(data stored in ACNUC10821 zone)

SWISSPROT: C8U2W1_ECO10

ID   C8U2W1_ECO10            Unreviewed;       137 AA.
AC   C8U2W1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Proofreading thioesterase EntH {ECO:0000256|HAMAP-Rule:MF_00907};
DE            EC=3.1.2.- {ECO:0000256|HAMAP-Rule:MF_00907};
DE   AltName: Full=Enterobactin synthase component H {ECO:0000256|HAMAP-Rule:MF_00907};
GN   Name=entH {ECO:0000256|HAMAP-Rule:MF_00907,
GN   ECO:0000313|EMBL:BAI29469.1};
GN   OrderedLocusNames=ECO103_0605 {ECO:0000313|EMBL:BAI29469.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29469.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29469.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Required for optimal enterobactin synthesis. Acts as a
CC       proofreading enzyme that prevents EntB misacylation by hydrolyzing
CC       the thioester bound existing between EntB and wrongly charged
CC       molecules. {ECO:0000256|HAMAP-Rule:MF_00907}.
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00907}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. Interacts specifically
CC       with the aryl carrier protein (ArCP) domain of EntB.
CC       {ECO:0000256|HAMAP-Rule:MF_00907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00907}.
CC   -!- SIMILARITY: Belongs to the thioesterase PaaI family.
CC       {ECO:0000256|HAMAP-Rule:MF_00907}.
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DR   EMBL; AP010958; BAI29469.1; -; Genomic_DNA.
DR   RefSeq; WP_000637953.1; NC_013353.1.
DR   SMR; C8U2W1; -.
DR   EnsemblBacteria; BAI29469; BAI29469; ECO103_0605.
DR   KEGG; eoh:ECO103_0605; -.
DR   HOGENOM; HOG000066991; -.
DR   OMA; HGGVYCS; -.
DR   BioCyc; ECOL585395:ECO103_RS03155-MONOMER; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U2W1.
DR   SWISS-2DPAGE; C8U2W1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00907};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00907}.
FT   DOMAIN       50    127       4HBT. {ECO:0000259|Pfam:PF03061}.
FT   ACT_SITE     63     63       Nucleophile or proton acceptor.
FT                                {ECO:0000256|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
//

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