HSCB_HAEIN
ID HSCB_HAEIN Reviewed; 174 AA.
AC Q57006; P96333;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Co-chaperone protein HscB homolog;
GN Name=hscB; OrderedLocusNames=HI_0375;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR EMBL; L42023; AAC22032.1; -; Genomic_DNA.
DR PIR; D64150; D64150.
DR RefSeq; NP_438536.1; NC_000907.1.
DR RefSeq; WP_005693789.1; NC_000907.1.
DR AlphaFoldDB; Q57006; -.
DR SMR; Q57006; -.
DR STRING; 71421.HI_0375; -.
DR EnsemblBacteria; AAC22032; AAC22032; HI_0375.
DR KEGG; hin:HI_0375; -.
DR PATRIC; fig|71421.8.peg.393; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OMA; KFMAKLQ; -.
DR PhylomeDB; Q57006; -.
DR BioCyc; HINF71421:G1GJ1-388-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:1990230; C:iron-sulfur cluster transfer complex; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Chaperone; Reference proteome.
FT CHAIN 1..174
FT /note="Co-chaperone protein HscB homolog"
FT /id="PRO_0000070971"
FT DOMAIN 3..75
FT /note="J"
SQ SEQUENCE 174 AA; 20431 MW; 13BB2F423408EDD4 CRC64;
MFNPFQIFDL PVDFQLDEKV LNARYLKLQK ALHPDNFVSS NALDQRVAMQ KSTEVNDALK
TLKDPILRAE AIIALNTGEQ LDLEQKSTQD VAFLMQQLQW REQLEEVERQ QDERALNAFA
KEIKQETQSL LTALFESLKS QQWARASQYC DKLRFTHKLS EEIERVEERI FELD
