FES_ECOL6
ID FES_ECOL6 Reviewed; 400 AA.
AC A0A0H2V760;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Iron(III) enterobactin esterase {ECO:0000305};
DE EC=3.1.1.108 {ECO:0000269|PubMed:16076215};
DE AltName: Full=Fe-Ent esterase {ECO:0000303|PubMed:16076215};
GN Name=fes {ECO:0000303|PubMed:16076215};
GN OrderedLocusNames=c0671 {ECO:0000312|EMBL:AAN79146.1};
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16076215; DOI=10.1021/ja0522027;
RA Lin H., Fischbach M.A., Liu D.R., Walsh C.T.;
RT "In vitro characterization of salmochelin and enterobactin trilactone
RT hydrolases IroD, IroE, and Fes.";
RL J. Am. Chem. Soc. 127:11075-11084(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent). Is
CC responsible for the release of iron from ferric enterobactin. Also
CC catalyzes the hydrolysis of iron-free enterobactin (Ent). Hydrolyzes
CC ferric monoglucosyl-C-Ent (Fe-MGE) poorly and does not hydrolyze ferric
CC diglucosyl-C-Ent (Fe-DGE) or ferric triglucosyl-C-Ent (Fe-TGE) at all.
CC Also hydrolyzes apo MGE, but catalyzes the hydrolysis of apo DGE very
CC poorly, and does not process apo TGE at all. The catalytic efficiency
CC for processing Fe-Ent is much higher than that for apo Ent, suggesting
CC that Fe-Ent is the physiological substrate.
CC {ECO:0000269|PubMed:16076215}.
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:0000269|PubMed:16076215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30112;
CC Evidence={ECO:0000269|PubMed:16076215};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for MGE {ECO:0000269|PubMed:16076215};
CC KM=0.29 uM for Fe-MGE {ECO:0000269|PubMed:16076215};
CC Note=kcat is 9 min(-1) with Fe-Ent as substrate. kcat is 850 min(-1)
CC with MGE as substrate. kcat is 1.4 min(-1) with Fe-MGE as substrate.
CC {ECO:0000269|PubMed:16076215};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13039}.
CC -!- SIMILARITY: Belongs to the Fes family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79146.1; -; Genomic_DNA.
DR RefSeq; WP_000125846.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2V760; -.
DR SMR; A0A0H2V760; -.
DR STRING; 199310.c0671; -.
DR EnsemblBacteria; AAN79146; AAN79146; c0671.
DR KEGG; ecc:c0671; -.
DR eggNOG; COG2382; Bacteria.
DR HOGENOM; CLU_024314_3_0_6; -.
DR OMA; VEQCPID; -.
DR Proteomes; UP000001410; Chromosome.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..400
FT /note="Iron(III) enterobactin esterase"
FT /id="PRO_0000452105"
SQ SEQUENCE 400 AA; 45641 MW; 43F2DE2C4E0B4594 CRC64;
MTALKVGSES WWQSKHGPEW QRLNDEMFEV TFWWRDPQGS EEYSTIKRVW VYITGVTDHH
QNSQPRSMQR IAGTDVWQWT TQLNANWRGS YCFIPTERDD IFSAPSPDRL ELREGWRKLL
PQAIADPLNP QSWKGGRGHA VSALEMPQAP LQPGWDCPQA PETPAKEIIW KSERLKNSRR
VWIFTTGDAT AEERPLAVLL DGEFWAQSMP VWPALTSLTH RRQLPPAVYV LIDAIDTTHR
AHELPCNADF WLAVQQELLP QVKAIAPFSD RADRTVVAGQ SFGGLSALYA GLHWPERFGC
VLSQSGSYWW PHRGGHQEGM LLEQLNTGEV SAEGLRIVLE AGVREPMIMQ ANQALYAQLH
PLKESIFWRQ VDGGHDALCW RGGLMQGLID LWQPLFHDRS
