ID   HSCB_AROAE              Reviewed;         177 AA.
AC   Q5NYT0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=AZOSEA36590;
GN   ORFNames=ebA6397;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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   ---------------------------------------------------------------------------
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; CR555306; CAI09784.1; -; Genomic_DNA.
DR   RefSeq; WP_011239437.1; NC_006513.1.
DR   AlphaFoldDB; Q5NYT0; -.
DR   SMR; Q5NYT0; -.
DR   STRING; 76114.ebA6397; -.
DR   EnsemblBacteria; CAI09784; CAI09784; ebA6397.
DR   KEGG; eba:ebA6397; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_068529_2_1_4; -.
DR   OMA; KFMAKLQ; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000006552; 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   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..177
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_0000070955"
FT   DOMAIN          8..80
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ   SEQUENCE   177 AA;  20674 MW;  A7810CCF2D2E24E3 CRC64;
     MSIDLQQDFF ALFGLPRRFR VDEAALEMAY HDLQGQVHPD RFAHLPDVEK RLSMQWATRV
     NEGFRTLRKP LPRAQYMLEL AGVDAGLHTN TAMSSAFLME QMEWREAVEE ARAAGEGHEL
     TQLHHRLRHH AREVFDELER TIDERHDFAA AAEIVRRLMF MEKIQHEIDD ALEALET