ID   PLSC_HAEIN              Reviewed;         240 AA.
AC   P44848;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
GN   Name=plsC; OrderedLocusNames=HI_0734;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22391.1; -; Genomic_DNA.
DR   PIR; D64089; D64089.
DR   RefSeq; NP_438893.1; NC_000907.1.
DR   RefSeq; WP_005689023.1; NC_000907.1.
DR   AlphaFoldDB; P44848; -.
DR   SMR; P44848; -.
DR   STRING; 71421.HI_0734; -.
DR   EnsemblBacteria; AAC22391; AAC22391; HI_0734.
DR   KEGG; hin:HI_0734; -.
DR   PATRIC; fig|71421.8.peg.768; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_10_3_6; -.
DR   OMA; KQRIKLW; -.
DR   PhylomeDB; P44848; -.
DR   BioCyc; HINF71421:G1GJ1-772-MON; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 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..240
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208169"
FT   MOTIF           73..78
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   240 AA;  27502 MW;  2333CE2618FF97BB CRC64;
     MLKLLRIFLV LICCILICVL GTIYSFIRFK NPSNVGIVAR WFGRLYPLFG LKVEHRIPQD
     QKQISRAIYI GNHQNNYDMV TISYMVQPRT VSVGKKSLIW IPFFGILYWV TGNIFLDREN
     RTKAHNTMSQ LARRINEDNL SIWMFPEGTR NRGRGLLPFK TGAFHAAISA GVPIIPVVCS
     STHNKINLNR WDNGKVICEI MDPIDVSGYT KDNVRDLAAY CHDLMEKRIA ELDEEIAKGN