ENTD_ECO57
ID ENTD_ECO57 Reviewed; 206 AA.
AC P0A3B9; Q54153; Q8XBW8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Enterobactin synthase component D {ECO:0000250|UniProtKB:P19925};
DE AltName: Full=4'-phosphopantetheinyl transferase EntD {ECO:0000250|UniProtKB:P19925};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:P19925};
DE AltName: Full=Enterochelin synthase D {ECO:0000250|UniProtKB:P19925};
GN Name=entD {ECO:0000250|UniProtKB:P19925}; OrderedLocusNames=Z0723, ECs0622;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-
CC dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding
CC for the three catechol functionalities that provide hexadentate
CC coordination for the tightly ligated iron(2+) atoms. Plays an essential
CC role in the assembly of the enterobactin by catalyzing the transfer of
CC the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-
CC domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their
CC holo-forms which make them competent for the activation of 2,3-
CC dihydroxybenzoate (DHB) and L-serine, respectively.
CC {ECO:0000250|UniProtKB:P19925}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[aryl-carrier protein] + CoA = adenosine 3',5'-
CC bisphosphate + H(+) + holo-[aryl-carrier protein];
CC Xref=Rhea:RHEA:48404, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC Evidence={ECO:0000250|UniProtKB:P19925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[peptidyl-carrier protein] + CoA = adenosine 3',5'-
CC bisphosphate + H(+) + holo-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:46228, Rhea:RHEA-COMP:11479, Rhea:RHEA-COMP:11480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC Evidence={ECO:0000250|UniProtKB:P19925};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P24224};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P19925}.
CC -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex called
CC enterobactin synthase. {ECO:0000250|UniProtKB:P19925}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19925}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family.
CC {ECO:0000250|UniProtKB:P19925}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG54917.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB34045.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG54917.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB34045.1; ALT_INIT; Genomic_DNA.
DR PIR; A85557; A85557.
DR PIR; F90706; F90706.
DR RefSeq; NP_308649.2; NC_002695.1.
DR RefSeq; WP_001506608.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A3B9; -.
DR SMR; P0A3B9; -.
DR STRING; 155864.EDL933_0651; -.
DR EnsemblBacteria; AAG54917; AAG54917; Z0723.
DR EnsemblBacteria; BAB34045; BAB34045; ECs_0622.
DR GeneID; 58391511; -.
DR GeneID; 916981; -.
DR KEGG; ece:Z0723; -.
DR KEGG; ecs:ECs_0622; -.
DR PATRIC; fig|386585.9.peg.730; -.
DR eggNOG; COG2977; Bacteria.
DR HOGENOM; CLU_075076_1_0_6; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009366; C:enterobactin synthetase complex; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR041354; 4PPT_N.
DR InterPro; IPR003542; Enbac_synth_compD-like.
DR PANTHER; PTHR38096; PTHR38096; 1.
DR Pfam; PF17837; 4PPT_N; 1.
DR Pfam; PF01648; ACPS; 1.
DR PRINTS; PR01399; ENTSNTHTASED.
DR SUPFAM; SSF56214; SSF56214; 1.
PE 3: Inferred from homology;
KW Enterobactin biosynthesis; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..206
FT /note="Enterobactin synthase component D"
FT /id="PRO_0000206070"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 23131 MW; 68005CD6E9C6AE0C CRC64;
MKTTHTSLPF AGHTLHFVEF DPANFCEQDL LWLPHYAQLQ HAGRKRKTEH LAGRIAAVYA
LREYGYKCVP AIGELRQPVW PAEVYGSISH CGATALAVVS RQPIGVDIEE IFSAQTATEL
TDNIITPAEH ERLADCGLAF SLALTLAFSA KESAFKASEI QTDAGFLDYQ IISWNKQQVI
IHRENEMFAV HWQIKEKIVI TLCQHD
