ID   HSCB_ECO57              Reviewed;         171 AA.
AC   P0A6M1; P36540;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Co-chaperone protein HscB;
DE   AltName: Full=Hsc20;
GN   Name=hscB; OrderedLocusNames=Z3794, ECs3393;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG57641.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36816.1; -; Genomic_DNA.
DR   PIR; A91053; A91053.
DR   RefSeq; NP_311420.1; NC_002695.1.
DR   RefSeq; WP_000384413.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A6M1; -.
DR   SMR; P0A6M1; -.
DR   MINT; P0A6M1; -.
DR   STRING; 155864.EDL933_3689; -.
DR   EnsemblBacteria; AAG57641; AAG57641; Z3794.
DR   EnsemblBacteria; BAB36816; BAB36816; ECs_3393.
DR   GeneID; 60903814; -.
DR   GeneID; 915200; -.
DR   KEGG; ece:Z3794; -.
DR   KEGG; ecs:ECs_3393; -.
DR   PATRIC; fig|386585.9.peg.3544; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OMA; KFMAKLQ; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome.
FT   CHAIN           1..171
FT                   /note="Co-chaperone protein HscB"
FT                   /id="PRO_0000070968"
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