ID   ENTH_CITRI              Reviewed;         138 AA.
AC   D2TMN6;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=ROD_06061;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/jb.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG87381.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2TMN6; -.
DR   SMR; D2TMN6; -.
DR   STRING; 637910.ROD_06061; -.
DR   KEGG; cro:ROD_06061; -.
DR   eggNOG; COG2050; Bacteria.
DR   HOGENOM; CLU_089876_13_1_6; -.
DR   OMA; QHGGVYC; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000001889; 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; Reference proteome.
FT   CHAIN           1..138
FT                   /note="Proofreading thioesterase EntH"
FT                   /id="PRO_0000413863"
FT   ACT_SITE        64
FT                   /note="Nucleophile or proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00907"
SQ   SEQUENCE   138 AA;  14992 MW;  E14B09ED2910505C CRC64;
     MMIWKRHLTL AELNATSQNT MVAHLGIVYT RLGDDVLEAE MPVDSRTHQP FGLLHGGASA
     ALAETLGSMA GFLLTRDGQC VVGTELNATH HRPVSQGKVR GVCQPLHLGR QSQSWEIVVF
     DEQGRRCCTC RLGTAVIG