ID   ENTH_SHIF2              Reviewed;         137 AA.
AC   D2A996;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=SFxv_0564;
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017;
RX   PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(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; CP001383; ADA72885.1; -; Genomic_DNA.
DR   RefSeq; WP_000637935.1; NC_017328.1.
DR   AlphaFoldDB; D2A996; -.
DR   SMR; D2A996; -.
DR   EnsemblBacteria; ADA72885; ADA72885; SFxv_0564.
DR   KEGG; sfe:SFxv_0564; -.
DR   PATRIC; fig|591020.3.peg.597; -.
DR   HOGENOM; CLU_089876_13_1_6; -.
DR   OMA; QHGGVYC; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000001884; 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_0000413878"
FT   ACT_SITE        63
FT                   /note="Nucleophile or proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00907"
SQ   SEQUENCE   137 AA;  14927 MW;  03A4E05E598B8BE1 CRC64;
     MIWKRHLTLD ELNATSDNTM VAHLGIVYTL LGDDVLEAEM PVDTRTHQPF GLLHGGASAA
     LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD
     EQGRRCCTCR LGTAVLG