HSCB_SHEON
ID HSCB_SHEON Reviewed; 174 AA.
AC Q8EEU6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=SO_2267;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55307.1; -; Genomic_DNA.
DR RefSeq; NP_717863.1; NC_004347.2.
DR RefSeq; WP_011072279.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EEU6; -.
DR SMR; Q8EEU6; -.
DR STRING; 211586.SO_2267; -.
DR PaxDb; Q8EEU6; -.
DR KEGG; son:SO_2267; -.
DR PATRIC; fig|211586.12.peg.2183; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OMA; KFMAKLQ; -.
DR OrthoDB; 1520143at2; -.
DR PhylomeDB; Q8EEU6; -.
DR BioCyc; SONE211586:G1GMP-2071-MON; -.
DR Proteomes; UP000008186; 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.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Reference proteome.
FT CHAIN 1..174
FT /note="Co-chaperone protein HscB homolog"
FT /id="PRO_0000070990"
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ SEQUENCE 174 AA; 20194 MW; D7664AB6CF797641 CRC64;
MNYFELFKFP PTFDIDTAVL ADRYRELQRA VHPDKFANDT EQQRLLSVQR TAQVNDGYQT
LKDPIRRAEH MLSLRGIDLS HETTTVKDTA FLMQQMEWRE ALEDIRESID HQAIINELYD
SFAAYRLKLT KLLAAQLSSG SDEDALLAAD QVRKLKFMAK LQDELTRIED ALLD
