ID A0A0K1J7D3_9RHOO Unreviewed; 177 AA. AC A0A0K1J7D3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 12-AUG-2020, entry version 24. DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000256|HAMAP-Rule:MF_00682}; GN Name=hscB {ECO:0000256|HAMAP-Rule:MF_00682}; GN ORFNames=AzCIB_2768 {ECO:0000313|EMBL:AKU12661.1}; OS Azoarcus sp. CIB. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae; OC Azoarcus; unclassified Azoarcus. OX NCBI_TaxID=198107 {ECO:0000313|EMBL:AKU12661.1, ECO:0000313|Proteomes:UP000066621}; RN [1] {ECO:0000313|EMBL:AKU12661.1, ECO:0000313|Proteomes:UP000066621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIB {ECO:0000313|EMBL:AKU12661.1, RC ECO:0000313|Proteomes:UP000066621}; RA Martin-Moldes Z., Zamarro M.T., del Cerro C., Valencia A., Gomez M.J., RA Udaondo Z., Garcia J.L., Nogales J., Carmona M., Diaz E.; RT "Whole-genome analysis of Azoarcus sp. strain CIB provides genetic insights RT to its different lifestyles and predicts novel metabolic features."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00682}. CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity. CC {ECO:0000256|HAMAP-Rule:MF_00682}. CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000256|ARBA:ARBA00010476, CC ECO:0000256|HAMAP-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; CP011072; AKU12661.1; -; Genomic_DNA. DR RefSeq; WP_050416408.1; NZ_CP011072.1. DR EnsemblBacteria; AKU12661; AKU12661; AzCIB_2768. DR KEGG; azi:AzCIB_2768; -. DR PATRIC; fig|198107.6.peg.2876; -. DR KO; K04082; -. DR OrthoDB; 1520143at2; -. DR Proteomes; UP000066621; Chromosome. DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro. DR GO; GO:0051087; F:chaperone binding; IEA:InterPro. DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:InterPro. 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. PE 3: Inferred from homology; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00682}; KW Reference proteome {ECO:0000313|Proteomes:UP000066621}. FT DOMAIN 93..169 FT /note="HSCB_C" FT /evidence="ECO:0000259|Pfam:PF07743" SQ SEQUENCE 177 AA; 20536 MW; 5D51E41AFFF36FDE CRC64; MSIDLQQDFF GLFGLHRRFR IDEAALELAY HDLQGRVHPD RFAHLPDSEK RLSMQWATQV NEGFRTLRKP LPRATYLLEL MGVDAGLHTN TAMAPAFLME QMEWREAVEE ARAAGDSEEL AQLHTRLRQH SREVFDELAR QCDDEHDYAG AAETVRRLMF MEKLQHEIDD ALEALES //