ID HSCB_VIBVY Reviewed; 171 AA.
AC Q7MNF9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=VV0758;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
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DR EMBL; BA000037; BAC93522.1; -; Genomic_DNA.
DR RefSeq; WP_011149602.1; NC_005139.1.
DR AlphaFoldDB; Q7MNF9; -.
DR SMR; Q7MNF9; -.
DR STRING; 672.VV93_v1c07040; -.
DR KEGG; vvy:VV0758; -.
DR PATRIC; fig|196600.6.peg.773; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR Proteomes; UP000002675; Chromosome I.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding 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; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 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 NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone.
FT CHAIN 1..171
FT /note="Co-chaperone protein HscB homolog"
FT /id="PRO_0000070996"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ SEQUENCE 171 AA; 19722 MW; 1C61BEE638064B75 CRC64;
MNHFELFGLP PQFSLDGSLL SSQFRELQKR FHPDNFATAS ERDRLLAVQK AAQINDAYQV
LKNPISRAEY LLSQNGLEIR GEQQTMQDPM FLMEQMELRE ELEEIPHGSD AESALAAFDA
RVSKMYKQHL ASIEQELNDA QWPQAADRVR KLKFIAKLKN EIELVEEKLF G
//
