ID   ENTH_ECOL6              Reviewed;         137 AA.
AC   P0A8Y9; P15050;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Proofreading thioesterase EntH {ECO:0000255|HAMAP-Rule:MF_00907};
DE            EC=3.1.2.- {ECO:0000255|HAMAP-Rule:MF_00907};
DE   AltName: Full=Enterobactin synthase component H {ECO:0000255|HAMAP-Rule:MF_00907};
GN   Name=entH {ECO:0000255|HAMAP-Rule:MF_00907}; OrderedLocusNames=c0684;
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).
CC   -!- FUNCTION: Required for optimal enterobactin synthesis. Acts as a
CC       proofreading enzyme that prevents EntB misacylation by hydrolyzing the
CC       thioester bound existing between EntB and wrongly charged molecules.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. Interacts specifically with the
CC       aryl carrier protein (ArCP) domain of EntB. {ECO:0000255|HAMAP-
CC       Rule:MF_00907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907}.
CC   -!- SIMILARITY: Belongs to the thioesterase PaaI family.
CC       {ECO:0000255|HAMAP-Rule:MF_00907}.
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DR   EMBL; AE014075; AAN79159.1; -; Genomic_DNA.
DR   RefSeq; WP_000637953.1; NC_004431.1.
DR   AlphaFoldDB; P0A8Y9; -.
DR   SMR; P0A8Y9; -.
DR   STRING; 199310.c0684; -.
DR   EnsemblBacteria; AAN79159; AAN79159; c0684.
DR   GeneID; 67416358; -.
DR   KEGG; ecc:c0684; -.
DR   eggNOG; COG2050; Bacteria.
DR   HOGENOM; CLU_089876_13_1_6; -.
DR   OMA; QHGGVYC; -.
DR   BioCyc; ECOL199310:C0684-MON; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00907; Thioesterase_EntH; 1.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR003736; PAAI_dom.
DR   InterPro; IPR026576; Thioesterase_EntH.
DR   InterPro; IPR006683; Thioestr_dom.
DR   Pfam; PF03061; 4HBT; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..137
FT                   /note="Proofreading thioesterase EntH"
FT                   /id="PRO_0000156677"
FT   ACT_SITE        63
FT                   /note="Nucleophile or proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00907"
SQ   SEQUENCE   137 AA;  14970 MW;  C8DF8DE63815F206 CRC64;
     MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA
     LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD
     EQGRRCCTCR LGTAVLG