PLSC_HELPY
ID PLSC_HELPY Reviewed; 240 AA.
AC O25903;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=HP_1348;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08393.1; -; Genomic_DNA.
DR PIR; D64688; D64688.
DR RefSeq; NP_208140.1; NC_000915.1.
DR RefSeq; WP_000841286.1; NC_018939.1.
DR AlphaFoldDB; O25903; -.
DR SMR; O25903; -.
DR STRING; 85962.C694_06955; -.
DR PaxDb; O25903; -.
DR EnsemblBacteria; AAD08393; AAD08393; HP_1348.
DR KEGG; hpy:HP_1348; -.
DR PATRIC; fig|85962.47.peg.1443; -.
DR eggNOG; COG0204; Bacteria.
DR OMA; NICWIAK; -.
DR PhylomeDB; O25903; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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_0000208170"
FT MOTIF 74..79
FT /note="HXXXXD motif"
SQ SEQUENCE 240 AA; 27745 MW; 22BD5D0EB190BBDD CRC64;
MKSNKKSNRL RAIYRALVIA IGLAVIIVFN YFNRKNNNAR SSRRACSCFF SLTGVNLEKI
GTFDTDAKLI VLNHQSLLDI IYLEAYHPRN ICWIAKKELG EIPFYGHALT DTGMILIDRE
DKKGIVSLLK ACKEKLDQNR PLVIFPEGTR GKGGEKFLPF KQGAKIIAEK FQLKIQPMVL
INSIKIFNSK PLEAYKARTR LVMLESYTPD FNSPTWYEEL QERMQKEYLK HYHELNPSEQ