ID HSCB_YERP3 Reviewed; 174 AA.
AC A7FFX4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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};
GN OrderedLocusNames=YpsIP31758_1171;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS47238.1; -; Genomic_DNA.
DR RefSeq; WP_011192812.1; NC_009708.1.
DR AlphaFoldDB; A7FFX4; -.
DR SMR; A7FFX4; -.
DR GeneID; 66844722; -.
DR KEGG; ypi:YpsIP31758_1171; -.
DR HOGENOM; CLU_068529_2_0_6; -.
DR Proteomes; UP000002412; Chromosome.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding 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; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 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 NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone.
FT CHAIN 1..174
FT /note="Co-chaperone protein HscB"
FT /id="PRO_1000083054"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ SEQUENCE 174 AA; 20649 MW; 8CBA4A36FF03A45A CRC64;
MDYFTLFGLP ARYLIDGNQL TTRYQELQRQ FHPDRFATQP ERERLASMQQ AATINDAYQT
LKHPLKRAEY MLSLQGFDLG NEQHTMRDTA FLMEQLELRE ELDAIERKPD AETLLAEFSR
RLAQMTTTRT QQMVEQLDAQ LWVQAADTVR KLRFLDKLQQ QVEQLEERLF DDFA
//
