PLSC_ECOLI
ID PLSC_ECOLI Reviewed; 245 AA.
AC P26647; Q2M9I2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 EC=2.3.1.n4;
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE AltName: Full=Phosphatidic acid synthase;
DE Short=PA synthase;
GN Name=plsC; Synonyms=parF; OrderedLocusNames=b3018, JW2986;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, FORMYLATION AT
RP MET-1, AND SUBCELLULAR LOCATION.
RX PubMed=1557036; DOI=10.1007/bf00280009;
RA Coleman J.;
RT "Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-
RT phosphate acyltransferase (plsC).";
RL Mol. Gen. Genet. 232:295-303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=2211622; DOI=10.1016/s0021-9258(17)44891-5;
RA Coleman J.;
RT "Characterization of Escherichia coli cells deficient in 1-acyl-sn-
RT glycerol-3- phosphate acyltransferase activity.";
RL J. Biol. Chem. 265:17215-17221(1990).
RN [5]
RP FATTY ACYL DONOR SPECIFICITY.
RX PubMed=16949372; DOI=10.1016/j.molcel.2006.06.030;
RA Lu Y.-J., Zhang Y.-M., Grimes K.D., Qi J., Lee R.E., Rock C.O.;
RT "Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive
RT pathogens.";
RL Mol. Cell 23:765-772(2006).
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-ACP as the fatty acyl donor.
CC {ECO:0000269|PubMed:2211622}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n4;
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:0000269|PubMed:1557036};
CC Peripheral membrane protein {ECO:0000269|PubMed:1557036}.
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; M63491; AAA24397.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69186.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76054.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77074.1; -; Genomic_DNA.
DR PIR; S20460; S20460.
DR RefSeq; NP_417490.1; NC_000913.3.
DR RefSeq; WP_000965722.1; NZ_SSZK01000023.1.
DR AlphaFoldDB; P26647; -.
DR SMR; P26647; -.
DR BioGRID; 4261779; 258.
DR DIP; DIP-10516N; -.
DR IntAct; P26647; 2.
DR STRING; 511145.b3018; -.
DR ChEMBL; CHEMBL3309004; -.
DR jPOST; P26647; -.
DR PaxDb; P26647; -.
DR PRIDE; P26647; -.
DR EnsemblBacteria; AAC76054; AAC76054; b3018.
DR EnsemblBacteria; BAE77074; BAE77074; BAE77074.
DR GeneID; 947496; -.
DR KEGG; ecj:JW2986; -.
DR KEGG; eco:b3018; -.
DR PATRIC; fig|1411691.4.peg.3712; -.
DR EchoBASE; EB1351; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_10_3_6; -.
DR InParanoid; P26647; -.
DR OMA; KQRIKLW; -.
DR PhylomeDB; P26647; -.
DR BioCyc; EcoCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON; -.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:P26647; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Formylation; 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_0000208168"
FT MOTIF 73..78
FT /note="HXXXXD motif"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:1557036"
SQ SEQUENCE 245 AA; 27453 MW; E9A1E697E7149838 CRC64;
MLYIFRLIIT VIYSILVCVF GSIYCLFSPR NPKHVATFGH MFGRLAPLFG LKVECRKPTD
AESYGNAIYI ANHQNNYDMV TASNIVQPPT VTVGKKSLLW IPFFGQLYWL TGNLLIDRNN
RTKAHGTIAE VVNHFKKRRI SIWMFPEGTR SRGRGLLPFK TGAFHAAIAA GVPIIPVCVS
TTSNKINLNR LHNGLVIVEM LPPIDVSQYG KDQVRELAAH CRSIMEQKIA ELDKEVAERE
AAGKV
