ID   PLSB_YERPB              Reviewed;         831 AA.
AC   B2K1U5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=YPTS_0391;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) 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; CP001048; ACC87380.1; -; Genomic_DNA.
DR   RefSeq; WP_012413439.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K1U5; -.
DR   SMR; B2K1U5; -.
DR   PRIDE; B2K1U5; -.
DR   KEGG; ypb:YPTS_0391; -.
DR   PATRIC; fig|502801.10.peg.4069; -.
DR   OMA; EVIYVPC; -.
DR   BioCyc; YPSE502801:YPTS_RS02055-MON; -.
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..831
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123103"
FT   REGION          801..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           304..309
FT                   /note="HXXXXD motif"
FT   COMPBIAS        801..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  94276 MW;  BD5C443F56ED6FDC 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 PEAPETPETP ETPEPEGKTE S