ID   HSCB_BUCAP              Reviewed;         165 AA.
AC   O51884;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Co-chaperone protein HscB;
DE   AltName: Full=Hsc20;
GN   Name=hscB; OrderedLocusNames=BUsg_579;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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       Interacts with IscU (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF008210; AAC38122.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM68113.1; -; Genomic_DNA.
DR   RefSeq; WP_011054079.1; NC_004061.1.
DR   AlphaFoldDB; O51884; -.
DR   SMR; O51884; -.
DR   STRING; 198804.BUsg_579; -.
DR   EnsemblBacteria; AAM68113; AAM68113; BUsg_579.
DR   KEGG; bas:BUsg_579; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OMA; KFMAKLQ; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000000416; 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..165
FT                   /note="Co-chaperone protein HscB"
FT                   /id="PRO_0000070961"
FT   DOMAIN          2..74
FT                   /note="J"
SQ   SEQUENCE   165 AA;  20154 MW;  00349D8C3A662B4B CRC64;
     MDYFALFNLP KKYIIDKFLL SKNFYKLQLK FHPDLFIHHS ESKKRIVLQK SIEINKGYKI
     LQDSLNRAIH LLFLNGFKIS KEKVLSEDNS FLKKYFFLYE ELDFLLKNNC DEVQIDIFFK
     KIRNKIDNYE KIIEIKFNEK KWDDIIKLIT KLLFFKKIQT RLKQS