ID   HSCB_ECO81              Reviewed;         171 AA.
AC   B7MYG1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Co-chaperone protein HscB {ECO:0000255|HAMAP-Rule:MF_00682};
DE   AltName: Full=Hsc20 {ECO:0000255|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=ECED1_2958;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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       Interacts with IscU. {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; CU928162; CAR09127.2; -; Genomic_DNA.
DR   RefSeq; WP_000384413.1; NC_011745.1.
DR   AlphaFoldDB; B7MYG1; -.
DR   SMR; B7MYG1; -.
DR   EnsemblBacteria; CAR09127; CAR09127; ECED1_2958.
DR   GeneID; 60903814; -.
DR   KEGG; ecq:ECED1_2958; -.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OMA; KFMAKLQ; -.
DR   Proteomes; UP000000748; Chromosome.
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; 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; -; 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.
FT   CHAIN           1..171
FT                   /note="Co-chaperone protein HscB"
FT                   /id="PRO_1000189914"
FT   DOMAIN          2..74
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ   SEQUENCE   171 AA;  20138 MW;  095193EE98AA60C9 CRC64;
     MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT
     LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR
     VKKMFDTRHQ LMVEQLDNET WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F