ID   FES_YEREN               Reviewed;         353 AA.
AC   Q56855;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Iron(III) enterobactin esterase {ECO:0000250|UniProtKB:P13039};
DE            EC=3.1.1.108 {ECO:0000250|UniProtKB:P13039};
DE   AltName: Full=Enterochelin esterase;
DE   AltName: Full=Ferric enterobactin esterase;
GN   Name=fes {ECO:0000303|PubMed:10515929};
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 51871 / WA-314 / Serotype O:8;
RX   PubMed=10515929; DOI=10.1128/jb.181.20.6387-6395.1999;
RA   Schubert S., Fischer D., Heesemann J.;
RT   "Ferric enterochelin transport in Yersinia enterocolitica: molecular and
RT   evolutionary aspects.";
RL   J. Bacteriol. 181:6387-6395(1999).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent). Is
CC       responsible for the release of iron from ferric enterobactin.
CC       {ECO:0000250|UniProtKB:P13039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-enterobactin + H(+) + 3 H2O = Fe(III)-[N-(2,3-
CC         dihydroxybenzoyl)-L-serine] + 2 N-(2,3-dihydroxybenzoyl)-L-serine;
CC         Xref=Rhea:RHEA:30111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28199, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010;
CC         EC=3.1.1.108; Evidence={ECO:0000250|UniProtKB:P13039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30112;
CC         Evidence={ECO:0000250|UniProtKB:P13039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-enterobactin + H2O = Fe(III)-[N-(2,3-
CC         dihydroxybenzoyl)-L-serine]3 + H(+); Xref=Rhea:RHEA:59256,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199,
CC         ChEBI:CHEBI:143011; Evidence={ECO:0000250|UniProtKB:P13039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59257;
CC         Evidence={ECO:0000250|UniProtKB:P13039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]3 + H(+) + H2O =
CC         Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + N-(2,3-
CC         dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59260, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143011,
CC         ChEBI:CHEBI:143012; Evidence={ECO:0000250|UniProtKB:P13039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59261;
CC         Evidence={ECO:0000250|UniProtKB:P13039};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + H(+) + H2O =
CC         Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + N-(2,3-
CC         dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59264, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010,
CC         ChEBI:CHEBI:143012; Evidence={ECO:0000250|UniProtKB:P13039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59265;
CC         Evidence={ECO:0000250|UniProtKB:P13039};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13039}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene abrogates enterochelin-
CC       supported growth on iron-chelated media. {ECO:0000269|PubMed:10515929}.
CC   -!- SIMILARITY: Belongs to the Fes family. {ECO:0000305}.
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DR   EMBL; U41370; AAB02191.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56855; -.
DR   SMR; Q56855; -.
DR   ESTHER; yeren-fes; A85-IroE-IroD-Fes-Yiel.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008849; F:enterochelin esterase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR021764; Enterochelin_esterase_N.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF11806; DUF3327; 1.
DR   Pfam; PF00756; Esterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..353
FT                   /note="Iron(III) enterobactin esterase"
FT                   /id="PRO_0000087232"
SQ   SEQUENCE   353 AA;  39840 MW;  AA2FFFBF2E6D4089 CRC64;
     MKSRGLSVST TNEHPDSQRL LADPLAGSES WWQQIAQWGT PLVEPISEDK VRLTFLWREP
     VAGADEPTYS RVYIDVNGVT DHHSTHPETL QRLGQTHVWY WQAEVESDFR GSYSFMPVTA
     EHCLNLPEGT PQERRQAQRN WWISLMDLAQ NDPFNHTAPH SSYRGRPLSA VHLADAIPQT
     AWQPIDAGQQ LPTDTQRLQL ITWHSELLGN SRNVWIYHTH GTEDNAERPL AILLDGQYWA
     TRQPIFGVLD NETDAGRLPA SVYVLIDIID QPHRSVELPC NQDFWQALQT ELLPQVAALQ
     PFTDQASRTV VAGQSFGWVG LAICRITLAA AFWWCAESSP VPSGGRMLII SKL