ID F4T0N7_ECOLX Unreviewed; 182 AA.
AC F4T0N7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|HAMAP-Rule:MF_01437};
DE EC=2.7.8.5 {ECO:0000256|HAMAP-Rule:MF_01437};
DE AltName: Full=Phosphatidylglycerophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01437};
DE Short=PGP synthase {ECO:0000256|HAMAP-Rule:MF_01437};
GN Name=pgsA {ECO:0000256|HAMAP-Rule:MF_01437};
GN ORFNames=ECIG_02000 {ECO:0000313|EMBL:EGI15366.1};
OS Escherichia coli M605.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656417 {ECO:0000313|EMBL:EGI15366.1, ECO:0000313|Proteomes:UP000004710};
RN [1] {ECO:0000313|EMBL:EGI15366.1, ECO:0000313|Proteomes:UP000004710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M605 {ECO:0000313|EMBL:EGI15366.1,
RC ECO:0000313|Proteomes:UP000004710};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M605.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000256|ARBA:ARBA00003973,
CC ECO:0000256|HAMAP-Rule:MF_01437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566, ECO:0000256|HAMAP-
CC Rule:MF_01437};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042, ECO:0000256|HAMAP-Rule:MF_01437}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01437}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01437}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|HAMAP-
CC Rule:MF_01437, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; GL883912; EGI15366.1; -; Genomic_DNA.
DR RefSeq; WP_001160188.1; NZ_GL883912.1.
DR AlphaFoldDB; F4T0N7; -.
DR GeneID; 75172033; -.
DR HOGENOM; CLU_051314_2_1_6; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000004710; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1760; -; 1.
DR HAMAP; MF_01437; PgsA; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR023762; PGP_synthase_bac.
DR InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR NCBIfam; TIGR00560; pgsA; 1.
DR PANTHER; PTHR14269:SF62; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01437};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01437};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01437};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01437}.
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01437"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 38..60
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01437"
FT TOPO_DOM 82..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01437"
FT TOPO_DOM 108..145
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01437"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 169..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01437"
SQ SEQUENCE 182 AA; 20715 MW; F8F1E02ABE6DC8D5 CRC64;
MQFNIPTLLT LFRVILIPFF VLVFYLPVTW SPFAAALIFC VAAVTDWFDG FLARRWNQST
RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS
VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARADLL
EQ
//
