HSCB_AERHH
ID HSCB_AERHH Reviewed; 172 AA.
AC A0KJ35;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=AHA_1750;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37912.1; -; Genomic_DNA.
DR RefSeq; WP_011705637.1; NC_008570.1.
DR RefSeq; YP_856286.1; NC_008570.1.
DR AlphaFoldDB; A0KJ35; -.
DR SMR; A0KJ35; -.
DR STRING; 380703.AHA_1750; -.
DR EnsemblBacteria; ABK37912; ABK37912; AHA_1750.
DR KEGG; aha:AHA_1750; -.
DR PATRIC; fig|380703.7.peg.1764; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OMA; KFMAKLQ; -.
DR Proteomes; UP000000756; 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..172
FT /note="Co-chaperone protein HscB homolog"
FT /id="PRO_1000082994"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ SEQUENCE 172 AA; 20234 MW; A9E46609C803E2B0 CRC64;
MNYFELFGLV EGFELDTRQL AETYRQLQTQ FHPDRFATAP EWEQLAAVQR AAQINDAFTT
LKAPLRRAEY LLSLRGTELR GEQQTLQDTA FLMQQLEWRE RLADLKGETD PERAIKDFRQ
EIRHDHQLLM QQLTQALATG EDPRAADCVR KLKFVDKLLE ELERFEDSLF ES