HSCB_SHIDS
ID HSCB_SHIDS Reviewed; 171 AA.
AC Q32D37;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Co-chaperone protein HscB {ECO:0000255|HAMAP-Rule:MF_00682};
DE AltName: Full=Hsc20 {ECO:0000255|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=SDY_2723;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00682}.
CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC Interacts with IscU. {ECO:0000255|HAMAP-Rule:MF_00682}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000255|HAMAP-
CC Rule:MF_00682}.
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DR EMBL; CP000034; ABB62768.1; -; Genomic_DNA.
DR RefSeq; WP_000384418.1; NC_007606.1.
DR RefSeq; YP_404259.1; NC_007606.1.
DR AlphaFoldDB; Q32D37; -.
DR SMR; Q32D37; -.
DR STRING; 300267.SDY_2723; -.
DR EnsemblBacteria; ABB62768; ABB62768; SDY_2723.
DR KEGG; sdy:SDY_2723; -.
DR PATRIC; fig|300267.13.peg.3284; -.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OMA; KFMAKLQ; -.
DR Proteomes; UP000002716; 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_1000083048"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ SEQUENCE 171 AA; 20166 MW; 095193F8E9CD60C9 CRC64;
MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT
LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR
VKKMFDTRHQ LMVEQLDNET WDAVADTVRK LRFLDKLRSS AEQLEEKLLD F
