ACPS_ECOLI
ID ACPS_ECOLI Reviewed; 126 AA.
AC P24224; Q2MAG7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101};
DE AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101};
GN Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101}; Synonyms=dpj;
GN OrderedLocusNames=b2563, JW2547;
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=1537799; DOI=10.1128/jb.174.5.1544-1553.1992;
RA Takiff H.E., Baker T., Copeland T., Chen S.-M., Court D.L.;
RT "Locating essential Escherichia coli genes by using mini-Tn10 transposons:
RT the pdxJ operon.";
RL J. Bacteriol. 174:1544-1553(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1537800; DOI=10.1128/jb.174.5.1554-1567.1992;
RA Lam H.-M., Tancula E., Dempsey W.B., Winkler M.E.;
RT "Suppression of insertions in the complex pdxJ operon of Escherichia coli
RT K-12 by lon and other mutations.";
RL J. Bacteriol. 174:1554-1567(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP AND MASS SPECTROMETRY.
RC STRAIN=K12;
RX PubMed=7559576; DOI=10.1074/jbc.270.42.24658;
RA Lambalot R.H., Walsh C.T.;
RT "Cloning, overproduction, and characterization of the Escherichia coli
RT holo-acyl carrier protein synthase.";
RL J. Biol. Chem. 270:24658-24661(1995).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND MUTAGENESIS OF GLY-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10625633; DOI=10.1074/jbc.275.2.959;
RA Flugel R.S., Hwangbo Y., Lambalot R.H., Cronan J.E. Jr., Walsh C.T.;
RT "Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in
RT Escherichia coli.";
RL J. Biol. Chem. 275:959-968(2000).
CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC the 'Ser-36' of acyl-carrier-protein. {ECO:0000269|PubMed:7559576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101,
CC ECO:0000269|PubMed:7559576};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101,
CC ECO:0000269|PubMed:7559576};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7559576}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=13950; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7559576};
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000255|HAMAP-Rule:MF_00101}.
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DR EMBL; M76470; AAA21846.1; -; Genomic_DNA.
DR EMBL; M74526; AAA24316.1; -; Genomic_DNA.
DR EMBL; D64044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U36841; AAA79825.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75616.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76739.1; -; Genomic_DNA.
DR PIR; B42294; B42294.
DR RefSeq; NP_417058.1; NC_000913.3.
DR RefSeq; WP_000986023.1; NZ_STEB01000011.1.
DR PDB; 5VBX; X-ray; 2.05 A; A/B/C=1-126.
DR PDB; 5VCB; X-ray; 4.10 A; A/B/C/G/H/I/M/N/O/S/T/U/a/b/c=1-126.
DR PDB; 5XU7; X-ray; 1.84 A; A/B/C=1-126.
DR PDB; 5XUH; X-ray; 2.02 A; A/B/C=1-126.
DR PDBsum; 5VBX; -.
DR PDBsum; 5VCB; -.
DR PDBsum; 5XU7; -.
DR PDBsum; 5XUH; -.
DR AlphaFoldDB; P24224; -.
DR SMR; P24224; -.
DR BioGRID; 4260598; 286.
DR DIP; DIP-9047N; -.
DR IntAct; P24224; 13.
DR STRING; 511145.b2563; -.
DR PaxDb; P24224; -.
DR PRIDE; P24224; -.
DR EnsemblBacteria; AAC75616; AAC75616; b2563.
DR EnsemblBacteria; BAE76739; BAE76739; BAE76739.
DR GeneID; 947037; -.
DR KEGG; ecj:JW2547; -.
DR KEGG; eco:b2563; -.
DR PATRIC; fig|1411691.4.peg.4171; -.
DR EchoBASE; EB0243; -.
DR eggNOG; COG0736; Bacteria.
DR HOGENOM; CLU_089696_3_1_6; -.
DR InParanoid; P24224; -.
DR OMA; DERHYAV; -.
DR PhylomeDB; P24224; -.
DR BioCyc; EcoCyc:HOLO-ACP-SYNTH-MON; -.
DR BioCyc; MetaCyc:HOLO-ACP-SYNTH-MON; -.
DR BRENDA; 2.7.8.7; 2026.
DR PRO; PR:P24224; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; TAS:EcoliWiki.
DR GO; GO:0006633; P:fatty acid biosynthetic process; NAS:EcoliWiki.
DR GO; GO:0018070; P:peptidyl-serine phosphopantetheinylation; IDA:EcoliWiki.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00516; acpS; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7559576"
FT CHAIN 2..126
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175643"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT MUTAGEN 5
FT /note="G->D: 5-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:10625633"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5XU7"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5XU7"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5XU7"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:5XU7"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:5XU7"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:5XU7"
SQ SEQUENCE 126 AA; 14052 MW; A80628315E69731E CRC64;
MAILGLGTDI VEIARIEAVI ARSGDRLARR VLSDNEWAIW KTHHQPVRFL AKRFAVKEAA
AKAFGTGIRN GLAFNQFEVF NDELGKPRLR LWGEALKLAE KLGVANMHVT LADERHYACA
TVIIES
