ID   PLSB_ECOUT              Reviewed;         827 AA.
AC   Q1R3P5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=UTI89_C4611;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE10019.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1R3P5; -.
DR   SMR; Q1R3P5; -.
DR   EnsemblBacteria; ABE10019; ABE10019; UTI89_C4611.
DR   KEGG; eci:UTI89_C4611; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001952; 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..827
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049431"
FT   MOTIF           325..330
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   827 AA;  93696 MW;  30DF48AC985EB183 CRC64;
     MTFCYPCRAF ALLTRGFTSF MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP
     IMYVLPYNSK ADLLTLRAQC LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE
     SIKLFHDYLD LHRSNPNLDV QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG
     RDSFVRFSPS VSLRRMADEH GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL
     LASRAIAKAV EDEARSKKIS HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ
     GINVHNAERV RQLAHDGHEL VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA
     GPIFRRLGAF FIRRTFKGNK LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG
     TLSMTIQAML RGGTRPITLI PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR
     NLGQGYVNFG EPMPLMTYLN QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG
     AANAMNLCCT ALLASRQRSL TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL
     QMNKFEVEKD TIGDIIILPR EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME
     HVNVLYPMLK AELFLRWDRD ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA
     AGARETLQRY AITFWLLSAN PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV
     LTLRDEGYIS DSGDAEPAET MKVYQLLAEL ITSDVRLTIE SATQGEG