ID   HSCB_RICTY              Reviewed;         166 AA.
AC   Q68XG7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Co-chaperone protein HscB homolog;
GN   Name=hscB; OrderedLocusNames=RT0191;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03675.1; -; Genomic_DNA.
DR   RefSeq; WP_011190662.1; NC_006142.1.
DR   AlphaFoldDB; Q68XG7; -.
DR   SMR; Q68XG7; -.
DR   STRING; 257363.RT0191; -.
DR   PRIDE; Q68XG7; -.
DR   EnsemblBacteria; AAU03675; AAU03675; RT0191.
DR   KEGG; rty:RT0191; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_5; -.
DR   OMA; SMEIREY; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000000604; 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_0000286449"
FT   DOMAIN          3..73
FT                   /note="J"
SQ   SEQUENCE   166 AA;  19899 MW;  9C39292700E177C1 CRC64;
     MQNYFQLLEL PQEYNIDLKI LEKQYFAMQI KYHPDKAKTV QEKEQNLIIA TELNKAYSTL
     KDALKRAEYM LLLQNINLND EKIRSLLSPL ELSIFWNEME RIENTILFSD LEKIKHKYEL
     MQQQNINSLK QAFEKRNLSD ATIHTSKLKY IRTLQNKLQE KIKSCK