PLSX_ECOLI
ID PLSX_ECOLI Reviewed; 356 AA.
AC P27247;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019};
GN OrderedLocusNames=b1090, JW5156;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1447160; DOI=10.1128/jb.174.23.7873-7874.1992;
RA Oh W., Larson T.J.;
RT "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the
RT Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 174:7873-7874(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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-30.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
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 reversible formation of acyl-phosphate (acyl-
CC PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00019, ECO:0000269|PubMed:17645809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00019};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with the membrane
CC possibly through PlsY. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59064.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M96793; AAB59064.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74174.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35898.2; -; Genomic_DNA.
DR PIR; G64852; G64852.
DR RefSeq; NP_415608.2; NC_000913.3.
DR RefSeq; WP_000197597.1; NZ_LN832404.1.
DR AlphaFoldDB; P27247; -.
DR SMR; P27247; -.
DR BioGRID; 4261030; 148.
DR DIP; DIP-10517N; -.
DR IntAct; P27247; 1.
DR STRING; 511145.b1090; -.
DR jPOST; P27247; -.
DR PaxDb; P27247; -.
DR PRIDE; P27247; -.
DR EnsemblBacteria; AAC74174; AAC74174; b1090.
DR EnsemblBacteria; BAA35898; BAA35898; BAA35898.
DR GeneID; 946165; -.
DR KEGG; ecj:JW5156; -.
DR KEGG; eco:b1090; -.
DR PATRIC; fig|511145.12.peg.1133; -.
DR EchoBASE; EB1407; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_0_6; -.
DR InParanoid; P27247; -.
DR OMA; HGKSNAR; -.
DR PhylomeDB; P27247; -.
DR BioCyc; EcoCyc:EG11437-MON; -.
DR UniPathway; UPA00085; -.
DR PRO; PR:P27247; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_00019; PlsX; 1.
DR InterPro; IPR003664; FA_synthesis.
DR InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR PANTHER; PTHR30100; PTHR30100; 1.
DR Pfam; PF02504; FA_synthesis; 1.
DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR TIGRFAMs; TIGR00182; plsX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000189875"
SQ SEQUENCE 356 AA; 38214 MW; 89C6C64C57184DF4 CRC64;
MTRLTLALDV MGGDFGPSVT VPAALQALNS NSQLTLLLVG NSDAITPLLA KADFEQRSRL
QIIPAQSVIA SDARPSQAIR ASRGSSMRVA LELVKEGRAQ ACVSAGNTGA LMGLAKLLLK
PLEGIERPAL VTVLPHQQKG KTVVLDLGAN VDCDSTMLVQ FAIMGSVLAE EVVEIPNPRV
ALLNIGEEEV KGLDSIRDAS AVLKTIPSIN YIGYLEANEL LTGKTDVLVC DGFTGNVTLK
TMEGVVRMFL SLLKSQGEGK KRSWWLLLLK RWLQKSLTRR FSHLNPDQYN GACLLGLRGT
VIKSHGAANQ RAFAVAIEQA VQAVQRQVPQ RIAARLESVY PAGFELLDGG KSGTLR
