IROE_ECOL6
ID IROE_ECOL6 Reviewed; 318 AA.
AC A0A0H2V871;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Apo-salmochelin esterase {ECO:0000305};
DE EC=3.1.1.107 {ECO:0000269|PubMed:16076215};
DE AltName: Full=Enterobactin hydrolase IroE {ECO:0000303|PubMed:16922493};
GN Name=iroE {ECO:0000303|PubMed:16076215};
GN OrderedLocusNames=c1251 {ECO:0000312|EMBL:AAN79708.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
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).
RN [3] {ECO:0007744|PDB:2GZR, ECO:0007744|PDB:2GZS}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 41-318 OF APOENZYME AND IN
RP COMPLEX WITH INHIBITOR DIISOPROPYL FLUOROPHOSPHONATE, SUBUNIT, DOMAIN,
RP ACTIVE SITE, AND MUTAGENESIS OF ASP-90; ARG-130; SER-189; SER-245; ASP-250;
RP GLU-253 AND HIS-287.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16922493; DOI=10.1021/bi060950i;
RA Larsen N.A., Lin H., Wei R., Fischbach M.A., Walsh C.T.;
RT "Structural characterization of enterobactin hydrolase IroE.";
RL Biochemistry 45:10184-10190(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of both the apo and Fe3(+)-bound
CC forms of enterobactin (Ent), monoglucosyl-C-Ent (MGE), diglucosyl-C-Ent
CC (DGE) and triglucosyl-C-Ent (TGE). It prefers apo siderophores as
CC substrates and hydrolyzes the Fe3(+)-bound siderophores very
CC inefficiently. Tends to hydrolyze the trilactone just once to produce
CC linearized trimers. May hydrolyze and linearize some or all of apo
CC enterobactins while they are being exported.
CC {ECO:0000269|PubMed:16076215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer;
CC Xref=Rhea:RHEA:60384, ChEBI:CHEBI:15377, ChEBI:CHEBI:77805,
CC ChEBI:CHEBI:143020; EC=3.1.1.107;
CC Evidence={ECO:0000269|PubMed:16076215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60385;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + monoglucosyl-enterobactin = [N-(2,3-dihydroxybenzoyl)-L-
CC seryl]2-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine
CC + H(+); Xref=Rhea:RHEA:60412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:142958, ChEBI:CHEBI:143023; EC=3.1.1.107;
CC Evidence={ECO:0000269|PubMed:16076215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60413;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diglucosyl-enterobactin + H2O = H(+) + N-(2,3-
CC dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-
CC dihydroxybenzoyl)-L-serine]2; Xref=Rhea:RHEA:60416,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:142959,
CC ChEBI:CHEBI:143022; EC=3.1.1.107;
CC Evidence={ECO:0000269|PubMed:16076215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60417;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + triglucosyl-enterobactin = [N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine]3 + H(+);
CC Xref=Rhea:RHEA:60420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:142960, ChEBI:CHEBI:143021; EC=3.1.1.107;
CC Evidence={ECO:0000269|PubMed:16076215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60421;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for Ent {ECO:0000269|PubMed:16076215};
CC KM=3.4 uM for Fe-Ent {ECO:0000269|PubMed:16076215};
CC KM=29 uM for MGE {ECO:0000269|PubMed:16076215};
CC KM=4.8 uM for Fe-MGE {ECO:0000269|PubMed:16076215};
CC KM=39 uM for DGE {ECO:0000269|PubMed:16076215};
CC KM=4.6 uM for Fe-DGE {ECO:0000269|PubMed:16076215};
CC KM=155 uM for TGE {ECO:0000269|PubMed:16076215};
CC Note=kcat is 375 min(-1) with Ent as substrate. kcat is 3.0 min(-1)
CC with Fe-Ent as substrate. kcat is 430 min(-1) with MGE as substrate.
CC kcat is 3.2 min(-1) with Fe-MGE as substrate. kcat is 320 min(-1)
CC with DGE as substrate. kcat is 2.5 min(-1) with Fe-DGE as substrate.
CC kcat is 450 min(-1) with TGE as substrate.
CC {ECO:0000269|PubMed:16076215};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16922493}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:16076215}; Single-pass membrane protein
CC {ECO:0000255}; Periplasmic side {ECO:0000305|PubMed:16076215}.
CC -!- DOMAIN: Contains a canonical alpha/beta-hydrolase fold with an atypical
CC catalytic dyad. {ECO:0000269|PubMed:16922493}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79708.1; -; Genomic_DNA.
DR RefSeq; WP_000271272.1; NC_004431.1.
DR PDB; 2GZR; X-ray; 2.30 A; A=41-318.
DR PDB; 2GZS; X-ray; 1.40 A; A=41-318.
DR PDBsum; 2GZR; -.
DR PDBsum; 2GZS; -.
DR AlphaFoldDB; A0A0H2V871; -.
DR SMR; A0A0H2V871; -.
DR STRING; 199310.c1251; -.
DR EnsemblBacteria; AAN79708; AAN79708; c1251.
DR KEGG; ecc:c1251; -.
DR eggNOG; COG2819; Bacteria.
DR HOGENOM; CLU_039834_3_2_6; -.
DR OMA; KPWVEAN; -.
DR BioCyc; MetaCyc:MON-20654; -.
DR BRENDA; 3.1.1.107; 2026.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Serine esterase; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Apo-salmochelin esterase"
FT /id="PRO_5002599607"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 189
FT /evidence="ECO:0000305|PubMed:16922493"
FT ACT_SITE 287
FT /evidence="ECO:0000305|PubMed:16922493"
FT MUTAGEN 90
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 130
FT /note="R->K,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 189
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 245
FT /note="S->D: Retains 60% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 245
FT /note="S->E: Retains 84% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 250
FT /note="D->A: Retains 59% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 250
FT /note="D->N: Retains 72% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 253
FT /note="E->A: Retains 78% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 253
FT /note="E->Q: Retains 92% of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
FT MUTAGEN 287
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16922493"
SQ SEQUENCE 318 AA; 35444 MW; 418876A5F94FA896 CRC64;
MYAREYRSTR PHKAIFFHLS CLTLICSAQV YAKPDMRPLG PNIADKGSVF YHFSATSFDS
VDGTRHYRVW TAVPNTTAPA SGYPILYMLD GNAVMDRLDD ELLKQLSEKT PPVIVAVGYQ
TNLPFDLNSR AYDYTPAAES RKTDLHSGRF SRKSGGSNNF RQLLETRIAP KVEQGLNIDR
QRRGLWGHSY GGLFVLDSWL SSSYFRSYYS ASPSLGRGYD ALLSRVTAVE PLQFCTKHLA
IMEGSATQGD NRETHAVGVL SKIHTTLTIL KDKGVNAVFW DFPNLGHGPM FNASFRQALL
DISGENANYT AGCHELSH
