTYLDP TIQADPNLLF FYFDFDAFFA SVEEIENPEL KNQPLIVGNR TSRSVVSTCN YLARSYGIKS GMPIAKALEL CPQAIFATSH FRNYRKYSAK IFAMIAEQFN LEVHTLSIDE GFVCFRDLSP RKAFSLAKRI QRHVYEQLNF HISIGISNQF TLAKIFSNQA KPFGVKSCFS KEVKRKLWPL PIVELPGIGK RQLDNAFKNN FHKIGDLAKC KDVTLFKRVF GIAWESLHAV ALGETYTQSE QDVKSRSIAV SETLEYLNYS SNQLQQKLTS IFNELYARLQ LSFQMCKGVV VQLKSNDFIV NSHSQSIKKY TADYQTLLVI VKKLFNRLLM GVGLNIRLIG VSFFGLKNNP SSSRPEGLLF YEYQQAKPKQ QTAHFALDQM IYEINQSFGY EIIQRAKKLA AS // ID Y565_MYCPN Reviewed; 152 AA. AC P75213; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG384.1 homolog; GN OrderedLocusNames=MPN_565; ORFNames=H03_orf152, MP277; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95925.1; -; Genomic_DNA. DR PIR; S73603; S73603. DR EnsemblBacteria; AAB95925; AAB95925; MPN_565. DR PATRIC; 20022609; VBIMycPne110_0627. DR OMA; FFLIRSK; -. DR OrthoDB; EOG664CF9; -. DR BioCyc; MPNE272634:GJ6Z-611-MONOMER; -. DR Proteomes; UP000000808; 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; IPR020375; Uncharacterised_MG384.1. DR ProDom; PD077269; Uncharacterised_MG384.1; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 152 Uncharacterized protein MG384.1 homolog. FT /FTId=PRO_0000210585. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. SQ SEQUENCE 152 AA; 17463 MW; 9E6E20296FA9748E CRC64; MGREVEPIFD LVLLWFLLVP LVVYALLLLL LFFTTPYLIV EAIPFCYGIA LMMISLFMSG MFPQAWNVWV IFGRFVLVLV VLMLSFFVIN KLTNLVLLRS RYAMVVAQGL VHTGKVKQQS QQAMSDIKTK WDKEKSKTVV VTIKKKRVKS SD // ID Y566_MYCPN Reviewed; 237 AA. AC P75212; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MG385 homolog; GN OrderedLocusNames=MPN_566; ORFNames=H03_orf237, MP276; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 GP-PDE domain. {ECO:0000305}. CC -!- SIMILARITY: To glycerophosphoryl diester phosphodiesterases CC (EC 3.1.4.46). {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG293. {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; U00089; AAB95924.1; -; Genomic_DNA. DR PIR; S73602; S73602. DR RefSeq; NP_110255.1; NC_000912.1. DR RefSeq; WP_010874923.1; NC_000912.1. DR ProteinModelPortal; P75212; -. DR EnsemblBacteria; AAB95924; AAB95924; MPN_566. DR GeneID; 876914; -. DR KEGG; mpn:MPN566; -. DR PATRIC; 20022611; VBIMycPne110_0628. DR KO; K01126; -. DR OMA; YQFYEND; -. DR OrthoDB; EOG6N0HGM; -. DR BioCyc; MPNE272634:GJ6Z-612-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.190; -; 1. DR InterPro; IPR004129; GlyceroP-diester-Pdiesterase. DR InterPro; IPR030395; GP_PDE_dom. DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl. DR PANTHER; PTHR23344; PTHR23344; 1. DR Pfam; PF03009; GDPD; 1. DR SUPFAM; SSF51695; SSF51695; 1. DR PROSITE; PS51704; GP_PDE; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MG385 homolog. FT /FTId=PRO_0000210587. FT DOMAIN 4 237 GP-PDE. SQ SEQUENCE 237 AA; 27716 MW; D0EE0A302F07F2C8 CRC64; MRKQFLIAHR GYSTIAPENT HLAFAAAQLF GFDGLWMEVQ LTKDKQIVVT NLDNYKVGNK THKLSDINLV NLKKINLAKQ FKVNVQEQTI LTLKEVLMEF LTPFRFLLLF IKGEEEQQNQ VLVEQLAQLL EGFELAKEKL ILLSSHFSTI KYLNEKLKSF KTSFVFNSKK QLVHLTKDEI TQNCRFLAPN DSFYHKNCAE LQSYGLPIIL WVIKGLLRYQ FYENDRFVKF QIAAQLY // ID Y583_MYCPN Reviewed; 225 AA. AC P75197; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 64. DE RecName: Full=Uncharacterized protein MPN_583; GN OrderedLocusNames=MPN_583; ORFNames=D02_orf225L, MP259; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95907.1; -; Genomic_DNA. DR PIR; S73585; S73585. DR RefSeq; NP_110272.1; NC_000912.1. DR RefSeq; WP_010874940.1; NC_000912.1. DR EnsemblBacteria; AAB95907; AAB95907; MPN_583. DR GeneID; 876816; -. DR KEGG; mpn:MPN583; -. DR PATRIC; 20022645; VBIMycPne110_0645. DR OrthoDB; EOG6DVJR7; -. DR BioCyc; MPNE272634:GJ6Z-629-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022382; DUF31. DR Pfam; PF01732; DUF31; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MPN_583. FT /FTId=PRO_0000210732. SQ SEQUENCE 225 AA; 25895 MW; 27BA3CE4783093D6 CRC64; MPNNAQAFVN VQTTVIPKTA FTAHDFVNYT LPKDKKKQND TENKKKQPKD GENDKQKEQA ETQPFEWIQQ KDADDKKESN TANTSDSLAY ADFAVLELTL FLDNPVDKKV FDHFIQPAIK TYEQLGNSLK LFAKPTLTEL KNHRYYLSGY PFLENKVNVL SVNQIKKDTS TETTINGQTV QQSNHEQPLI VRSTIAKPTL IRNQGDDFNG SNWVWNYDNS RVFRF // ID Y623_MYCPN Reviewed; 450 AA. AC P75172; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Probable ATP-dependent RNA helicase MG425 homolog; DE EC=3.6.4.13; GN OrderedLocusNames=MPN_623; ORFNames=C12_orf450, MP219; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95867.1; -; Genomic_DNA. DR PIR; S73545; S73545. DR RefSeq; NP_110312.1; NC_000912.1. DR RefSeq; WP_010874980.1; NC_000912.1. DR ProteinModelPortal; P75172; -. DR IntAct; P75172; 3. DR EnsemblBacteria; AAB95867; AAB95867; MPN_623. DR GeneID; 877188; -. DR KEGG; mpn:MPN623; -. DR PATRIC; 20022729; VBIMycPne110_0687. DR OMA; QQIDVEM; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; MPNE272634:GJ6Z-669-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 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; 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; 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; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 450 Probable ATP-dependent RNA helicase MG425 FT homolog. FT /FTId=PRO_0000055115. FT DOMAIN 34 206 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 234 384 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 47 54 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 3 31 Q motif. FT MOTIF 154 157 DEVD box. SQ SEQUENCE 450 AA; 51245 MW; 4CEBA56788821185 CRC64; MDSTFNELGV SPALIATLKD NNINQPTTIQ QLAIPQFLQH QNLIVHSPTG TGKTAVFGIP VIETLLKKPS KGTTQTLVVA PTRELAEQIK TTFINFAKHT HLKVVSLIGG IPIWQQLKQL ENQPEIVVGT MGRVMDLLER GVIKFEHLEH LIIDEVDLML DRGFKRKLFD LLSRIEKFEQ IAVYSASYNE ETIETAKQIT KNGIFLAAPE LKQNAPEPDN KLIDQFVCYL FSNRKKQALY SLVSQTRAKS IIVFCDTKKL VDELCIFLRK NDVKTYPLHG DKAQFIRERN LKLFANTTAP IVLVTTDLIG RGIHVEGVDM VVNYSACVNF ETYLHRMGRT GRNNHKGSCI TFCTSHEKQA FLKLLEQVND KRISPLRPMR LRLIPLKCKT QPKKGKLSLQ SVQKIYVNPR SNGTFKRVPL AGDLFKSRMR QPERDMQKNK LHDSDWQSNM // ID Y639_MYCPN Reviewed; 283 AA. AC P75158; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 20-JAN-2016, entry version 69. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 6; DE Flags: Precursor; GN OrderedLocusNames=MPN_639; ORFNames=E09_orf287o, MP203; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB95851.1; 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; U00089; AAB95851.1; ALT_INIT; Genomic_DNA. DR PIR; S73529; S73529. DR RefSeq; NP_110328.1; NC_000912.1. DR EnsemblBacteria; AAB95851; AAB95851; MPN_639. DR GeneID; 876994; -. DR KEGG; mpn:MPN639; -. DR PATRIC; 20022759; VBIMycPne110_0702. DR BioCyc; MPNE272634:GJ6Z-685-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 283 Uncharacterized lipoprotein MG439 homolog FT 6. FT /FTId=PRO_0000014048. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 283 AA; 31865 MW; E3F6CD684CA47187 CRC64; MALKLRKWIW ASIPSLALIL SSCSALVASV ELKSLSELQN LADRNTELTK NKRTLITTLR ESYGLNPKGT LNLLFEGWRY TLLSQRILER WQTEVGRFAK SFGNGSNQNS VQPNATLKGL KLSERSTTEI QLLAEQAITV SKQEVKEFTY KVESNKQFEA TVKIKADLKI DPTKAMSHIE NIFKDDETKK KDAQNSLTMS MGQNEALEAT FTYSPATQGI FGRASFDRFT SNIKLNTKLR IQVSSTSDLM KKLLENSLTS SLKDQSFDNE GVNLFPYTLF ALL // ID Y646_MYCPN Reviewed; 277 AA. AC P75151; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized lipoprotein MG440 homolog 1; DE Flags: Precursor; GN OrderedLocusNames=MPN_646; ORFNames=E09_orf277, MP196; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95844.1; -; Genomic_DNA. DR PIR; S73522; S73522. DR RefSeq; NP_110335.1; NC_000912.1. DR RefSeq; WP_010875003.1; NC_000912.1. DR EnsemblBacteria; AAB95844; AAB95844; MPN_646. DR GeneID; 877022; -. DR KEGG; mpn:MPN646; -. DR PATRIC; 20022773; VBIMycPne110_0709. DR OMA; FENNSEG; -. DR OrthoDB; EOG62K24M; -. DR BioCyc; MPNE272634:GJ6Z-692-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 277 Uncharacterized lipoprotein MG440 homolog FT 1. FT /FTId=PRO_0000014050. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 277 AA; 31097 MW; A17DC45BED6D3065 CRC64; MNKKSIWSKT AFGSLFLLLG TAFTACSNYD FQANLTSLNQ LRTSANKDIN LTQDKNTLID ALKTAFENNS EGTTKVLLDA WKFSLYDAKI LEKQDPVKFV KAFGSGKSKE DIEPSAGVRG LRFVERFGDN TASLIKNAIL LDQQKVEVFN IRFKSSRDFT IQIKLNAKGN YKKSEVEKYK SQIGVQDNEL GDKEEGTLEA DLIFTYTPPA SNLFSKSNFD KLTKSINFNT NLKLEMVGKD EVMRKILNSS AFTNNLASVN YPNQAVNLLP YVLYSIL // ID Y673_MYCPN Reviewed; 169 AA. AC P75118; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MG459 homolog; GN OrderedLocusNames=MPN_673; ORFNames=K05_orf169, MP169; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95817.1; -; Genomic_DNA. DR PIR; S73495; S73495. DR RefSeq; NP_110362.1; NC_000912.1. DR RefSeq; WP_010875030.1; NC_000912.1. DR ProteinModelPortal; P75118; -. DR EnsemblBacteria; AAB95817; AAB95817; MPN_673. DR GeneID; 877015; -. DR KEGG; mpn:MPN673; -. DR PATRIC; 20022835; VBIMycPne110_0740. DR OMA; DYKHAIF; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; MPNE272634:GJ6Z-719-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:InterPro. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.50; -; 1. DR InterPro; IPR003526; MECDP_synthase. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein MG459 homolog. FT /FTId=PRO_0000210628. SQ SEQUENCE 169 AA; 19467 MW; B15A9B8DA3120FBE CRC64; MQFRVGLGKK KYRIKPRAEQ KNKFWIGGVE IEDSKYIYDH DASDDASDVI QLAVADALFG ATALGDGQIV FNKEKTQIPL KGNPRKEAPR ILARTYNFIR KNWYINNIDI TLEIPSQQKM DDYKHAIFDF ICTALRITEL TINLKVREPL NPNEISCLAV VLVERQRLK // ID Y676_MYCPN Reviewed; 106 AA. AC P75116; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 51. DE RecName: Full=Uncharacterized protein MPN_676; GN OrderedLocusNames=MPN_676; ORFNames=K05_orf106, MP166; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95814.1; -; Genomic_DNA. DR PIR; S73492; S73492. DR IntAct; P75116; 1. DR EnsemblBacteria; AAB95814; AAB95814; MPN_676. DR BioCyc; MPNE272634:GJ6Z-722-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 106 Uncharacterized protein MPN_676. FT /FTId=PRO_0000210704. SQ SEQUENCE 106 AA; 12407 MW; 0EA13580DA2F0CB9 CRC64; MAWRLWSTTL KVSLTSTLKS LNSASMFANL RSTMTLHSSN SFRVTYYVFG FFTFRWQRSL IITSKVPSGN GIQFDFNSRT SHWLLNFLYS LSEYHLLFKV KTPFLT // ID Y433_MYCPN Reviewed; 270 AA. AC P75355; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Putative ABC transporter ATP-binding protein MG304 homolog; GN OrderedLocusNames=MPN_433; ORFNames=A05_orf270L, MP408; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96056.1; -; Genomic_DNA. DR PIR; S73734; S73734. DR RefSeq; NP_110121.1; NC_000912.1. DR RefSeq; WP_010874789.1; NC_000912.1. DR ProteinModelPortal; P75355; -. DR EnsemblBacteria; AAB96056; AAB96056; MPN_433. DR GeneID; 876836; -. DR KEGG; mpn:MPN433; -. DR PATRIC; 20022262; VBIMycPne110_0468. DR KO; K16786; -. DR OMA; KLPMIIC; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MPNE272634:GJ6Z-462-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 270 Putative ABC transporter ATP-binding FT protein MG304 homolog. FT /FTId=PRO_0000093246. FT DOMAIN 2 232 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 270 AA; 30770 MW; 6512640E4BC051B4 CRC64; MLNVTNLSFT YPRHSQPALK KLNFSLKPNT HVAIIGHNGS GKSTLVKLLG GFLKAPKQTI FFRGQPLEEV GFRQIGILLQ DPDMQLLGDT LHQELIFSLE NHGVDPKQMD RVIADVLAVV ELQGKQFTPL SKLSFGEKQR AVFACLLAVK PELYLLDEAF SMLDGKLASK LKRFIFKVIK EQQKTVINVT HDFNDLFLAD EIIFLSKGQL LKQFSPAAIY KQLHLFHQHH FTLPFPWLLA HEVADHLHHE MKGPIEELQD VVDWICKHLK // ID Y436_MYCPN Reviewed; 1244 AA. AC P75342; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized lipoprotein MG307 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_436; ORFNames=A05_orf1244, MP405; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96053.1; -; Genomic_DNA. DR PIR; S73731; S73731. DR RefSeq; NP_110124.1; NC_000912.1. DR RefSeq; WP_010874792.1; NC_000912.1. DR IntAct; P75342; 1. DR EnsemblBacteria; AAB96053; AAB96053; MPN_436. DR GeneID; 876848; -. DR KEGG; mpn:MPN436; -. DR PATRIC; 20022268; VBIMycPne110_0471. DR OMA; WYENNED; -. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MPNE272634:GJ6Z-465-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 1244 Uncharacterized lipoprotein MG307 FT homolog. FT /FTId=PRO_0000014031. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1244 AA; 139117 MW; BBDAF1AED587882A CRC64; MKKFLRKPQF WLLTLGGFLS TSVILAACAT PSNSALQTVF KARSSQFFNG EQGSLQSALT TALKNPVANK QFIAAPLLKA LEAWYENNED KKITQFLKDT KSNVDSQYTT AVDKVVSASR NKSLFVQQDL LDNAGGSEAT WKAQKLLEQL ISDFASRVFQ KNYLNYKKDG QVSTGPFTYD ELHKEESWKN FEFSAPRFSE TNDDFFAKIQ SQVFDQWVEY TDPTLISQVN YKYSAPSQGL GQIYNREKLK DKLTPSYAFP FFAEEKDIAP NQNVGNKRWK QLVKGEGAIT DNNIGQSGTN SQKTGLLKYR NESNKGDFLD FPLNLSDTNE TKQLVDASNI VDQLEAANLG AALNLKLQVF EQDNDELPQI KELKEDLNNT IVVDKSKDVE KASKTNALFY NDQEGKQQQS DSDPIAGALD DIFAQNTSEG TNLSKLAEQV KKAAATKMEA KTAVLRTNNS KGQQNNYVVL DAAIPTFNST TSKSKNNSAS NEVLVALKSG SINLRQVQQT DQNSYSPIKF RIVRNSTGVT VFGLDGGSYY LKQDSTNKKS VSKQSLTLLT KSSSGNSNKV LRDLDKQKQF LKFRAFQAKT NTFYSTNFAF SFPLNETLKS WFDKHRELIL ANALVNASLD QKDKASKALT EAFNPYKELI KEFAPVALAT TMISFYFDQM KALNNKLLER ARNLNQNVNQ ANPTPWLNGL SAKLPYVNTN GNYEKLNNYF TFLITKTLWP KVGQEETSIS EESNKLKTKT ADVDKIRDKI LENIQTKVND FVKNKLKPAL APRPAYSNVI LLNVNNDKVL SSGANWSLAS LLQSDKVNPL SFMLLKQAFD NNDLFKKAQK LFKDIQEKSS NNGGMQSSST TNSDADALSK VIGNYYYTTW AKLTDKSIYG NPKDNKFDEL FKLAFEASID EKSFNVDYKA VIDHYRFIYT LQWLVDQKLK NFKSLLKTNL KFGEVAFIAY KNTETTNFSN PQGVFGSYFN YENSASEVKE STQTLDPNNF FYKTTTKPTV QAIQQVASLA LVQKQQMQQN STDHYGFTGL STSTSSMFDA SSRDAILQQI TKTSLQQYGS KDQLKKIIQG TNNQLLLDRI AVQLSGLNPS TTNGGSGKTI ATYFQVDAVG NPTLDFQAKR KLLLDLLDQY QNYFGNGAQK SQRDSTPSGT GNYLTYQNGS DKYTYTQFTY QDIDSLSLTT TSGTNNKIAS DVVAALLLFQ AADKGTQQLA LSAINKPQLN IGDKRIESGL KLLK // ID Y437_MYCPN Reviewed; 572 AA. AC P75341; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MPN_437; GN OrderedLocusNames=MPN_437; ORFNames=H08_orf572o, MP404; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; U00089; AAB96052.1; -; Genomic_DNA. DR PIR; S73730; S73730. DR IntAct; P75341; 1. DR EnsemblBacteria; AAB96052; AAB96052; MPN_437. DR PATRIC; 20022272; VBIMycPne110_0473. DR OMA; MGANWAL; -. DR BioCyc; MPNE272634:GJ6Z-466-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 572 Uncharacterized protein MPN_437. FT /FTId=PRO_0000210675. SQ SEQUENCE 572 AA; 64220 MW; 2B82223F88CFF0B4 CRC64; MINFLFNQMN ALNNKFLERA KALNQNVNQA NPTPWLNGLS AKLPYVRTNG NYEKLNNYFT FLIVKYMWKK VGNEDASLSK DSSINKLKTK TEDVNKIRDK ILEDIQKKVQ EFVKNKLKPT LAPRQTYSNV ILLNVNNDKV WSMGANWALA NLLDTSKINP LSFMLLKQTF DQNDLFKKAK KLFEDIQSKT NGGSSGGMQG SNTSSSEGAD ALSKVIGNYY YNSWAKLTDK SIYGNPKDNK FDDLFKLAFE DSINEKSFNV DYKAVIEHYR FIYTLEWLVN GNLKNFKDLL KANLKFGEIA FIAYKNTETK EFSNPQGVFG SAFNYENETN EVKIAAQNLD PNNFFYKTTT KPEEVKTAQN GASMMVMQQK MQSTMQDSNH YGFTGLNTST SSMLGAATQQ AILDQITKNS LQQYGSQQEL KTLIEKTNNQ LLLDRIASQL SGLNPSTTGN SNNGKGKNIA TYFQLDAIGN PTLSFQQKRK LLLDVLDQYK DFFGTNTQAA QRDSGKGGHG SYSTYQDGSD KITYLQFSYK DIDNLSLSDK GNSKLASDVV AALLLFQAAD KGTQQLALSA IN // ID Y443_MYCPN Reviewed; 409 AA. AC P75335; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable ATP-dependent RNA helicase MG308 homolog; DE EC=3.6.4.13; GN OrderedLocusNames=MPN_443; ORFNames=H08_orf409, MP398; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96046.1; -; Genomic_DNA. DR PIR; S73724; S73724. DR RefSeq; NP_110131.1; NC_000912.1. DR RefSeq; WP_010874799.1; NC_000912.1. DR ProteinModelPortal; P75335; -. DR IntAct; P75335; 1. DR EnsemblBacteria; AAB96046; AAB96046; MPN_443. DR GeneID; 877046; -. DR KEGG; mpn:MPN443; -. DR PATRIC; 20022284; VBIMycPne110_0479. DR OMA; NERKHIF; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; MPNE272634:GJ6Z-472-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 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 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; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 409 Probable ATP-dependent RNA helicase MG308 FT homolog. FT /FTId=PRO_0000055113. FT DOMAIN 26 179 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 190 349 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 39 46 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 126 129 DEVD box. SQ SEQUENCE 409 AA; 47001 MW; 02AC88B04F93A07C CRC64; MHFIQPLQAF LQTKHIVEFS SIQQAVFKVW PRQNVVGIAE TGSGKTFAYL LPALNQIDVT LNKPQAVVFV PTKELKWQIL TILNDIKASF TGLKVSENFN SNAHLIVSLI GKDIILHETI KYVVFDEVDM FLEDSSQAEW INCVQLFQKH KPHFGFFSAT LFNEQLQQIR KQVAPLTVVN QKKRAWKHSL VKHFLLNLNG QEPFAGLLAL LNYHHNEQVL VFCSNAKSLK QLTSLLAHNQ LSFKSLHGQL TPNERKHIFT SAANNTVRVL VVSDLLARGI DLPHFSVVIS WDLPLVDSFY IHRSGRVARF NSWGNSYVFD LPHNQHKLTK FAHKGILFNS VHLERDGTLK FPQLKQSKQK PAVSSELKTA IKRIKAGYKK VKPNYKKRQK QQIAELFAKR KQRRSWKNF // ID Y451_MYCPN Reviewed; 369 AA. AC Q50361; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MG316 homolog; GN OrderedLocusNames=MPN_451; ORFNames=H08_orf369, MP390; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8675025; DOI=10.1016/0378-1119(96)00050-9; RA Dirksen L.B., Proft T., Hilbert H., Plagens H., Herrmann R., RA Krause D.C.; RT "Sequence analysis and characterization of the hmw gene cluster of RT Mycoplasma pneumoniae."; RL Gene 171:19-25(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis ComEC. {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; L38997; AAA61693.1; -; Genomic_DNA. DR EMBL; U00089; AAB96038.1; -; Genomic_DNA. DR PIR; S73716; S73716. DR RefSeq; NP_110139.1; NC_000912.1. DR RefSeq; WP_010874807.1; NC_000912.1. DR EnsemblBacteria; AAB96038; AAB96038; MPN_451. DR GeneID; 877267; -. DR KEGG; mpn:MPN451; -. DR PATRIC; 20022300; VBIMycPne110_0487. DR OMA; QWVILAS; -. DR OrthoDB; EOG647TWC; -. DR BioCyc; MPNE272634:GJ6Z-480-MONOMER; -. DR Proteomes; UP000000808; 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; IPR004477; ComEC_N. DR Pfam; PF03772; Competence; 1. DR TIGRFAMs; TIGR00360; ComEC_N-term; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 369 Uncharacterized protein MG316 homolog. FT /FTId=PRO_0000210533. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255}. SQ SEQUENCE 369 AA; 43117 MW; CE66FA7481594333 CRC64; MKWKLFYFFT LLTFTPAYFF IEQNQWVILA SFLVIVNLIS LTVHWKFGLL LISCSAALLA YCQLMPEFQL AKLMKANWLR TPFISWLDQH TSGVFNQYLK LFLINETTKN TLYQSAIQLN IVHLFVISGF HLSFLFGVME RWLYKRFYIN KITGFVMLLL YLFLVGFAFS ALRVFVSKLL RQMFPKQLPE NNLGLTALLI ILMSPGALHN FGFNFSFLAC FVLFAINKVK LWKPLQAVLT STLILIVVSP ITLHLNRKLN ALSVFHNLLF TPIALFYFCA SWLLLPLIPW MGNSLVGFYW PLPWLSQWAL NTTVFLNLPK PNWVFYLVYY GLWGLLYTVG TVFYYDRSLW CRYWVNSPAV KPTAQPSRL // ID Y459_MYCPN Reviewed; 569 AA. AC P75324; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized lipoprotein MPN_459; DE Flags: Precursor; GN OrderedLocusNames=MPN_459; ORFNames=H08_orf591, MP382; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: To M.pneumoniae MPN_456 and M.genitalium MG321 N- CC terminal region. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96030.1; 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; U00089; AAB96030.1; ALT_INIT; Genomic_DNA. DR PIR; S73708; S73708. DR EnsemblBacteria; AAB96030; AAB96030; MPN_459. DR PATRIC; 20022324; VBIMycPne110_0496. DR OrthoDB; EOG6SFP68; -. DR BioCyc; MPNE272634:GJ6Z-491-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 569 Uncharacterized lipoprotein MPN_459. FT /FTId=PRO_0000014061. FT LIPID 25 25 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 25 25 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 569 AA; 63118 MW; 1CE6F077E15B13F3 CRC64; MKFQRKYWGL LSTLGVSSAV ALSACAAQAR DVYVTSSASD LLKNNLVPMS MFNVSPTSSF FGSKYAGLTT YIATGSNKDD GVNVTSQTQE KLVLELATSV KGYKKKTSTA SNMKTASVSS SSSSTGNNGS TEDEWEVVGS EIKRESGKGD NGKSITEDSN FQTISQQATR YEFTIDTSIK WVDNNGKPVK DEKGQEVKLS SKDFERGFEA YILSSELRFN RNGYFIDLMG LDVEKTVGMT NGKNGTQVKK MTTDSSSTQQ SEEKKIEITD DNYDPEDYRS TSDDKFNVYL TSPFPFLLSM MSKEFFFPIP HTHPKVKAIK VGPNSPLVYN EKNSAKILDQ TKTNFDGIYG GGGVNAWRDA WSVGPYYVES FNQSQIVFKR NKEYDDHITP NLPKTREGNE QPIPTMINYF QPGATPEVFY SNYIAGGLSS AGVSYSQQED ARSRFASTGD LRWVKVQKTA QSAQITYSSR PYILEGETVK TNSNITETEA KFLYNSESEE ALTIRAGING LINWQNLAII LLPNSGDLNY SIVPFGIFKE KGKDVQVKQK NTGQASQGSD LMNDYYYKI // ID Y461_MYCPN Reviewed; 231 AA. AC P75322; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized protein MG323 homolog; GN OrderedLocusNames=MPN_461; ORFNames=H08_orf231, MP380; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 RCK C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96028.1; -; Genomic_DNA. DR PIR; S73706; S73706. DR RefSeq; NP_110149.1; NC_000912.1. DR RefSeq; WP_010874817.1; NC_000912.1. DR ProteinModelPortal; P75322; -. DR IntAct; P75322; 2. DR EnsemblBacteria; AAB96028; AAB96028; MPN_461. DR GeneID; 877150; -. DR KEGG; mpn:MPN461; -. DR PATRIC; 20022342; VBIMycPne110_0498. DR KO; K03499; -. DR OMA; QLAKMNC; -. DR OrthoDB; EOG6HQSSJ; -. DR BioCyc; MPNE272634:GJ6Z-500-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 231 Uncharacterized protein MG323 homolog. FT /FTId=PRO_0000210540. FT DOMAIN 5 126 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 134 221 RCK C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. SQ SEQUENCE 231 AA; 25773 MW; B09F242FAC56CFE1 CRC64; MKRADFCIIG LGRFGMQVAH SLKENNFTLV LIDNDQHKTN TAAQEFDHVV CCDGSNLTAL AELQLEEFSA VIVGVTNIEA SIMICANLRE LGQKNIIARA KNEVHNRVLR TMGIREALIP EKIVGKNLVI RLIHGMETEI INLGNDILFV RAPVNNKKLF NRTLGEINIR EHTNANLISI MRNGKDVVFP LGPNTQIQPG DVITAVCQLS GVNQYLRYIN PNDKNKYKAS E // ID Y463_MYCPN Reviewed; 157 AA. AC P75320; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 60. DE RecName: Full=Uncharacterized protein MPN_463; GN OrderedLocusNames=MPN_463; ORFNames=H08_orf157a, MP378; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: To M.pneumoniae MPN_091 and MPN_413. {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; U00089; AAB96026.1; -; Genomic_DNA. DR PIR; S73704; S73704. DR RefSeq; NP_110151.1; NC_000912.1. DR RefSeq; WP_010874819.1; NC_000912.1. DR EnsemblBacteria; AAB96026; AAB96026; MPN_463. DR GeneID; 876798; -. DR KEGG; mpn:MPN463; -. DR BioCyc; MPNE272634:GJ6Z-502-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Uncharacterized protein MPN_463. FT /FTId=PRO_0000210682. SQ SEQUENCE 157 AA; 17842 MW; B7F5CCB853B95DB7 CRC64; MGGWMSCAPP IYTPHTNSWT ESGWDRTSWW RWSAQRWSGW SFKIVRANKA LRVMAKTKMP LVLIPPSPNK PYSKLAINQE LHLTPHKKTS PATSSSLKPR PGPRGYLNAR LSWRCPTLSR KVRVPTIKVP MVRAPSTKPS KTSSSNNPWP LTPRMRG // ID Y464_MYCPN Reviewed; 445 AA. AC P75319; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 29-APR-2015, entry version 62. DE RecName: Full=Putative MgpC-like protein MPN_464; GN OrderedLocusNames=MPN_464; ORFNames=H08_orf445, MP377; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB96025.1; -; Genomic_DNA. DR PIR; S73703; S73703. DR RefSeq; NP_110152.1; NC_000912.1. DR RefSeq; WP_010874820.1; NC_000912.1. DR EnsemblBacteria; AAB96025; AAB96025; MPN_464. DR GeneID; 876799; -. DR KEGG; mpn:MPN464; -. DR PATRIC; 20022346; VBIMycPne110_0500. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-503-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 445 Putative MgpC-like protein MPN_464. FT /FTId=PRO_0000210725. SQ SEQUENCE 445 AA; 48275 MW; 322C4E9892CFF0B7 CRC64; MAAVTDNQQS GDNNGLVSLA QRSTTVAVQK SDSSGSQGQG TTDNKFQKYL NTTQALHQMG VIVPSLETWP GKPSTGIATR AAGGVSVQAA TRQSTSTNED LSNVITQLYH TSTSQLAYLN GQIVVMGSDR VPSLWYWVVD ERTTSGRATW WAHTELNWGT DKQKQFVENQ LGFKDDSNSD SKNSNLKAQG LTQPAYLIAG LDVVADHLVF AAFKAGAVGY DMTTDSNAST KDQVLAWSTT AGLDSDGGYK ALVENTAGLN GPINGLFILL DTFAYVTPVS GMKGGSKNTE AVQTKYPVKD DSKASAKIAS LINASPLNSY GDDGVTVFDA LGLNFNFKLD EARLPSRTDQ LLVYGIVNES ELKSARENAQ STSDDNSNTK VKWTNTASHY LPVPYYYSAN FPEAGNRRRA EQRNGVITIK KAIYPEVRGR QLQNIFDDWK TNKSR // ID Y465_MYCPN Reviewed; 199 AA. AC P75318; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 70. DE RecName: Full=Uncharacterized protein MPN_465; GN OrderedLocusNames=MPN_465; ORFNames=MP376, P01_orf199; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.pneumoniae MPN_037. {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; U00089; AAB96024.1; -; Genomic_DNA. DR PIR; S73702; S73702. DR EnsemblBacteria; AAB96024; AAB96024; MPN_465. DR BioCyc; MPNE272634:GJ6Z-504-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 199 Uncharacterized protein MPN_465. FT /FTId=PRO_0000210683. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. SQ SEQUENCE 199 AA; 23170 MW; 7FCAC9DA043A490C CRC64; MAFLFISNEW KYQQLIFKIN CWHFCYYPKN YLGGSILSKR LFIPPSACRI DLSVFPWAFI CSPWNFCSTW SSLICSPCFS TVWVSLLICS PWRSTTWTNW LICSPCFSTV WVNLLICSPW AAKVVSIFVS RWLFEFLYSL NSLRVTYSVF TGITGLLSLN CLLNLPENST LLFSGLMMYQ PEKVPFLVFF TMSWNSFSL // ID Y499_MYCPN Reviewed; 163 AA. AC P75288; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MPN_499; GN OrderedLocusNames=MPN_499; ORFNames=MP344, P02_orf163; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95991.1; -; Genomic_DNA. DR PIR; S73670; S73670. DR RefSeq; NP_110187.1; NC_000912.1. DR RefSeq; WP_010874855.1; NC_000912.1. DR IntAct; P75288; 4. DR EnsemblBacteria; AAB95991; AAB95991; MPN_499. DR GeneID; 877262; -. DR KEGG; mpn:MPN499; -. DR PATRIC; 20022430; VBIMycPne110_0542. DR OMA; ENIVILW; -. DR OrthoDB; EOG63C0SS; -. DR BioCyc; MPNE272634:GJ6Z-540-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR020324; Uncharacterised_MPN499. DR ProDom; PD095699; Uncharacterised_MPN499; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 163 Uncharacterized protein MPN_499. FT /FTId=PRO_0000210688. SQ SEQUENCE 163 AA; 19095 MW; 10CE2D2F077DFEAC CRC64; MVKMLTMDKI LSKKIKVNWL GGVFWLLPNL LDLFSASKRK ASVRPYQSLL ELVQENFLNR YDLVHFSFNG DHDFFHFNDL QAIRSFNFTI EEEQLGAMQP DEVLLFEPVD RVTVELDQKG LSLIHSGKAF CASANYFKHW LKRVPQQDKV TLVWRKSGFE LKQ // ID Y503_MYCPN Reviewed; 381 AA. AC P75283; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Putative MgpC-like protein MPN_503; GN OrderedLocusNames=MPN_503; ORFNames=MP339, P02_orf381; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MgpC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; U00089; AAB95987.1; -; Genomic_DNA. DR PIR; S73665; S73665. DR EnsemblBacteria; AAB95987; AAB95987; MPN_503. DR PATRIC; 20022446; VBIMycPne110_0550. DR OrthoDB; EOG6WQDBQ; -. DR BioCyc; MPNE272634:GJ6Z-544-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 381 Putative MgpC-like protein MPN_503. FT /FTId=PRO_0000210726. SQ SEQUENCE 381 AA; 40896 MW; 5CFD05505E344852 CRC64; MNGVAQDKVH GLEQTTQWNQ QASQKNLTNN PAPKAVTGFK LDKGRAYRKL NEAWPVYEPL DSTKDGKGKD KDGWTTSGAS EPKGDAPLVS STESQMAAVT DSQQSGHNSG LVSLAQRSTT VAVQKSDSSG SQGQGTTDNK FQKYLNTAQA LHQMGVIVPS LETWPGKPST GIATRAGGGV SVQAATRQSS STNEDLPNVI TQLYHTSTSQ LAYLNGQIVV MGSNAVPSLW YWVVDERTTS GRATWWAHTE LNWGTDKQKQ FVENQLGFKD DSNSSLTNFK SQGLTQPAYL IAGLDVVQDH LVFAAFKAGA VGYDMTTDSN ASTKDQALAW STTAGLDSAG GYNKLVENTG GLNGPINELV YPARHLCLCD PGEWDERGES E // ID Y511_MYCPN Reviewed; 260 AA. AC P75275; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAY-2015, entry version 50. DE RecName: Full=Uncharacterized protein MPN_511; GN OrderedLocusNames=MPN_511; ORFNames=F04_orf260V, MP331; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; U00089; AAB95979.1; -; Genomic_DNA. DR PIR; S73657; S73657. DR RefSeq; NP_110199.1; NC_000912.1. DR RefSeq; WP_010874867.1; NC_000912.1. DR EnsemblBacteria; AAB95979; AAB95979; MPN_511. DR GeneID; 876809; -. DR KEGG; mpn:MPN511; -. DR PATRIC; 20022472; VBIMycPne110_0563. DR BioCyc; MPNE272634:GJ6Z-552-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR Pfam; PF03072; DUF237; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 260 Uncharacterized protein MPN_511. FT /FTId=PRO_0000215258. SQ SEQUENCE 260 AA; 30422 MW; 85B7FD19D955FB6E CRC64; MQAFKEYWQK QKKDVTDKKQ LLEALKLSFA KEQNKTFAFL IKNFQDGISN YYPNDQEDQS EAAKTAFGTQ GIAFPQSGLK GIFMSEWLRK QLGEKAKINL DIKSLKVTDS KISPTIKWNK DIGIKRNQDK PYNFRFEIDI EYQGNYKLSW LEAIIAKFSG IPGEWKGKLN LKFIVDGDLS WEIVQKPDYP GSLFQFDDQK QQLLFKLHVW EKITVQEPEF MELIKSQNLH NLELRTESTK PPVVDLASYL HYQLLKLNQQ // ID Y518_MYCPN Reviewed; 348 AA. AC P75269; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MG343 homolog; GN OrderedLocusNames=MPN_518; ORFNames=G12_orf348, MP324; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95972.1; -; Genomic_DNA. DR PIR; S73650; S73650. DR RefSeq; NP_110206.1; NC_000912.1. DR RefSeq; WP_010874874.1; NC_000912.1. DR IntAct; P75269; 1. DR EnsemblBacteria; AAB95972; AAB95972; MPN_518. DR GeneID; 876959; -. DR KEGG; mpn:MPN518; -. DR PATRIC; 20022494; VBIMycPne110_0574. DR OMA; NCICLLE; -. DR OrthoDB; EOG60CWQ3; -. DR BioCyc; MPNE272634:GJ6Z-559-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 348 Uncharacterized protein MG343 homolog. FT /FTId=PRO_0000210552. SQ SEQUENCE 348 AA; 40716 MW; FE23C1409FDC47EE CRC64; MAQTTINEQT LVNEQRLLAY DCFQNTNKVG LLSALEYLDF VNHLVKSNQI KYLLVPSASQ TVYQHVFFDH FRFLSFDNNL LSGFGLAIRL HKEAETVFML VEKTKQTETE IKKLLEAVKQ FSGLKLVVLL VNSPFENKRT KLSYEIVKII KKHGYQYKRY CRKNFEKKFF NTWNHQKRKQ KTKNNLFFVE LNSQFAFGTS MANSNSFDLS FTSFKERFNT ENNLDIDVHF NVPHKYLLKN LESIKHHLQI DNNTIWKQAF INFAGQLLLY FENLQVFAQE ASTLQVNAIV IKQDAYFIVE VMKGYNYDNN CICLLEANKD QNVGLTTAST NTLIGDIKQY EPCFFIEK // ID Y523_MYCPN Reviewed; 305 AA. AC P75255; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized lipoprotein MG348 homolog; DE Flags: Precursor; GN OrderedLocusNames=MPN_523; ORFNames=G12_orf305, MP319; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95967.1; -; Genomic_DNA. DR PIR; S73645; S73645. DR RefSeq; NP_110211.1; NC_000912.1. DR RefSeq; WP_010874879.1; NC_000912.1. DR EnsemblBacteria; AAB95967; AAB95967; MPN_523. DR GeneID; 876839; -. DR KEGG; mpn:MPN523; -. DR PATRIC; 20022508; VBIMycPne110_0580. DR OMA; YSTITDE; -. DR OrthoDB; EOG60SCM0; -. DR BioCyc; MPNE272634:GJ6Z-565-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 29 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 30 305 Uncharacterized lipoprotein MG348 FT homolog. FT /FTId=PRO_0000014039. FT LIPID 30 30 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 30 30 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 305 AA; 33536 MW; 38A143D603F4BBE3 CRC64; MKKWFSSISK KKVSFSTLLL LGSGIVLSSC SNIDKPNVFR TLSQQSVENK VDYSKLPKEN KTVRNLVFGT AEYNDGNYVL VVTTETDSSQ INFLNGSNNQ AVSTENWAGD LGTTVKQVQN RYSTYPKGVK FLIWNDIDPN PVKWNPFARY PVIASDNELA KQTDKDNSDK LRRNDESAIQ YREIVTFIQT VYSGSVNNLI NQSNVHAQTV GTDVTKAIVI AFRKNNLDQI SAHFYNPDNS NGSNAPGSNQ PNQDSGNNGS TTPAAPAAAA AKKSYSAGSF GVKRHAVQVS INFLNFLDSV YTPLN // ID Y524_MYCPN Reviewed; 168 AA. AC P75254; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0134 protein MPN_524; GN OrderedLocusNames=MPN_524; ORFNames=G12_orf168, MP318; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the UPF0134 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; U00089; AAB95966.1; -; Genomic_DNA. DR PIR; S73644; S73644. DR RefSeq; NP_110212.1; NC_000912.1. DR RefSeq; WP_010874880.1; NC_000912.1. DR ProteinModelPortal; P75254; -. DR IntAct; P75254; 1. DR EnsemblBacteria; AAB95966; AAB95966; MPN_524. DR GeneID; 876879; -. DR KEGG; mpn:MPN524; -. DR PATRIC; 20022514; VBIMycPne110_0582. DR OMA; DKIENRM; -. DR BioCyc; MPNE272634:GJ6Z-567-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR002862; DUF16. DR Pfam; PF01519; DUF16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 168 UPF0134 protein MPN_524. FT /FTId=PRO_0000221612. SQ SEQUENCE 168 AA; 20110 MW; 0878B81DEB019170 CRC64; MKEKISEKEY KALIRKIGKE HFDGEKEEYG DGTVGVWTYE LRKYKLKPPV KVKYVTQEQF QEYKDSNNQR LIKIETTLAA QGEQIRIQVE QIKELQIEQK AQGETLKLIL QTLQKMSDRL DKMEVKMDKM EEKMDKMEGK IDKIENRMDK MEVKMDKMEK RIDKLESK // ID Y534_MYCPN Reviewed; 140 AA. AC P75244; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 49. DE RecName: Full=Uncharacterized protein MPN_534; GN OrderedLocusNames=MPN_534; ORFNames=G12_orf140b, MP308; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95956.1; -; Genomic_DNA. DR PIR; S73634; S73634. DR RefSeq; NP_110223.1; NC_000912.1. DR RefSeq; WP_010874891.1; NC_000912.1. DR EnsemblBacteria; AAB95956; AAB95956; MPN_534. DR GeneID; 877374; -. DR KEGG; mpn:MPN534; -. DR PATRIC; 20022545; VBIMycPne110_0596. DR BioCyc; MPNE272634:GJ6Z-579-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MPN_534. FT /FTId=PRO_0000210693. SQ SEQUENCE 140 AA; 16381 MW; 4A601D739B3FEF81 CRC64; MNTFKETLFS LKKSNYLLNE SAQILNDCVV NNNEIDERLR NSIKFALGII NLASYCLKNE QEQLDHELNH GNEAPWEFSF NEAEQLIECT VKNNFGNEKL VDLIFHIGDA METYRTTNIK FRVPKSYYDA KQQIRKVIKN // ID Y555_MYCPN Reviewed; 193 AA. AC P75223; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Uncharacterized protein MG377 homolog; GN OrderedLocusNames=MPN_555; ORFNames=H03_orf193o, MP287; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95935.1; -; Genomic_DNA. DR PIR; S73613; S73613. DR RefSeq; NP_110244.1; NC_000912.1. DR RefSeq; WP_010874912.1; NC_000912.1. DR PDB; 1ZXJ; X-ray; 2.80 A; A/B/C/D=1-193. DR PDBsum; 1ZXJ; -. DR ProteinModelPortal; P75223; -. DR SMR; P75223; 4-190. DR IntAct; P75223; 2. DR EnsemblBacteria; AAB95935; AAB95935; MPN_555. DR GeneID; 877212; -. DR KEGG; mpn:MPN555; -. DR PATRIC; 20022587; VBIMycPne110_0617. DR OMA; YHELTHI; -. DR OrthoDB; EOG6F55F3; -. DR BioCyc; MPNE272634:GJ6Z-600-MONOMER; -. DR EvolutionaryTrace; P75223; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR SUPFAM; SSF109998; SSF109998; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 193 Uncharacterized protein MG377 homolog. FT /FTId=PRO_0000210581. FT STRAND 8 11 {ECO:0000244|PDB:1ZXJ}. FT STRAND 21 23 {ECO:0000244|PDB:1ZXJ}. FT HELIX 30 41 {ECO:0000244|PDB:1ZXJ}. FT HELIX 49 73 {ECO:0000244|PDB:1ZXJ}. FT HELIX 74 76 {ECO:0000244|PDB:1ZXJ}. FT STRAND 77 80 {ECO:0000244|PDB:1ZXJ}. FT HELIX 83 95 {ECO:0000244|PDB:1ZXJ}. FT HELIX 104 127 {ECO:0000244|PDB:1ZXJ}. FT HELIX 133 146 {ECO:0000244|PDB:1ZXJ}. FT HELIX 152 155 {ECO:0000244|PDB:1ZXJ}. FT HELIX 158 179 {ECO:0000244|PDB:1ZXJ}. FT STRAND 183 185 {ECO:0000244|PDB:1ZXJ}. SQ SEQUENCE 193 AA; 22434 MW; 6794C97B3DCEE778 CRC64; MATNLKSTAK LVKPIQYDEV IEVERIFADP AFIEQHRQRI LASFKDAKES ALYHELTHIV IKDNLFSCAM NAIVGYFEFN IDEAELKNVM EGLKRDVIQG AEDNTVQAIA EKIIKKALVF NHLQKEWKVE ITDEVVKNVI SLYYEKTNQS VREYLDDKQK FEGVRTALLE ERMVLETINH FKFHFNLTGQ LPN // ID Y579_MYCPN Reviewed; 109 AA. AC P75201; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JUN-2015, entry version 66. DE RecName: Full=Uncharacterized protein MPN_579; GN OrderedLocusNames=MPN_579; ORFNames=D02_orf109, MP263; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95911.1; -; Genomic_DNA. DR PIR; S73589; S73589. DR RefSeq; NP_110268.1; NC_000912.1. DR RefSeq; WP_010874936.1; NC_000912.1. DR EnsemblBacteria; AAB95911; AAB95911; MPN_579. DR GeneID; 876800; -. DR KEGG; mpn:MPN579; -. DR PATRIC; 20022635; VBIMycPne110_0640. DR BioCyc; MPNE272634:GJ6Z-625-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 109 Uncharacterized protein MPN_579. FT /FTId=PRO_0000210696. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. SQ SEQUENCE 109 AA; 12793 MW; D61B890EC1C95896 CRC64; MENKEQNNTD QLQTGDLNKA RKLHKCYLWL FVVSLIIWLG FISLFFLYYL PISLVIALVV IAFIFVLVFL GFLETWRKNI NQEEEFLRLE GLLITSPTDT QSAIHKDNQ // ID Y608_MYCPN Reviewed; 225 AA. AC P75187; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MG409 homolog; GN OrderedLocusNames=MPN_608; ORFNames=C12_orf225, MP234; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95882.1; -; Genomic_DNA. DR PIR; S73560; S73560. DR RefSeq; NP_110297.1; NC_000912.1. DR RefSeq; WP_010874965.1; NC_000912.1. DR ProteinModelPortal; P75187; -. DR EnsemblBacteria; AAB95882; AAB95882; MPN_608. DR GeneID; 877098; -. DR KEGG; mpn:MPN608; -. DR PATRIC; 20022697; VBIMycPne110_0671. DR KO; K02039; -. DR OMA; STWIISK; -. DR OrthoDB; EOG63FW0S; -. DR BioCyc; MPNE272634:GJ6Z-654-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro. DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IEA:InterPro. DR InterPro; IPR028366; P_trasport_PhoU. DR InterPro; IPR026022; PhoU_dom. DR Pfam; PF01895; PhoU; 2. DR TIGRFAMs; TIGR02135; phoU_full; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MG409 homolog. FT /FTId=PRO_0000210597. SQ SEQUENCE 225 AA; 26856 MW; 545A6A1144507E20 CRC64; MESINYQILK RSEKKLLGLF FDYFQHVIKM HETLNKLLCE ADVTKREKLI QAIYEMEDFS NKSEFKLINE SIWAISKNSP LTNHLRLTIT IIMCSRDLER ICDYANNLTK FVKHYQHLDV SIFSKLVNLH KSVLNNLKQT FASLQDKEKP LTIQFENVTK ILTEFEQQYR VVLTEYYDKV KDEKLSDRIF LIDLILSVKH IERINDYCYN IIKAFLFVKN PEVFN // ID Y630_MYCPN Reviewed; 404 AA. AC P75166; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MG432 homolog; GN OrderedLocusNames=MPN_630; ORFNames=C12_orf404, MP212; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95860.1; -; Genomic_DNA. DR PIR; S73538; S73538. DR RefSeq; NP_110319.1; NC_000912.1. DR RefSeq; WP_010874987.1; NC_000912.1. DR EnsemblBacteria; AAB95860; AAB95860; MPN_630. DR GeneID; 876776; -. DR KEGG; mpn:MPN630; -. DR PATRIC; 20022743; VBIMycPne110_0694. DR OMA; IHIACLL; -. DR OrthoDB; EOG6TR0BM; -. DR BioCyc; MPNE272634:GJ6Z-676-MONOMER; -. DR Proteomes; UP000000808; 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; IPR019264; DUF2179. DR InterPro; IPR003740; YitT. DR Pfam; PF10035; DUF2179; 1. DR Pfam; PF02588; YitT_membrane; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 404 Uncharacterized protein MG432 homolog. FT /FTId=PRO_0000210611. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TRANSMEM 272 292 Helical. {ECO:0000255}. SQ SEQUENCE 404 AA; 45989 MW; 2627C0B1B21D4E47 CRC64; MQDKNVKIQG NLVRVHLSGS FLKFQAIYKV KKLYLQLLIL SVIAFFWGLL GVVFVQFSGL YDIGIASISQ GLARLADYLI RSNKVSVDAD TIYNVIFWLS QILINIPLFV LGWYKISKKF TLLTLYFVVV SNVFGFAFSY IPGVENFFLF ANLTELTKAN GGLEQAINNQ GVQLIFWEQT AEKQISLMFY ALIWGFLQAV FYSVILIIDA SSGGLDFLAF WYSEKKHKDI GGILFIVNTL SFLIGYTIGT YLTGSLLAQG FQEDRQKPFG VAFFLSPNLV FTIFMNIILG IFTSYFFPKY QFVKVEVYGK HMEQMRNYLL SSNQSFAVTM FEVEGGYSRQ KNQVLVTNCL FTKTAELLEA VRRVDPDALF SITFIKKLDG YIYERKAPDK VVPPVKDPVK AQEN // ID Y640_MYCPN Reviewed; 300 AA. AC P75157; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 5; DE Flags: Precursor; GN OrderedLocusNames=MPN_640; ORFNames=E09_orf300, MP202; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95850.1; -; Genomic_DNA. DR PIR; S73528; S73528. DR RefSeq; NP_110329.1; NC_000912.1. DR RefSeq; WP_010874997.1; NC_000912.1. DR IntAct; P75157; 2. DR EnsemblBacteria; AAB95850; AAB95850; MPN_640. DR GeneID; 877026; -. DR KEGG; mpn:MPN640; -. DR PATRIC; 20022761; VBIMycPne110_0703. DR OMA; SINFPAN; -. DR OrthoDB; EOG69PQBN; -. DR BioCyc; MPNE272634:GJ6Z-686-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 300 Uncharacterized lipoprotein MG439 homolog FT 5. FT /FTId=PRO_0000014047. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 300 AA; 32975 MW; 09B4884317941277 CRC64; MKLKLLLIPL LGSSLLLSAC SSATSQVISS LSSAQKYFEA NKGELNKKNV INILKDGYNS DPNKTVNALL AGWKYTLMDQ KLLERNLDAS RFASAFGSTS KKDDITPNIS EKSLFLADTF PGISSEIAKV FKVEKQTVSG FSYSWNSPKK FQVNIQIKMD GKIDESSKAL IKSFLEGNSS GGKGSNGKNS IDESEYTGEK AKFTGNFIFT YTPPTGGARN FSDKSFDVPT SSINFPANVK IDVTTSHTKL NELLESNEQV KKMKSRQLTG KLFNLLPFFT TLCFNSFSPF TVFAVIFTIV // ID Y642_MYCPN Reviewed; 279 AA. AC P75155; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 4; DE Flags: Precursor; GN OrderedLocusNames=MPN_642; ORFNames=E09_orf279, MP200; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95848.1; -; Genomic_DNA. DR PIR; S73526; S73526. DR RefSeq; NP_110331.1; NC_000912.1. DR RefSeq; WP_010874999.1; NC_000912.1. DR IntAct; P75155; 1. DR EnsemblBacteria; AAB95848; AAB95848; MPN_642. DR GeneID; 877006; -. DR KEGG; mpn:MPN642; -. DR PATRIC; 20022765; VBIMycPne110_0705. DR BioCyc; MPNE272634:GJ6Z-688-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 279 Uncharacterized lipoprotein MG439 homolog FT 4. FT /FTId=PRO_0000014046. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 279 AA; 31287 MW; FABBBBD5D54B647E CRC64; MKLKLYLIPL LASGIILSAC SSTTSQVISS LSSAQKYFEA NKGELNKNNV INILKDGYNS DPNKTVNALL AGWKYTLMDQ KLLENNLDPS RFKNTFGPNK NKDDVTPNIS EKGLFLNETF TGLGSQIAEV FNVQKQIVSG FSYSWTSPKS FKVNIHIKME GMINEKSKET IKSFLSNKDS NGSNSVEESE YTGDKAKFTA DFIFSYTPPT GGTRSLTDKS FDVITNMINF PADVKIDVNT SHNKLNELLE KNDQVKRMKS RTFNGRNIDL LPFFYYALL // ID Y670_MYCPN Reviewed; 345 AA. AC P75121; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MG456 homolog; GN OrderedLocusNames=MPN_670; ORFNames=K05_orf345, MP172; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95820.1; -; Genomic_DNA. DR PIR; S73498; S73498. DR RefSeq; NP_110359.1; NC_000912.1. DR RefSeq; WP_010875027.1; NC_000912.1. DR ProteinModelPortal; P75121; -. DR EnsemblBacteria; AAB95820; AAB95820; MPN_670. DR GeneID; 877025; -. DR KEGG; mpn:MPN670; -. DR PATRIC; 20022825; VBIMycPne110_0735. DR OMA; NEIPNIA; -. DR OrthoDB; EOG67X21S; -. DR BioCyc; MPNE272634:GJ6Z-716-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 345 Uncharacterized protein MG456 homolog. FT /FTId=PRO_0000210626. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. SQ SEQUENCE 345 AA; 39203 MW; 84D54E38FE36B507 CRC64; MPELTRFQKF FLTPEKFNKF TRVVGFCGVF ALIALSLGIY SYVGQGSIVP KVAALFLIAL GGFTLLLSFV INFVALYKRS QLIHLVNRQD RTDLWLQKMA NNKQFEQFEL FEKGPISADI LPTFYPATIY NFELVPKQFK VQYKNGQTLN FAKLSAIKRS TSKNEKVACL VAIIDAVSDQ HWFLTKSDFP LINTGFYESL TESNRQNNVL LYTEKDASFN FNQLDKEMIK QVLFNPVNVY ANFNVYNNTT HTYLMMSVPI TFMDTSLRME EAVGDLELNI TRQAGYDAAT LDSFHKVVEL LKTKLIGDFN NAETTSATET TVVAEVTEPT TNSKRKPVKA KKAKK // ID Y687_MYCPN Reviewed; 250 AA. AC Q50315; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MPN_687; GN OrderedLocusNames=MPN_687; ORFNames=K05_orf250, MP155; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium RT Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a RT cluster of ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 29342 / M129; RX PubMed=11271496; RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6; RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., RA Herrmann R., Frank R.; RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae."; RL Electrophoresis 21:3765-3780(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34816; AAC43647.1; -; Genomic_DNA. DR EMBL; U00089; AAB95803.1; -; Genomic_DNA. DR PIR; S62838; S62838. DR RefSeq; NP_110376.1; NC_000912.1. DR RefSeq; WP_010875044.1; NC_000912.1. DR EnsemblBacteria; AAB95803; AAB95803; MPN_687. DR GeneID; 877038; -. DR KEGG; mpn:MPN687; -. DR PATRIC; 20022863; VBIMycPne110_0754. DR OrthoDB; EOG6TTW08; -. DR BioCyc; MPNE272634:GJ6Z-733-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 250 Uncharacterized protein MPN_687. FT /FTId=PRO_0000210705. SQ SEQUENCE 250 AA; 28662 MW; 4378A2834BBB7877 CRC64; MAISKKKRFF FDLAQDEDDA ETVQEVKKVE QQLKLEPVVQ PQHDLTNQTK ANQSSQDRKF FSKDMPQFDF GPLLKFGDEF VKSFNQFPKQ EPQTSTQPVN VQPQSEPTNF NNQVPTQPVH QTAEVHLNEF QQPTTTNFNQ QPVATSNIQV EATQPIVEPV PQPEPQPAVE QPQVKQTTRP SNKLQEEENL PPPKAKVPGI IPLERQERLT TGVHFYTSTR VWNKVKRYAK AVNIPISRIL TMILDQVIEE // ID Y542_MYCPN Reviewed; 218 AA. AC P75236; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MG364 homolog; GN OrderedLocusNames=MPN_542; ORFNames=G12_orf218, MP300; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95948.1; -; Genomic_DNA. DR PIR; S73626; S73626. DR RefSeq; NP_110231.1; NC_000912.1. DR RefSeq; WP_010874899.1; NC_000912.1. DR IntAct; P75236; 2. DR EnsemblBacteria; AAB95948; AAB95948; MPN_542. DR GeneID; 877168; -. DR KEGG; mpn:MPN542; -. DR PATRIC; 20022561; VBIMycPne110_0604. DR OMA; ERDYETE; -. DR OrthoDB; EOG6MSS30; -. DR BioCyc; MPNE272634:GJ6Z-587-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MG364 homolog. FT /FTId=PRO_0000210566. SQ SEQUENCE 218 AA; 25572 MW; 38812CA4F5A1C1CB CRC64; MNGGGQQGGF FGLLVIIIPV ILLIVFFSKK KNSQKTEFGG EGGSRASKKD EVWKTVKQFL QEQNERGKEI IKTFVAKNPN PLHSRKDRQF FNQEVQAYIT AHNLSKTAAK RYRHEQLKLK QRELYCIYFI TKDAKTSVFD EARIIEAEVY QKPNKTGKGA PERLIRILGL KNFNDEMKWI QPLMDREEKR KEKEEKRKRE LAARQLKRQE KKKQKTSK // ID Y577_MYCPN Reviewed; 346 AA. AC P75203; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Uncharacterized protein MPN_577; GN OrderedLocusNames=MPN_577; ORFNames=D02_orf346, MP265; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; U00089; AAB95913.1; -; Genomic_DNA. DR PIR; S73591; S73591. DR RefSeq; NP_110266.1; NC_000912.1. DR RefSeq; WP_010874934.1; NC_000912.1. DR EnsemblBacteria; AAB95913; AAB95913; MPN_577. DR GeneID; 877386; -. DR KEGG; mpn:MPN577; -. DR PATRIC; 20022633; VBIMycPne110_0639. DR OMA; AINTYER; -. DR BioCyc; MPNE272634:GJ6Z-623-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF00949; Peptidase_S7; 1. DR PRINTS; PR00840; Y06768FAMILY. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 346 Uncharacterized protein MPN_577. FT /FTId=PRO_0000210729. SQ SEQUENCE 346 AA; 39374 MW; B75C0A42AC759698 CRC64; MQLANNKWRV FGTGWLIDWK KPKRTHNLSE PFYLYLATNL HIAVALSNPK DYAPFNKASI GNSLTTVFCL GKYINPQLFK LRTDVSNAFV SIQTSTIPKT AFVARDFVPL QNRGNQWVAP VRASEDDPAL AKSYLDFAII EVPLFLHNQM DKQIYDHFMR PAINTYERLG NSVGIFAYQP MASFKRDSYF ALGYPQVESN IAALNLNQTE VKPTRPEDVA QVTFKEPWSV DHHREIPTLT TNQLTTIKTK HFSGSKLSWP FDHTKSFKIK NKWLGQNYQM YGHGLGIDQV NLRKGTSSSL VINQKRQIVG IYFATVITNP KKAVRNDVGL VQMLRFQGEG NSLNPN // ID Y578_MYCPN Reviewed; 100 AA. AC P75202; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAY-2015, entry version 53. DE RecName: Full=Uncharacterized protein MPN_578; GN OrderedLocusNames=MPN_578; ORFNames=D02_orf100, MP264; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95912.1; -; Genomic_DNA. DR PIR; S73590; S73590. DR RefSeq; NP_110267.1; NC_000912.1. DR RefSeq; WP_010874935.1; NC_000912.1. DR EnsemblBacteria; AAB95912; AAB95912; MPN_578. DR GeneID; 876758; -. DR KEGG; mpn:MPN578; -. DR BioCyc; MPNE272634:GJ6Z-624-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MPN_578. FT /FTId=PRO_0000210695. SQ SEQUENCE 100 AA; 11580 MW; AE82D2B513BE3F5D CRC64; MLNSNNHQTE WKWPRLIQIM EIGNSAMKNT MSKTLYMSYN FIARTSGKTY HAPVLVVDCS VNEGWLWMRI CHNCLGCLCT GYWAAQRTFA TTTGLRLVWL // ID Y614_MYCPN Reviewed; 334 AA. AC P75181; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MPN_614; GN OrderedLocusNames=MPN_614; ORFNames=C12_orf334, MP228; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Belongs to the MG414/MG415 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; U00089; AAB95876.1; -; Genomic_DNA. DR PIR; S73554; S73554. DR RefSeq; NP_110303.1; NC_000912.1. DR RefSeq; WP_010874971.1; NC_000912.1. DR EnsemblBacteria; AAB95876; AAB95876; MPN_614. DR GeneID; 877143; -. DR KEGG; mpn:MPN614; -. DR PATRIC; 20022711; VBIMycPne110_0678. DR OrthoDB; EOG6W19D7; -. DR BioCyc; MPNE272634:GJ6Z-660-MONOMER; -. DR Proteomes; UP000000808; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 334 Uncharacterized protein MPN_614. FT /FTId=PRO_0000210699. SQ SEQUENCE 334 AA; 39223 MW; C8466B3A7B52AF1C CRC64; MPFLKYWKLM GFSLTPLLLS SATINSHVID SSFYLTKNLV ESENQSPIQF NQLSRIILVQ LEFDPDSIVD NTSITFNNRT LGQKALLKLR FKREFTLAIQ EITELNQLVD QAIDKNTVLQ NFLTLKNVER KQQWERLSYL YKLLNFDFRD PQELSLVRDL PRLLKTIFES ASINFQVRMG GQLRKITLVK NNNNVFNLGQ FEQFLNLDQI SINLFEVEFL SFDFISDQYP SWTAKNLPVF SLFESAKNKP TIQKTNQGIQ YRLRFRSNYN EQYLNKYRFS IPVVNNGKEF SVLDIQDKEL TEEQKNQIAF VIKNGFFISG WYGINCCLKF NQIS // ID Y647_MYCPN Reviewed; 290 AA. AC P75150; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MG439 homolog 1; DE Flags: Precursor; GN OrderedLocusNames=MPN_647; ORFNames=E09_orf290, MP195; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; U00089; AAB95843.1; -; Genomic_DNA. DR PIR; S73521; S73521. DR RefSeq; NP_110336.1; NC_000912.1. DR RefSeq; WP_010875004.1; NC_000912.1. DR EnsemblBacteria; AAB95843; AAB95843; MPN_647. DR GeneID; 877023; -. DR KEGG; mpn:MPN647; -. DR PATRIC; 20022775; VBIMycPne110_0710. DR OMA; LLENPMD; -. DR OrthoDB; EOG69PQBN; -. DR BioCyc; MPNE272634:GJ6Z-693-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 290 Uncharacterized lipoprotein MG439 homolog FT 1. FT /FTId=PRO_0000014043. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 290 AA; 31823 MW; 499A344A5FA80F17 CRC64; MNKKSILSKT SLGSLFFLFG TALSACSSAT TEVISSFSSA QKYFSANKKE LNKRNLVTIL KDSYNSDPKS TVNSLLAGWK YSLLDQKLLE NPMDPSRFSK AFGSNTKDDV NPNISEKGLY LAETYPGVSS QIAQVLGVQS QKVTGFSYSW TSKTKFEVKI LIKMKGKVGS DGTSQTLIKS FLGTDSKGSG SNNQNGGVTE KDFEGDQANF DGNFIFTYTQ PSDGRRLASN NFDPITGTIN FPADLQIEVS TSHEKLNTLM TTNTQVGMIK NRSFKGKSFN LLPFFYYALL // ID Y661_MYCPN Reviewed; 549 AA. AC P75130; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MG447 homolog; GN OrderedLocusNames=MPN_661; ORFNames=K05_orf499, MP181; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34741.1; -; Genomic_DNA. DR PIR; S73507; S73507. DR RefSeq; NP_110350.1; NC_000912.1. DR RefSeq; WP_010875018.1; NC_000912.1. DR ProteinModelPortal; P75130; -. DR EnsemblBacteria; AAG34741; AAG34741; MPN_661. DR GeneID; 877020; -. DR KEGG; mpn:MPN661; -. DR PATRIC; 20022807; VBIMycPne110_0726. DR OMA; GYIVTVY; -. DR OrthoDB; EOG63NMF0; -. DR BioCyc; MPNE272634:GJ6Z-707-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015297; F:antiporter activity; IEA:InterPro. DR GO; GO:0015238; F:drug transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 549 Uncharacterized protein MG447 homolog. FT /FTId=PRO_0000210619. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 233 253 Helical. {ECO:0000255}. FT TRANSMEM 265 285 Helical. {ECO:0000255}. FT TRANSMEM 308 328 Helical. {ECO:0000255}. FT TRANSMEM 352 372 Helical. {ECO:0000255}. FT TRANSMEM 399 419 Helical. {ECO:0000255}. FT TRANSMEM 434 454 Helical. {ECO:0000255}. FT TRANSMEM 472 492 Helical. {ECO:0000255}. FT TRANSMEM 501 521 Helical. {ECO:0000255}. SQ SEQUENCE 549 AA; 61650 MW; 7E281376051D02D8 CRC64; MDSQQDRLAK QVLIQKSFES KRLFLTILRF AIPTFFFALF SAAYVFVDQI MVIKFVPHGP LNPDSIFTDQ ALIEEFKASA FYKGGDIPNH TELTASQLVK TVLNISQPIV VILNAITIFV PLGTGVIFSK TIGKGDEKKI KDAWNTGLVS TTLFALVTQI IVLAIAKEWL QFNLDKVDEQ HHVQVADQFQ HFFNEKAVAI GSEYVYILIG FNIIPMLSRL FFYLGQSEGR QLFIAIVPPL SNLLNVLFVF LLVRFSTLGV VGSAVAAILV YFITFMAYVV YLISLNKRGL TYLSLRDFSF KRVSFNLFLV ISMVGLASFF RNGSLSILNT FYESFLVNLT KTLTDQSDTF YLVLLTGPIA IANLTSAAIF GVLQGVRTVV SYKFGQGQLA DIKRINVYTL LVCLVFAALL YLILAVGLGK EILVHLFDTS AATLMLANQF SLIVQAQVFF VAIGATSQQY FQNNNRVLYS WIVSLMQGVI VFVPLLFIFQ AITLQTKNIE IFIWLLTANA ALAGLINVLI GQVHIHFFMD KYFAQKHKSR IVQFIERYS // ID YIDC_MYCPN Reviewed; 385 AA. AC P75112; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Membrane protein insertase YidC; DE AltName: Full=Foldase YidC; DE AltName: Full=Membrane integrase YidC; DE AltName: Full=Membrane protein YidC; GN Name=yidC; OrderedLocusNames=MPN_680; ORFNames=MP162; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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 (By similarity). {ECO:0000250}. 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 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB95810.1; -; Genomic_DNA. DR PIR; S73488; S73488. DR RefSeq; NP_110369.1; NC_000912.1. DR RefSeq; WP_010875037.1; NC_000912.1. DR EnsemblBacteria; AAB95810; AAB95810; MPN_680. DR GeneID; 876762; -. DR KEGG; mpn:MPN680; -. DR PATRIC; 20022849; VBIMycPne110_0747. DR KO; K03217; -. DR OMA; FKVITIC; -. DR OrthoDB; EOG67MF0Q; -. DR BioCyc; MPNE272634:GJ6Z-726-MONOMER; -. DR Proteomes; UP000000808; 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 InterPro; IPR028055; Membr_insert_YidC/Oxa1_C. DR InterPro; IPR001708; Membrane_insert_OXA1/ALB3/YidC. DR PANTHER; PTHR12428; PTHR12428; 1. DR Pfam; PF02096; 60KD_IMP; 1. DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1. PE 3: Inferred from homology; KW Cell membrane; Chaperone; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 385 Membrane protein insertase YidC. FT /FTId=PRO_0000124728. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 270 290 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. FT TRANSMEM 346 366 Helical. {ECO:0000255}. SQ SEQUENCE 385 AA; 44239 MW; C85BB5A28DC5B82D CRC64; MPLNLNKKHK ELKTTFNPFW SAAVVNEKNG LKNLKKAWGI IFKVLKVAIF IFLTIVGLWG CTQTLAQPWT GTNQLLGSGL EIGYNFGTTG DYRYDLQSNN VGPYFTFSDY TLAYGPFYGW FVWPASQIVL PIMYATRVPL GSGPELGFNM ILSLIVLLFL VRLITIVITL NSTLALEKMN EVQGKLAEIN AKYKGALDLQ SKRNRQMEIM SLYKKHNIKS SASFVQVFVT LPIFLIIYRI VTTLRPIKAI ILFNFWDLSK VPLTEIFSNF TSTGWTFIIF LIIVLPVQFI SQKLPQIWAS KRNENAKAHS QKSIEQLNKT KRMQLIFYFV FAVITAFSAA GVGVYWFLNA LFTLLQSYLT HLFIVKRRTR RRLTYSKLEQ MLERE // ID YBEY_MYCPN Reviewed; 154 AA. AC P75209; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 11-NOV-2015, entry version 77. 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=MPN_569; ORFNames=MP273; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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=AAB95921.1; 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; U00089; AAB95921.1; ALT_INIT; Genomic_DNA. DR PIR; S73599; S73599. DR RefSeq; NP_110258.2; NC_000912.1. DR RefSeq; WP_015344925.1; NC_000912.1. DR ProteinModelPortal; P75209; -. DR IntAct; P75209; 1. DR EnsemblBacteria; AAB95921; AAB95921; MPN_569. DR GeneID; 876862; -. DR KEGG; mpn:MPN569; -. DR PATRIC; 20022617; VBIMycPne110_0631. DR KO; K07042; -. DR OMA; GEIFLCP; -. DR OrthoDB; EOG6NGVW6; -. DR BioCyc; MPNE272634:GJ6Z-615-MONOMER; -. DR Proteomes; UP000000808; 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 Pfam; PF02130; UPF0054; 1. DR TIGRFAMs; TIGR00043; TIGR00043; 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 1 154 Endoribonuclease YbeY. FT /FTId=PRO_0000210589. FT METAL 117 117 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 121 121 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 127 127 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. SQ SEQUENCE 154 AA; 18130 MW; 1F4BCAA037B9F037 CRC64; MKPSFSINSN YLFKRFFGKN FEAGIELCLQ IIKDSLQLSF QPEFALMIVS PWKMKRLNRQ FLNRKGVTDV ISICYNENEA GFSPAIGEIF LCPKHIFKQA KQFGCTPWFL LTRNLIHGLL HLFEFDHEQS LAFESVTMFF QDEIHETVLK LWNR // ID YQGF_MYCPN Reviewed; 140 AA. AC P57114; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 20-JAN-2016, entry version 88. 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=MPN_418; ORFNames=MP422.1; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] RP IDENTIFICATION. RC STRAIN=ATCC 29342 / M129; RX PubMed=10954595; DOI=10.1093/nar/28.17.3278; RA Dandekar T., Huynen M., Regula J.T., Ueberle B., Zimmermann C.U., RA Andrade M.A., Doerks T., Sanchez-Pulido L., Snel B., Suyama M., RA Yuan Y.P., Herrmann R., Bork P.; RT "Re-annotating the Mycoplasma pneumoniae genome sequence: adding RT value, function and reading frames."; RL Nucleic Acids Res. 28:3278-3288(2000). CC -!- FUNCTION: Could be a nuclease involved in processing of the 5'-end CC of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SIMILARITY: Belongs to the YqgF nuclease family. CC {ECO:0000255|HAMAP-Rule:MF_00651}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAG34748.1; -; Genomic_DNA. DR RefSeq; NP_110106.1; NC_000912.1. DR RefSeq; WP_010874774.1; NC_000912.1. DR ProteinModelPortal; P57114; -. DR IntAct; P57114; 1. DR EnsemblBacteria; AAG34748; AAG34748; MPN_418. DR GeneID; 877299; -. DR KEGG; mpn:MPN419; -. DR PATRIC; 20022232; VBIMycPne110_0453. DR KO; K07447; -. DR OMA; NTIDRFP; -. DR OrthoDB; EOG6N94FV; -. DR BioCyc; MPNE272634:GJ6Z-447-MONOMER; -. DR Proteomes; UP000000808; 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 1 140 Putative pre-16S rRNA nuclease. FT /FTId=PRO_0000172098. SQ SEQUENCE 140 AA; 15936 MW; 16DF2E48C5C1C150 CRC64; MQYILGIDFG LKRIGTALVN TIDRFPSPFR VFAVQNNLQQ AVNTLFKDLK QAGYELVQIV IGFPHFHYQS SIQVSIHKFV ELIKTRFNVP VTLIDESGTT SEVKANLQEL GLKNRTFKKA KDTLAATLIL ERFLNQQKPN // ID YHIT_MYCPN Reviewed; 144 AA. AC P75504; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized 16.1 kDa HIT-like protein; GN OrderedLocusNames=MPN_273; ORFNames=A65_orf144, MP562; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., RA Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- SIMILARITY: Contains 1 HIT domain. {ECO:0000255|PROSITE- CC ProRule:PRU00464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00089; AAB96210.1; -; Genomic_DNA. DR PIR; S73888; S73888. DR RefSeq; NP_109961.1; NC_000912.1. DR RefSeq; WP_010874630.1; NC_000912.1. DR ProteinModelPortal; P75504; -. DR EnsemblBacteria; AAB96210; AAB96210; MPN_273. DR GeneID; 876967; -. DR KEGG; mpn:MPN273; -. DR PATRIC; 20021873; VBIMycPne110_0293. DR KO; K02503; -. DR OMA; EGHILIL; -. DR OrthoDB; EOG69GZSV; -. DR BioCyc; MPNE272634:GJ6Z-280-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR23089; PTHR23089; 1. DR Pfam; PF01230; HIT; 1. DR PRINTS; PR00332; HISTRIAD. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 144 Uncharacterized 16.1 kDa HIT-like FT protein. FT /FTId=PRO_0000109821. FT DOMAIN 13 120 HIT. {ECO:0000255|PROSITE- FT ProRule:PRU00464}. FT MOTIF 105 109 Histidine triad motif. SQ SEQUENCE 144 AA; 16086 MW; 180F684630F33517 CRC64; MVQKQSMANN NCIFCGIVEG NVKSFKVGEN EHAFAFLDAF PVADGHTLVI PKKHAVNYSS TDDESLKAVS LLAKEMALKL QQRLQPAGLN YVVNEGAKAG QEVFHYHMHV VPKYETGLGF CYNVRKTNNR SIEANWELLT KEVD //