ID   PLSB_SALAR              Reviewed;         806 AA.
AC   A9MGP8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-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}; OrderedLocusNames=SARI_03443;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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; CP000880; ABX23272.1; -; Genomic_DNA.
DR   RefSeq; WP_012210697.1; NC_010067.1.
DR   AlphaFoldDB; A9MGP8; -.
DR   SMR; A9MGP8; -.
DR   STRING; 41514.SARI_03443; -.
DR   EnsemblBacteria; ABX23272; ABX23272; SARI_03443.
DR   KEGG; ses:SARI_03443; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002084; 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..806
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000080289"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   806 AA;  91194 MW;  DE95C57970679C63 CRC64;
     MSGWPRIYYK LLNLPLSILV KSKSIPAEPA QELGLDTSRP IMYVLPYNSK ADLLTLRAQC
     LAHDLPDPLE PLEIDGALLP RYVFIHGGPR VFTYYTPKEE SVKLFHDYLD LHRGNPALDV
     QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAISWLG RDSFVRFSPS VSLRRMADEH
     GTDKIIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASKAIARAV EDEARSKKIS
     HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEI
     VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
     LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLV
     PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN
     QHVPEWRESI DPIEAIRPAW LTPTVNSIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL
     TREQLTEQLD CYLDLMRNVP YSTDSTVPAA SAGELIDHAL QMNKFEAEKD TIGDIIILPR
     EQAVLMTYYR NNIAHMLIMP SLMAAIITQH RRISRDALQQ HVEALYPMLK AELFLRWERE
     ELASVIDALA SEMQRQGLIT LQDNELHINP AHSRTLQLLA AGARETLQRY AITFWLLSAN
     PSINRSTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DTGDAEPAET
     MKIYQMLADL ITSDVRLTIE SATQGE