ID I2B7Z7_SHIBC Unreviewed; 182 AA.
AC I2B7Z7; K6UQC5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 ECO:0000313|EMBL:AFJ46651.1};
GN OrderedLocusNames=EBL_c15540 {ECO:0000313|EMBL:AFJ46651.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ46651.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ46651.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
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; CP001560; AFJ46651.1; -; Genomic_DNA.
DR RefSeq; WP_002440110.1; NZ_BAHA01000004.1.
DR AlphaFoldDB; I2B7Z7; -.
DR STRING; 630626.EBL_c15540; -.
DR KEGG; ebt:EBL_c15540; -.
DR PATRIC; fig|630626.3.peg.1500; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_051314_2_1_6; -.
DR OrthoDB; 9796672at2; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000001955; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001955};
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 31..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..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..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; 20911 MW; F8873F0EB17DB37C CRC64;
MRFNIPTLLT LFRVILIPFF VLAFYLPFTW APFACAFIFW LAAITDWFDG FLARRWNQST
RFGAFLDPVA DKVMVAIAMV LVVEYYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS
VAVSWIGKVK TTAQMLALIA LLWRPNMWIE SLGIALFFVA AVLTLWSMFQ YLSAARGDLL
DQ
//
