PLSC_SALTY
ID PLSC_SALTY Reviewed; 245 AA.
AC P0A257; P26974;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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; Synonyms=parF; OrderedLocusNames=STM3173;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1751451;
RA Luttinger A.L., Springer A.L., Schmid M.B.;
RT "A cluster of genes that affects nucleoid segregation in Salmonella
RT typhimurium.";
RL New Biol. 3:687-697(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-245.
RC STRAIN=LT2;
RA Cong J., Schmid M.B.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating an acyl moiety at the 2 position. This enzyme can
CC utilize either acyl-CoA or acyl-acyl-carrier-protein as the fatty acyl
CC donor.
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; Peripheral membrane protein.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M68936; AAA27181.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22047.1; -; Genomic_DNA.
DR EMBL; U09309; AAA56678.1; ALT_SEQ; Unassigned_DNA.
DR PIR; B45582; B45582.
DR RefSeq; NP_462088.1; NC_003197.2.
DR RefSeq; WP_000965730.1; NC_003197.2.
DR AlphaFoldDB; P0A257; -.
DR SMR; P0A257; -.
DR STRING; 99287.STM3173; -.
DR PaxDb; P0A257; -.
DR EnsemblBacteria; AAL22047; AAL22047; STM3173.
DR GeneID; 1254696; -.
DR KEGG; stm:STM3173; -.
DR PATRIC; fig|99287.12.peg.3364; -.
DR HOGENOM; CLU_027938_10_3_6; -.
DR OMA; KQRIKLW; -.
DR PhylomeDB; P0A257; -.
DR BioCyc; SENT99287:STM3173-MON; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000001014; 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..245
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000208178"
FT MOTIF 73..78
FT /note="HXXXXD motif"
SQ SEQUENCE 245 AA; 27339 MW; 5361B851BC96D919 CRC64;
MLYIFRLIVT VIYSILVCVF GSIYCLFSPR NPKHVATFGH MFGRLAPLFG LKVECRKPAD
AENYGNAIYI ANHQNNYDMV TAANIVQPPT VTVGKKSLLW IPFFGQLYWL TGNLLIDRNN
RAKAHSTIAA VVNHFKKRRI SIWMFPEGTR SRGRGLLPFK TGAFHAAIAA GVPIIPVCVS
NTSNKVNLNR LNNGLVIVEM LPPVDVSEYG KDQVRELAAH CRALMEQKIA ELDKEVAERE
ATGKV
