ID   PLSB_YERE8              Reviewed;         822 AA.
AC   A1JRU2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=YE3857;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL13879.1; -; Genomic_DNA.
DR   RefSeq; WP_005174551.1; NC_008800.1.
DR   RefSeq; YP_001008005.1; NC_008800.1.
DR   AlphaFoldDB; A1JRU2; -.
DR   SMR; A1JRU2; -.
DR   STRING; 393305.YE3857; -.
DR   EnsemblBacteria; CAL13879; CAL13879; YE3857.
DR   GeneID; 67422004; -.
DR   KEGG; yen:YE3857; -.
DR   PATRIC; fig|393305.7.peg.4108; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000642; 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..822
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049470"
FT   MOTIF           304..309
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   822 AA;  93409 MW;  7391BE213C7E8334 CRC64;
     MSGWRKIYYK LLNLPLKLLV KSKVIPADPV TELGLDPSRP ILYVLPYNSK ADLLTLRAQC
     QAQDLPDPLI PLEIDGVQLP SHVFIDNGPR VFRYYAPKQE SVKIFHDYLD LHRNNPELDI
     QMLPVSVMFG RSPGREGHGT PHLRVLNGVQ KFFAVLWLGR DSFVRFSTTV SLRRMASEHG
     TDKTIAHKLA RVARMHFSRQ RLAAVGPSLP ARQDLFKKLL TSKAIEKAVA DEARTKKISH
     EKAQQNAITL MEEIAADFSY EAVRLSDRVL SWTWNRLYQG INVHNAERVR QLAQDGHEIV
     YVPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
     YSTVFREYLG ELFTRGYSVE YFVEGGRSRT GRLLEPKTGT LSMTIQAMLR GGSRPITLVP
     IYIGYEHVME VGTYAKELRG ATKEKESLLQ MLRGLRKLRN LGQGYVNFGE PIPLTTYLNT
     NVPQWRDAID PIEAQRPSWL TPAVNDLAGK IMVRINNAAA ANAMNLCSTA LLASRQRSLT
     REQLLEQLDC YLQLMRNVPY AKDVTVPDKT PEELLNHALN MNKFEVEKDN IGDIIILPRE
     QAVLMTYYRN NIQHLLILPS LIASMVMYQR RITRAELLRQ ISMIYPMLKA ELFLHYSKEQ
     LPQTLDTLID ELARQQLICD KGSELVLNPA RIRPLQLLAA GVRETLQRYA ITLSLLSANP
     SINRGALEKE SRIMAQRLSV LHGINAPEFF DKAVFSTLVG TLREEGYISD SGDAIQEHTL
     EVYNMLSALM TPEVKLTIES VSMPAETNNL LPEPEAEDKE EN