ID   PLSB_ALTMD              Reviewed;         818 AA.
AC   B4S1W8; F2GCF9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
GN   OrderedLocusNames=MADE_1020115;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CP001103; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP001103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; B4S1W8; -.
DR   SMR; B4S1W8; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001870; 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; Transferase.
FT   CHAIN           1..818
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123074"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   818 AA;  92322 MW;  36D4704FA216914F CRC64;
     MSWMRKALLS VFHYPVKLLV KAHSIPVNVE TELGIDKSKP IVYLLPTNSV TDQLSLRMST
     QALDLPSPTK TLTLAGREYS STLFLRKTQP LFRSSAKDTG IEEVFTDLFH LHRDHENLDL
     QVVPVYVTWG RAPGRGNPGL SDLIADKAAP SWLRKLFIVL FLGRDNFINY SKAVSARAMS
     NQHGSDQSIA HKLVRVASTH FQRKRQSMTG PTLLERQELN NSVLGSDAVR RAIAEESRSK
     KVSHDKAKAC AQSYITEIAA DYREGLIRFG DRLLTRIWNK IYNGISVGHA ERIRELAANG
     HEIIYVPCHR SHMDYLLLTY VIYHEGMVTP HIAAGINLNF WPVGKMFRRG GAFFLRRSFA
     GNKLYTAVFR EYLELLFNKG YSVKYYPEGG RSRTGRLIPP KTGMLAITIQ AMLKGVNRPV
     SIVPVYIGYE NVMEVKSYLN ELKGSKKKKE SNLQVFSAIR KLKNYGHGYV NFGEPIALNQ
     FLESHVPNWR DCKDAEPEKK PAWLTPAVNE LANNVMTRIN RAAALNGMAL TSLCLLSSKT
     QTMSEAELKQ SIGDFMDLFK AVPFSDDATI PDSTAEALLR DTLKLGRFDI KEDDYGRLIS
     PQPKSAVYLT YYRNNILHLF AIPGLVMASV FAKKGTTKND ILQLIAALYP LLQKELFLHL
     TQDEALAHTD ALVTALLNNG LLRQKDKELL PPDAHCKQFH SAWLLSRCMQ ETLQRYAVVL
     TILDKEKVIS RGALERESKQ VAERLSALYG LSSPEFYDKN VLSSFIGALK ENHWLDSEKD
     GSLKYSEECE ALRQDVMALI WPEMMQHLEN VALNGQTN