PLSY_ECOLI
ID PLSY_ECOLI Reviewed; 205 AA.
AC P60782; P31056; Q2M9E6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable glycerol-3-phosphate acyltransferase;
DE AltName: Full=G3P acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15;
DE EC=2.3.1.n5;
DE AltName: Full=Lysophosphatidic acid synthase;
DE Short=LPA synthase;
GN Name=plsY; Synonyms=ygiH; OrderedLocusNames=b3059, JW3031;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-204.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=8389741; DOI=10.1128/jb.175.12.3784-3789.1993;
RA Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M.;
RT "Amplification of the bacA gene confers bacitracin resistance to
RT Escherichia coli.";
RL J. Bacteriol. 175:3784-3789(1993).
RN [4]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP CATALYTIC ACTIVITY, AND 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).
RN [7]
RP FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17645809; DOI=10.1186/1471-2180-7-69;
RA Yoshimura M., Oshima T., Ogasawara N.;
RT "Involvement of the YneS/YgiH and PlsX proteins in phospholipid
RT biosynthesis in both Bacillus subtilis and Escherichia coli.";
RL BMC Microbiol. 7:69-69(2007).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to
CC glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This
CC enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-
CC PO(4) (Probable). {ECO:0000305|PubMed:17645809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:16949372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42300, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n5; Evidence={ECO:0000269|PubMed:16949372};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000305}.
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DR EMBL; U28379; AAA89139.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76095.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77110.1; -; Genomic_DNA.
DR EMBL; L12966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A65094; A65094.
DR RefSeq; NP_417531.1; NC_000913.3.
DR RefSeq; WP_001272796.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P60782; -.
DR SMR; P60782; -.
DR BioGRID; 4259257; 299.
DR IntAct; P60782; 1.
DR STRING; 511145.b3059; -.
DR TCDB; 9.B.31.1.1; the plsy/yqih (plsy) family.
DR jPOST; P60782; -.
DR PaxDb; P60782; -.
DR PRIDE; P60782; -.
DR EnsemblBacteria; AAC76095; AAC76095; b3059.
DR EnsemblBacteria; BAE77110; BAE77110; BAE77110.
DR GeneID; 66673042; -.
DR GeneID; 947561; -.
DR KEGG; ecj:JW3031; -.
DR KEGG; eco:b3059; -.
DR PATRIC; fig|1411691.4.peg.3672; -.
DR EchoBASE; EB1625; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_0_2_6; -.
DR InParanoid; P60782; -.
DR OMA; WRHRGNL; -.
DR PhylomeDB; P60782; -.
DR BioCyc; EcoCyc:EG11674-MON; -.
DR UniPathway; UPA00085; -.
DR PRO; PR:P60782; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..205
FT /note="Probable glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188368"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 205 AA; 22193 MW; 13066C8FBA2543E2 CRC64;
MSAIAPGMIL IAYLCGSISS AILVCRLCGL PDPRTSGSGN PGATNVLRIG GKGAAVAVLI
FDVLKGMLPV WGAYELGVSP FWLGLIAIAA CLGHIWPVFF GFKGGKGVAT AFGAIAPIGW
DLTGVMAGTW LLTVLLSGYS SLGAIVSALI APFYVWWFKP QFTFPVSMLS CLILLRHHDN
IQRLWRRQET KIWTKFKRKR EKDPE
