ID Q4QNG7_HAEI8 Unreviewed; 174 AA.
AC Q4QNG7;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, 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:AAX87430.1};
GN OrderedLocusNames=NTHI0495 {ECO:0000313|EMBL:AAX87430.1};
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX87430.1, ECO:0000313|Proteomes:UP000002525};
RN [1] {ECO:0000313|EMBL:AAX87430.1, ECO:0000313|Proteomes:UP000002525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP {ECO:0000313|EMBL:AAX87430.1,
RC ECO:0000313|Proteomes:UP000002525};
RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S.Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(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: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; CP000057; AAX87430.1; -; Genomic_DNA.
DR RefSeq; WP_011272012.1; NC_007146.2.
DR AlphaFoldDB; Q4QNG7; -.
DR GeneID; 72526430; -.
DR KEGG; hit:NTHI0495; -.
DR HOGENOM; CLU_068529_2_0_6; -.
DR Proteomes; UP000002525; Chromosome.
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 174 AA; 20363 MW; 68AD9E0A0BB334C4 CRC64;
MFNPFQIFDL PVDFQLDEKV LNARYLKLQK ALHPDNFVSS SALEQRVAMQ KSTEVNDALK
TLKDPILRAE AIIALNTGEQ LDLEQKSTQD VAFLMQQLQW REQLEDVESQ QDERALNVFA
KEIKQETQSL LTALFESLKS QQWARASQYC DKLRFTHKLS EEIERVEERI FELD
//
