ENTB_ECO57
ID ENTB_ECO57 Reviewed; 285 AA.
AC P0ADI5; P15048;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Enterobactin synthase component B {ECO:0000250|UniProtKB:P0ADI4};
DE EC=6.3.2.14 {ECO:0000250|UniProtKB:P0ADI4};
DE AltName: Full=Enterobactin biosynthesis bifunctional protein EntB {ECO:0000250|UniProtKB:P0ADI4};
DE AltName: Full=Enterochelin synthase B {ECO:0000250|UniProtKB:P0ADI4};
DE Includes:
DE RecName: Full=Isochorismatase {ECO:0000250|UniProtKB:P0ADI4};
DE EC=3.3.2.1 {ECO:0000250|UniProtKB:P0ADI4};
DE AltName: Full=2,3-dihydro-2,3-dihydroxybenzoat synthase {ECO:0000250|UniProtKB:P0ADI4};
DE AltName: Full=Isochorismate lyase {ECO:0000250|UniProtKB:P0ADI4};
DE Includes:
DE RecName: Full=Aryl carrier protein {ECO:0000250|UniProtKB:P0ADI4};
DE Short=ArCP {ECO:0000250|UniProtKB:P0ADI4};
GN Name=entB {ECO:0000250|UniProtKB:P0ADI4}; OrderedLocusNames=Z0737, ECs0634;
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. EntB is a
CC bifunctional protein that serves as an isochorismate lyase and an aryl
CC carrier protein (ArCP). Catalyzes the conversion of isochorismate to
CC 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-
CC dihydroxybenzoate (DHB). In the enterobactin assembly, EntB functions
CC as an aryl carrier protein phosphopantetheinylated near the C terminus
CC by EntD to yield holo-EntB, which is then acylated by EntE with 2,3-
CC dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then this product will
CC serve in the formation of the amide bond between 2,3-dihydroxybenzoate
CC (DHB) and L-serine. {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6
CC diphosphate + enterobactin + 4 H(+); Xref=Rhea:RHEA:30571,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805,
CC ChEBI:CHEBI:456215; EC=6.3.2.14;
CC Evidence={ECO:0000250|UniProtKB:P0ADI4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-
CC dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1;
CC Evidence={ECO:0000250|UniProtKB:P0ADI4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0ADI4};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme complex
CC called enterobactin synthase. Dimer. {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-
CC dihydroxybenzoate in a reaction catalyzed by EntE.
CC {ECO:0000250|UniProtKB:P0ADI4}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the isochorismatase
CC family. {ECO:0000250|UniProtKB:P0ADI4}.
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DR EMBL; AE005174; AAG54930.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34057.1; -; Genomic_DNA.
DR PIR; B90708; B90708.
DR PIR; F85558; F85558.
DR RefSeq; NP_308661.1; NC_002695.1.
DR RefSeq; WP_001007138.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ADI5; -.
DR SMR; P0ADI5; -.
DR STRING; 155864.EDL933_0665; -.
DR EnsemblBacteria; AAG54930; AAG54930; Z0737.
DR EnsemblBacteria; BAB34057; BAB34057; ECs_0634.
DR GeneID; 916993; -.
DR KEGG; ece:Z0737; -.
DR KEGG; ecs:ECs_0634; -.
DR PATRIC; fig|386585.9.peg.744; -.
DR eggNOG; COG1535; Bacteria.
DR eggNOG; COG3433; Bacteria.
DR HOGENOM; CLU_068979_2_0_6; -.
DR OMA; RDIKPFF; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; ISS:UniProtKB.
DR GO; GO:0008908; F:isochorismatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016291; Isochorismatase.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00857; Isochorismatase; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001111; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Enterobactin biosynthesis; Hydrolase; Ligase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0ADI4"
FT CHAIN 2..285
FT /note="Enterobactin synthase component B"
FT /id="PRO_0000201823"
FT DOMAIN 209..284
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 2..213
FT /note="Isochorismatase"
FT /evidence="ECO:0000250|UniProtKB:P0ADI4"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADI4"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADI4"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADI4"
FT MOD_RES 245
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 285 AA; 32554 MW; E98C62D5ED23BAB1 CRC64;
MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC PMMEQVIANI
AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT RSPEQQKVVD RLTPDADDTV
LVKWRYSAFH RSPLEQMLKE SGRNQLIITG VYAHIGCMTT ATDAFMRDIK PFMVADALAD
FSRDEHLMSL KYVAGRSGRV VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID
YGLDSVRMMA LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
