ID   HSCB_ECOL6              Reviewed;         171 AA.
AC   P0A6M0; P36540;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Co-chaperone protein HscB;
DE   AltName: Full=Hsc20;
GN   Name=hscB; OrderedLocusNames=c3052;
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: Co-chaperone involved in the maturation of iron-sulfur
CC       cluster-containing proteins. Seems to help targeting proteins to be
CC       folded toward HscA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC       Interacts with IscU (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81502.1; -; Genomic_DNA.
DR   RefSeq; WP_000384413.1; NC_004431.1.
DR   AlphaFoldDB; P0A6M0; -.
DR   SMR; P0A6M0; -.
DR   STRING; 199310.c3052; -.
DR   EnsemblBacteria; AAN81502; AAN81502; c3052.
DR   GeneID; 60903814; -.
DR   KEGG; ecc:c3052; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OMA; KFMAKLQ; -.
DR   BioCyc; ECOL199310:C3052-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 1.20.1280.20; -; 1.
DR   HAMAP; MF_00682; HscB; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR004640; HscB.
DR   InterPro; IPR036386; HscB_C_sf.
DR   InterPro; IPR009073; HscB_oligo_C.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR14021; PTHR14021; 1.
DR   Pfam; PF07743; HSCB_C; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF47144; SSF47144; 1.
DR   TIGRFAMs; TIGR00714; hscB; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone.
FT   CHAIN           1..171
FT                   /note="Co-chaperone protein HscB"
FT                   /id="PRO_0000070967"
FT   DOMAIN          2..74
FT                   /note="J"
SQ   SEQUENCE   171 AA;  20138 MW;  095193EE98AA60C9 CRC64;
     MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT
     LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR
     VKKMFDTRHQ LMVEQLDNET WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F