ID   HSCB_BUCAI              Reviewed;         174 AA.
AC   P57659;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Co-chaperone protein HscB;
DE   AltName: Full=Hsc20;
GN   Name=hscB; OrderedLocusNames=BU604;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
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DR   EMBL; BA000003; BAB13288.1; -; Genomic_DNA.
DR   RefSeq; NP_240402.1; NC_002528.1.
DR   RefSeq; WP_010896182.1; NC_002528.1.
DR   AlphaFoldDB; P57659; -.
DR   SMR; P57659; -.
DR   STRING; 107806.10039254; -.
DR   EnsemblBacteria; BAB13288; BAB13288; BAB13288.
DR   KEGG; buc:BU604; -.
DR   PATRIC; fig|107806.10.peg.606; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OMA; KFMAKLQ; -.
DR   Proteomes; UP000001806; 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; Reference proteome.
FT   CHAIN           1..174
FT                   /note="Co-chaperone protein HscB"
FT                   /id="PRO_0000070960"
FT   DOMAIN          2..74
FT                   /note="J"
SQ   SEQUENCE   174 AA;  21293 MW;  00844A684D551F2C CRC64;
     MNYFTLFDLP RKFNIDKKLL SQNFYKLQLK FHPDLFINDS ESKKKIILEK SIQINKGYKT
     LKNFLNRAIY FLCLNGYEVK KETLLLKNND FLIRYFSLYE QLDNLKENNF NKKELNNLEQ
     IIQKKIIYCK KKIELEFEKT RYKKVIKIIS ELLFFEKIKD VLKKEYNIYL SQIN