ID   HSCB_RICPR              Reviewed;         166 AA.
AC   Q9ZDW4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=RP201;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA14666.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ235270; CAA14666.1; ALT_INIT; Genomic_DNA.
DR   PIR; C71731; C71731.
DR   RefSeq; NP_220589.2; NC_000963.1.
DR   RefSeq; WP_004595975.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDW4; -.
DR   SMR; Q9ZDW4; -.
DR   STRING; 272947.RP201; -.
DR   EnsemblBacteria; CAA14666; CAA14666; CAA14666.
DR   GeneID; 57569329; -.
DR   KEGG; rpr:RP201; -.
DR   PATRIC; fig|272947.5.peg.210; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_5; -.
DR   Proteomes; UP000002480; 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; Reference proteome.
FT   CHAIN           1..166
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_0000070985"
FT   DOMAIN          3..73
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ   SEQUENCE   166 AA;  19684 MW;  7BC9E305C430725D CRC64;
     MQNYFQLLEL PQEYNIDLKI LEKQYFAMQV KYHPDTAKTA QEKAQNLITS TELNKAYSTL
     KDALKRAEYM LLLQNINLND EKIRSLLSPL ELSIFWDEME RIENTTLFSD LEKLKNKYEL
     MQQQNINSLK QAFVEQNLSD ATIYTSKLKY IRTLQSKLQE KIKSCK