PLSC_HELPJ
ID PLSC_HELPJ Reviewed; 237 AA.
AC Q9ZJN8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=jhp_1267;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06852.1; -; Genomic_DNA.
DR PIR; B71827; B71827.
DR RefSeq; WP_000841245.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJN8; -.
DR SMR; Q9ZJN8; -.
DR STRING; 85963.jhp_1267; -.
DR EnsemblBacteria; AAD06852; AAD06852; jhp_1267.
DR KEGG; hpj:jhp_1267; -.
DR PATRIC; fig|85963.30.peg.1304; -.
DR eggNOG; COG0204; Bacteria.
DR OMA; NICWIAK; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
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; Transferase.
FT CHAIN 1..237
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000208171"
FT MOTIF 74..79
FT /note="HXXXXD motif"
SQ SEQUENCE 237 AA; 27188 MW; E10F517D42A1731F CRC64;
MKSNKKSNHL RAIYRALVIA IGLAVIIVFN YFNRKNNNAR SSRRACSCFF SLTGVNLEKI
GSFDTGAKLI VLNHQSLLDI IYLEAYHPSN ICWIAKKELG EIPFYGHALT DTGMILIDRE
DKKGIVSLLK ACKEKLDQNR PLVIFPEGTR GKGGEKFLPF KQGAKIIAEK FQLKIQPMVL
INSIKIFNSK PLEAYKARTR LVMLESYTPD FSSPTWYEEL QERMQKEYLK HYHELNA
