ID   PLSB_GLAP5              Reviewed;         811 AA.
AC   B8F321;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=HAPS_0018;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL31723.1; -; Genomic_DNA.
DR   RefSeq; WP_012621501.1; NC_011852.1.
DR   AlphaFoldDB; B8F321; -.
DR   SMR; B8F321; -.
DR   STRING; 557723.HAPS_0018; -.
DR   PRIDE; B8F321; -.
DR   EnsemblBacteria; ACL31723; ACL31723; HAPS_0018.
DR   KEGG; hap:HAPS_0018; -.
DR   PATRIC; fig|557723.8.peg.20; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000006743; 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..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000192405"
FT   MOTIF           303..308
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  92931 MW;  7BD590513281E20F CRC64;
     MSMLLNLYRK ALNLPLSLLV KTRSIPTDPV NELGLKLDQP IVYVLPYTSQ TDLLILQKNC
     QALNLPDPLV NNDIQGVSLS RFVFLDEGRR FFKSKGAKSE TELVFYRYLD LNRNDEQLDI
     QVVPVSVLWG RAPGKEKGLP VLRLLGTFQR LVTMLWFGRD NFIRFSQAVS LRYMITNHGT
     DENLAQKLAR VAKMHFAKQR YSATGPQLPD RQAMFNKLLQ SPAILAAIED EAKKPKSSLE
     KARKEAEKIL DEIAANVRHD SLRSADRVLS WLWNKLYQGI NVQYAERVRK LALEGHELVY
     VPCHRSHMDY LLLSYILYHQ GLVPPHIAAG INLNFWPAGP IFRSWGAFFI RRTFKGNRLY
     STIFREYLAE LFYRGYSVEY FIEGGRSRTG RLLDPKTGMM SMTLQALQRG LTRPISIVPV
     YIGYEHVLEV DTYAKELRGA EKEKENAGLV LRVIKKLKKL GQGYVNFGEP IPLNHYLNQY
     FPEWKEPLTD ENGRPKWLNS AVEAVSKQVM VHINNAVAVN AKNLIGSVLL ASRQRSLTRE
     QLIEQVESYM QLFKNVPYTA EVTLPTDTAE AMLDHVINLP RSGVISEKDN FGEIIRLDRQ
     SAVLMTYYRN NIQHLFVLPS LVASIVLHHE TVSKDLIIQS VNRIYPFLQA ELFMHFKAEE
     VRGHIEAILA EFVAQNLIKN ESDMFVINRQ RIRSLQLHSS GVRELLQRYY ISLSILIEQP
     EISRNELEQE SRSIAQRLSV LHGINAPEFF DKALFSTFSA TLKEQGYFDE EGDTIVSKVQ
     STEELIRGLI SVEIQHTVQG AMVKLEEVNN I