ID   HSCB_BORBR              Reviewed;         170 AA.
AC   Q7WK60;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=BB2279;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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       {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; BX640443; CAE32775.1; -; Genomic_DNA.
DR   RefSeq; WP_003812456.1; NC_002927.3.
DR   AlphaFoldDB; Q7WK60; -.
DR   SMR; Q7WK60; -.
DR   STRING; 257310.BB2279; -.
DR   EnsemblBacteria; CAE32775; CAE32775; BB2279.
DR   GeneID; 56478394; -.
DR   GeneID; 66438531; -.
DR   KEGG; bbr:BB2279; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_1_4; -.
DR   OMA; KFMAKLQ; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000001027; 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..170
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_0000070957"
FT   DOMAIN          5..79
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ   SEQUENCE   170 AA;  19563 MW;  C9A954261D59395C CRC64;
     MAADDHFSLF GLPTRFALDP VQLEQAWRAV AARVHPDRYA TASAAERRVA MQWAARANEA
     YRQLRDPMLR ARYLCEQAGV DLQTESNTAM DPAFLMQQME WREMLDDARR DPAAFAALRA
     ELEQARLRMQ QTLSELIDER GDYQQAGTKV REWMFVEKLA QELSAAQPMQ