HSCB_VIBCH
ID HSCB_VIBCH Reviewed; 171 AA.
AC Q9KTX9;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=VC_0751;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93916.1; -; Genomic_DNA.
DR PIR; B82286; B82286.
DR RefSeq; NP_230400.1; NC_002505.1.
DR RefSeq; WP_001105747.1; NZ_LT906614.1.
DR PDB; 4IT5; X-ray; 2.15 A; A/B/C/D=1-171.
DR PDBsum; 4IT5; -.
DR AlphaFoldDB; Q9KTX9; -.
DR SMR; Q9KTX9; -.
DR STRING; 243277.VC_0751; -.
DR DNASU; 2615760; -.
DR EnsemblBacteria; AAF93916; AAF93916; VC_0751.
DR GeneID; 57739461; -.
DR KEGG; vch:VC_0751; -.
DR PATRIC; fig|243277.26.peg.715; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OMA; KFMAKLQ; -.
DR BioCyc; VCHO:VC0751-MON; -.
DR EvolutionaryTrace; Q9KTX9; -.
DR Proteomes; UP000000584; Chromosome 1.
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; PF00226; DnaJ; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..171
FT /note="Co-chaperone protein HscB homolog"
FT /id="PRO_0000070992"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4IT5"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 41..62
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:4IT5"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4IT5"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4IT5"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 111..138
FT /evidence="ECO:0007829|PDB:4IT5"
FT HELIX 142..169
FT /evidence="ECO:0007829|PDB:4IT5"
SQ SEQUENCE 171 AA; 19627 MW; 4516C70B3B51AF29 CRC64;
MNYFELFGLP IQFELDGSLL SSQFRALQKR FHPDNFATAS ERDRLMAVQQ AAQINDAYQT
LKDPLRRAEY LLSLQGIEMN AEQQTLQDPM FLMEQMELRE ELESVTACAD PEAALVAFDT
KVTAMQRHYL AQLQGQLAQS EWLAAADQIR KLKFIAKLKN EVERVEDQLL G
