ID   PLSB_YERPP              Reviewed;         825 AA.
AC   A4TRU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=YPDSF_3659;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pestoides F;
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   Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-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; CP000668; ABP42009.1; -; Genomic_DNA.
DR   RefSeq; WP_002214644.1; NZ_CP009715.1.
DR   AlphaFoldDB; A4TRU7; -.
DR   SMR; A4TRU7; -.
DR   GeneID; 57974292; -.
DR   KEGG; ypp:YPDSF_3659; -.
DR   PATRIC; fig|386656.14.peg.321; -.
DR   OMA; EVIYVPC; -.
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..825
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049473"
FT   REGION          803..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           304..309
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   825 AA;  93621 MW;  0D0C9A0CDC751127 CRC64;
     MSGWRKIYYK LLNLPLKLLV KSKVIPADPV SELGLDPSRP ILYVLPYNSK ADLLTLRAQC
     LAQDLPDPLI PLEIDGVQLP SHVFIENGPR VFRYYVPKQE SVKLFHDYLD LHRNNPALDI
     QMLPVSVMFG RSPGREGHGT PHLRVLNGVQ KFFAVLWLGR DSFVRFSTTV SLRRMASEHG
     TDKTIAHKLA RVARMHFSRQ RLAAVGPSLP ARQDLFKKLL ASKAIEKAVA DEARSKKISH
     EKAQQNAITL MEEIAANFSY EAVRLSDRVL SWTWNRLYQG INVHNAERVR QLAQDGHEIV
     YVPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
     YSTVFREYLG ELFTRGYSVE YFVEGGRSRT GRLLEPKTGT LSMTIQAMLR GGTRPITLVP
     IYIGYEHVME VGTYAKELRG AIKEKENLLQ MLRGLRKLRN LGQGYVNFGE PLPLTTYLNT
     HVPQWRDAID PIEAQRPSWL TPAVNDLANQ IMVRINNAAA ANAMNLCSTA LLASRQRSLT
     REQLLEQLDC YLQLMRNAPY AKDTTVPDKT PEELLNHALN MNKFEVEKDT IGDIIILPRE
     QAVLMTYYRN NIQHLLILPS LIASMVMYHR RITRTELLHK ISMIYPMLKA ELFLHYSKEQ
     LPETLDTLID ELARQQLICD KGSELVLNPA RIRPLQLLAA GVRETLQRYA ITLSLLSATP
     SINRGALEKE SRIMAQRLSV LHGINAPEFF DKAVFSTLVA TLREEGYISD SGDAIQEHTL
     EVYNMLSALM TPEVKLTIES VSMPAETSNQ PEAPETPEPE GKTES