ID   PLSB_HAES1              Reviewed;         811 AA.
AC   Q0I2G8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=HS_0385;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI24663.1; -; Genomic_DNA.
DR   RefSeq; WP_011608541.1; NC_008309.1.
DR   AlphaFoldDB; Q0I2G8; -.
DR   SMR; Q0I2G8; -.
DR   STRING; 205914.HS_0385; -.
DR   EnsemblBacteria; ABI24663; ABI24663; HS_0385.
DR   KEGG; hso:HS_0385; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
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..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049436"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  92687 MW;  61444F0420B80C71 CRC64;
     MSSILNFYRN LLSVPLSFLV KNNPIPQQPI EELSLDISQP IIYLLPYTSQ TDLIIIRKNC
     LSVGLPDPLE ENELGGQCLP RYVFLDEGRR FFKSKGAKSA TIQIVEKYLE LHRSLPDLNV
     QLVPVSVLWG RSPGHEKQVG LPKLRLLNSI QKTAVAIWFG RDTFVRFSQA VSLRYMADEY
     GTDASIALKL ARVAKIHFAK QRMSATGPRL PNRQAMFNKL LQSPAILNAI ADEAKSKRIS
     KEKARKEAYK ILDEIAANVN YEGLRVADRF LGWLWNKLYQ GIDVQNAERV RKLALEGHEI
     VYIPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPV GMMFRRGGAF FIRRTFKGNR
     LYSTIFREYL AELFHRGYSV EFFIEGGRSR TGRLLAPKTG MMSMTVQALQ QNQIRPISVV
     PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIRKLR NLGQGYVNFA EPITLSNYLN
     QHFPEWKDSQ LEEHSQWFNP AVNAISNQVM ININKAAAIN AMNLTGTALL SSRQRALSRE
     QLLEQLKSYQ RFLQHAPYSN DIIVPTDTPE EILTHVLNLE RVGLIVEKDN FGEMLRLERS
     AAVLMTYYRN NIQHVFVLPS LIASIIFHHG AIQKELVSNA ARKIYPFLKE ELFLHFSQDE
     LDEYVEKIIE EFTRQKLILC AENLLSINKE RVRVLQLWMA GVREILQRYY ITVSILQDTP
     NIAKATLEKE SQSIAQRLSV LHGINAPEFF DKAVFSAFIG SLRSNGYFDK NGVAITEKLN
     DISDILDRII STEVQLTIKS AVGKHEEVQE Y