ID Q0I1K9_HISS1 Unreviewed; 172 AA.
AC Q0I1K9;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000256|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000256|HAMAP-Rule:MF_00682,
GN ECO:0000313|EMBL:ABI24562.1};
GN OrderedLocusNames=HS_0284 {ECO:0000313|EMBL:ABI24562.1};
OS Histophilus somni (strain 129Pt) (Haemophilus somnus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914 {ECO:0000313|EMBL:ABI24562.1};
RN [1] {ECO:0000313|EMBL:ABI24562.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129PT {ECO:0000313|EMBL:ABI24562.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Dalin E., Tice H., Pitluck S., Brettin T.S., Bruce D., Challacombe J.F.,
RA Chertkov O., Detter J.C., Gilna P., Han S., Misra M., Tapia R.,
RA Thayer N.N., Xie G., Inzana T.J., Duncan A.J., Siddaramppa S.,
RA Richardson P.;
RT "Complete genome sequence of Haemophilus somnus 129PT.";
RL Submitted (AUG-2006) 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|ARBA:ARBA00025596, ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; CP000436; ABI24562.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0I1K9; -.
DR KEGG; hso:HS_0284; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
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; 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.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00682}.
FT DOMAIN 2..67
FT /note="J"
FT /evidence="ECO:0000259|SMART:SM00271"
SQ SEQUENCE 172 AA; 20538 MW; F2720BB5071A60A0 CRC64;
MINPFALFDL EIDFNLDQQI LSQRYLTLQK SLHPDNFAHR SAQEQRLALQ KSAEINDALQ
ILKDPISRAD SIINLHLGEQ NIEQKTNQDM MFLMQQMEWR ERLEQVEQQQ NMDKLLHFSQ
EVECVQRDIL AELQEFLAQQ NWQQAQLLND RLRFIKKLFV EIERVEEQLA GF
//
