ID   PLSB_SERP5              Reviewed;         821 AA.
AC   A8GKB6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Spro_4462;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV43556.1; -; Genomic_DNA.
DR   RefSeq; WP_012147156.1; NC_009832.1.
DR   AlphaFoldDB; A8GKB6; -.
DR   SMR; A8GKB6; -.
DR   STRING; 399741.Spro_4462; -.
DR   EnsemblBacteria; ABV43556; ABV43556; Spro_4462.
DR   KEGG; spe:Spro_4462; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
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..821
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000060778"
FT   MOTIF           304..309
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   821 AA;  93297 MW;  09B53B7CF8287DCA CRC64;
     MSGWRKIYYK LLNLPLKLLV RSKVIPSDPV TELGLDPSRP ILYVLPYNSK ADLLTLRTQC
     LAQDLPDPLN PLEIDGTVLP SHVFIHDGPR VFRYYTPKEE SVKLFHDYLD LHRSNPDLDI
     QMLPVSVMFG RSPGREGHGT PHLRLLNGVQ KFFAVLWLGR DSFVRFSNTV SLRRMATEHG
     TDKIIAQKLA RVARMHFSRQ RLAAVGPSLP ARQDLFNKLL ASKAIEKAVE DEARSKKISH
     EKAQQNAIAL MEEIAADFSY ETVRLSDRVL SWTWNRLYQG INVTNAERVR QLAQDGHEIV
     YVPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
     YSTVFREYLG ELFTRGYSVE YFVEGGRSRT GRLLEPKTGT LSMTIQAMLR GGSRPITLVP
     IYIGYEHVME VGTYAKELRG ATKEKESLLQ MLRGLRKLRN LGQGYVNFGD PLPLTAYLNQ
     NVPQWRESID PIEAQRPSWL TPTVNDLAAK IMVRINNAAA ANAMNLCSTA LLASRQRSLT
     REQLLEQLEC YLQLMRNVPY AGDVTVPTQT PDELLDHALN MNKFEVEKDN IGDIIILPRE
     QAVLMTYYRN NIHHLLVLPS LIATIVMHHR RVSRAELLRQ IGLIYPMLKA ELFLHNDKEQ
     LPEVLRPLID EMIRQQLICD KGDDLVLNPA RIRPLQLLAA GVRETLQRYA ITMSILSANP
     SINRGALEKE SRIMAQRLSV LHGINAPEFF DKAVFSTLVA TLRAEGYIND IGDAVREHTM
     EVYNMLSDLI TPEIKLTIES VSMPAETNAL PETVAAEEKE D