FES_ECOLI
ID FES_ECOLI Reviewed; 400 AA.
AC P13039; P77094;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Iron(III) enterobactin esterase {ECO:0000305};
DE EC=3.1.1.108 {ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808, ECO:0000269|PubMed:8148617};
DE AltName: Full=Enterochelin esterase {ECO:0000303|PubMed:150859};
DE AltName: Full=Ferric enterobactin esterase {ECO:0000303|PubMed:1534808};
GN Name=fes {ECO:0000303|PubMed:3040679}; OrderedLocusNames=b0585, JW0576;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-31.
RX PubMed=2974033; DOI=10.1016/s0021-9258(18)37361-7;
RA Pettis G.S., Brickman T.J., McIntosh M.A.;
RT "Transcriptional mapping and nucleotide sequence of the Escherichia coli
RT fepA-fes enterobactin region. Identification of a unique iron-regulated
RT bidirectional promoter.";
RL J. Biol. Chem. 263:18857-18863(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-307.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [6]
RP PROTEIN SEQUENCE OF 6-15.
RC STRAIN=K12 / BW25113;
RX PubMed=23908556; DOI=10.1074/mcp.m113.029165;
RA Krug K., Carpy A., Behrends G., Matic K., Soares N.C., Macek B.;
RT "Deep coverage of the Escherichia coli proteome enables the assessment of
RT false discovery rates in simple proteogenomic experiments.";
RL Mol. Cell. Proteomics 12:3420-3430(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=150859; DOI=10.1016/0005-2744(78)90216-4;
RA Greenwood K.T., Luke R.K.;
RT "Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia
RT Coli K-12. Properties of enterochelin esterase.";
RL Biochim. Biophys. Acta 525:209-218(1978).
RN [8]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=3040679; DOI=10.1128/jb.169.9.4154-4162.1987;
RA Pettis G.S., McIntosh M.A.;
RT "Molecular characterization of the Escherichia coli enterobactin cistron
RT entF and coupled expression of entF and the fes gene.";
RL J. Bacteriol. 169:4154-4162(1987).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1534808; DOI=10.1016/s0021-9258(19)49846-3;
RA Brickman T.J., McIntosh M.A.;
RT "Overexpression and purification of ferric enterobactin esterase from
RT Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and
RT its iron complex.";
RL J. Biol. Chem. 267:12350-12355(1992).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8148617; DOI=10.1007/bf00140485;
RA Winkelmann G., Cansier A., Beck W., Jung G.;
RT "HPLC separation of enterobactin and linear 2,3-dihydroxybenzoylserine
RT derivatives: a study on mutants of Escherichia coli defective in regulation
RT (fur), esterase (fes) and transport (fepA).";
RL BioMetals 7:149-154(1994).
RN [11]
RP INDUCTION.
RX PubMed=9573216; DOI=10.1128/jb.180.9.2579-2582.1998;
RA Escolar L., Perez-Martin J., de Lorenzo V.;
RT "Coordinated repression in vitro of the divergent fepA-fes promoters of
RT Escherichia coli by the iron uptake regulation (Fur) protein.";
RL J. Bacteriol. 180:2579-2582(1998).
CC -!- FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent)
CC (PubMed:150859, PubMed:1534808, PubMed:8148617). Is responsible for the
CC release of iron from ferric enterobactin (PubMed:1534808). Also
CC catalyzes the hydrolysis of iron-free enterobactin (Ent)
CC (PubMed:150859, PubMed:1534808, PubMed:8148617). Cleavage of ferric
CC enterobactin results in a mixture of three hydrolysis products, 2,3-
CC dihydroxybenzoylserine (DHBS), the linear dimer (DHBS)2 and the linear
CC trimer (DHBS)3, while cleavage of iron-free enterobactin yields only
CC the monomer (PubMed:8148617). Hydrolysis of ferric enterobactin is less
CC efficient than hydrolysis of unliganded enterobactin (PubMed:150859,
CC PubMed:1534808). It also cleaves the aluminum (III) complex at a rate
CC similar to the ferric complex (PubMed:1534808).
CC {ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808,
CC ECO:0000269|PubMed:8148617}.
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:150859,
CC ECO:0000269|PubMed:1534808, ECO:0000269|PubMed:8148617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30112;
CC Evidence={ECO:0000269|PubMed:150859, ECO:0000269|PubMed:1534808,
CC ECO:0000269|PubMed:8148617};
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:0000269|PubMed:8148617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59257;
CC Evidence={ECO:0000269|PubMed:8148617};
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:0000269|PubMed:8148617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59261;
CC Evidence={ECO:0000269|PubMed:8148617};
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:0000269|PubMed:8148617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59265;
CC Evidence={ECO:0000269|PubMed:8148617};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide.
CC {ECO:0000269|PubMed:150859}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1534808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1534808}.
CC -!- INDUCTION: Expression is increased under iron stress (PubMed:3040679).
CC Repressed by Fur under iron-rich conditions (PubMed:9573216).
CC {ECO:0000269|PubMed:3040679, ECO:0000269|PubMed:9573216}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to produce linear DHBS
CC compounds. {ECO:0000269|PubMed:8148617}.
CC -!- SIMILARITY: Belongs to the Fes family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23757.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA35226.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J04216; AAA23757.1; ALT_INIT; Genomic_DNA.
DR EMBL; U82598; AAB40784.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73686.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35226.2; ALT_INIT; Genomic_DNA.
DR PIR; A31958; BVECES.
DR RefSeq; NP_415117.2; NC_000913.3.
DR RefSeq; WP_000125843.1; NZ_SSZK01000032.1.
DR AlphaFoldDB; P13039; -.
DR SMR; P13039; -.
DR BioGRID; 4259896; 327.
DR DIP; DIP-9598N; -.
DR IntAct; P13039; 5.
DR STRING; 511145.b0585; -.
DR ESTHER; ecoli-fes; A85-IroE-IroD-Fes-Yiel.
DR PaxDb; P13039; -.
DR PRIDE; P13039; -.
DR EnsemblBacteria; AAC73686; AAC73686; b0585.
DR EnsemblBacteria; BAA35226; BAA35226; BAA35226.
DR GeneID; 945181; -.
DR KEGG; ecj:JW0576; -.
DR KEGG; eco:b0585; -.
DR PATRIC; fig|1411691.4.peg.1686; -.
DR EchoBASE; EB0295; -.
DR eggNOG; COG2382; Bacteria.
DR HOGENOM; CLU_024314_3_0_6; -.
DR InParanoid; P13039; -.
DR OMA; VEQCPID; -.
DR BioCyc; EcoCyc:EG10299-MON; -.
DR BioCyc; MetaCyc:EG10299-MON; -.
DR PHI-base; PHI:4859; -.
DR PRO; PR:P13039; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008849; F:enterochelin esterase activity; IDA:EcoliWiki.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0046214; P:enterobactin catabolic process; IMP:EcoCyc.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:EcoCyc.
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; Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..400
FT /note="Iron(III) enterobactin esterase"
FT /id="PRO_0000087230"
SQ SEQUENCE 400 AA; 45652 MW; EDB7C0F043A8112D CRC64;
MTALKVGSES WWQSKHGPEW QRLNDEMFEV TFWWRDPQGS EEYSTIKRVW VYITGVTDHH
QNSQPQSMQR IAGTNVWQWT TQLNANWRGS YCFIPTERDD IFSVPSPDRL ELREGWRKLL
PQAIADPLNL QSWKGGRGHA VSALEMPQAP LQPGWDCPQA PEIPAKEIIW KSERLKKSRR
VWIFTTGDAT AEERPLAVLL DGEFWAQSMP VWPVLTSLTH RQQLPPAVYV LIDAIDTTHR
AHELPCNADF WLAVQQELLP LVKAIAPFSD RADRTVVAGQ SFGGLSALYA GLHWPERFGC
VLSQSGSYWW PHRGGQQEGV LLEKLKAGEV SAEGLRIVLE AGIREPMIMR ANQALYAQLH
PIKESIFWRQ VDGGHDALCW RGGLMQGLID LWQPLFHDRS
