ID   HSCB_RICBR              Reviewed;         166 AA.
AC   Q1RJ71;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Co-chaperone protein HscB homolog;
GN   Name=hscB; OrderedLocusNames=RBE_0512;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE04593.1; -; Genomic_DNA.
DR   RefSeq; WP_011477184.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ71; -.
DR   SMR; Q1RJ71; -.
DR   STRING; 336407.RBE_0512; -.
DR   EnsemblBacteria; ABE04593; ABE04593; RBE_0512.
DR   KEGG; rbe:RBE_0512; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_068529_2_0_5; -.
DR   OMA; SMEIREY; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000001951; 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; PF00226; DnaJ; 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..166
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_0000286448"
FT   DOMAIN          3..73
FT                   /note="J"
SQ   SEQUENCE   166 AA;  19670 MW;  A1AA7054AF3E7D5F CRC64;
     MQNYFELLGL EQIYNIDLKI LEKQYFAMQI KYHPDKAKNL QEKEQNLIIA SNLNKAYYTL
     KDSLKRAEYM LLLYGVNLND EKVRSKLSAL ELSIFWDEME LIENTSSYKS LEEIKSKYEL
     MEKAEVNFLA ESFKKQDLSD ATIKTSKLKY IHTLLSKLQE KMKLCK