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ENTH_SALPB
ID   ENTH_SALPB              Reviewed;         137 AA.
AC   A9MVB6;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=SPAB_02964;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX68328.1; -; Genomic_DNA.
DR   RefSeq; WP_000637966.1; NC_010102.1.
DR   AlphaFoldDB; A9MVB6; -.
DR   SMR; A9MVB6; -.
DR   KEGG; spq:SPAB_02964; -.
DR   PATRIC; fig|1016998.12.peg.2795; -.
DR   HOGENOM; CLU_089876_13_1_6; -.
DR   OMA; QHGGVYC; -.
DR   BioCyc; SENT1016998:SPAB_RS12075-MON; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000008556; 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_0000413874"
FT   ACT_SITE        63
FT                   /note="Nucleophile or proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00907"
SQ   SEQUENCE   137 AA;  14925 MW;  2C04E6D14B94F28B CRC64;
     MIWKRHLTLD ELNATSQNTL VAHLGIVYTR LGDDVLEAEM PVDARTHQPF GLLHGGASAA
     LAETLGSMAG YLMTRDGQCV VGTELNATHH RAVSQGKVRG VCLPLHLGRQ NQSWEITLFD
     EQGRRCCTCR LGTAVMG
 
 
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