ID   PLSB_PSEA6              Reviewed;         811 AA.
AC   Q15MZ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393}; OrderedLocusNames=Patl_4248;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
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DR   EMBL; CP000388; ABG42747.1; -; Genomic_DNA.
DR   RefSeq; WP_011576933.1; NC_008228.1.
DR   AlphaFoldDB; Q15MZ1; -.
DR   SMR; Q15MZ1; -.
DR   STRING; 342610.Patl_4248; -.
DR   EnsemblBacteria; ABG42747; ABG42747; Patl_4248.
DR   KEGG; pat:Patl_4248; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001981; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049441"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  91594 MW;  4DE8E797439DC370 CRC64;
     MAWLHKLLLT MISVPLKWLV KVNSIPTDIA TELGIDNTKP IIYLLRTHSV TDQFALKMST
     NSLGLPKPSE PVQIGGKELP ACLFLQQPRS LLTRKVKITK IADDVTRLFQ LHREHPELDL
     QIVPVSIFWG RAPGRKLSGW SDIIANQVSP NWLRKFFIVL FLGRDNFVCY SKAVSSRTMA
     DLKGSDEEIG HKLIRLAGTH FHRRRQNLIG PMLLERQELY NAVLGADSVR QAVSDEARSK
     KQSNHQIQAK AKKYVDEIAA DYREGLVRIG DRLLTKIWNK VYNGIEVKHA DKVRALAQNG
     HEIIYVPCHR SHMDYLLLTY VIYHEGLVTP HIAAGINLNF WPIGGILRKC GAFFLRRSFA
     GNKLYTAVFR EYLELLFNKG YSVKYYPEGG RSRTGRLLPP KTGMLAMTLQ GLIKGINRPV
     SIVPVYIGYE HVMEVSSYLK ELKGTDKKKE SFFQVFSAVR KLKNYGNGFL NFGDPINLSN
     FLDSEVPDWR EAQNLEPDKK PRWLTPAVNT LANDVMGRIN QAAAVSGMSL CAMCLLSAKK
     HAMAQDELER AIDDYLDLLK AAPYSDLSSI PELDGKALVE NTLKLNKLEV SQDSFGTIIS
     LKRKNAVALT YYRNNILHLF ALPGLVSAIV FAHKGLARPQ VISLVGQLYP LLQRELFIYM
     SHEEAMNYTD RLLSTMIDIG LLRAEDDTLC PPAATSKAFY SFWLLNRSIQ ETLQRYAAVL
     TILKKEQTIG RGRLEKQSRE FAERLAALHG INSPEFFDKN VLSTFIHALK DNELINASSE
     GQLQHSDTSE ALLASVEELI SPEITQRLQQ I