ID   HSCB_PARXL              Reviewed;         175 AA.
AC   Q13WZ0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; OrderedLocusNames=Bxeno_A2861;
GN   ORFNames=Bxe_A1556;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE31399.1; -; Genomic_DNA.
DR   RefSeq; WP_011488977.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13WZ0; -.
DR   SMR; Q13WZ0; -.
DR   STRING; 266265.Bxe_A1556; -.
DR   EnsemblBacteria; ABE31399; ABE31399; Bxe_A1556.
DR   KEGG; bxb:DR64_3717; -.
DR   KEGG; bxe:Bxe_A1556; -.
DR   PATRIC; fig|266265.5.peg.3003; -.
DR   eggNOG; COG1076; Bacteria.
DR   OMA; KFMAKLQ; -.
DR   OrthoDB; 1520143at2; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..175
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_1000083003"
FT   DOMAIN          7..79
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00682"
SQ   SEQUENCE   175 AA;  19607 MW;  B74EAF4F8F9770DA CRC64;
     MASLNDSHFD LFDLPAQFAL DASALDHAYR TVQAQVHPDR FAAAGDAQKR IAMQWATRTN
     EAYQTLRDPL KRATYLLHLR GIDVGAENNT AMEPAFLMQQ MEWRESIEDA AAAKNVDALD
     ALLTELRDEE RMRFDKLGAL LDSGANQAAG EAVRQLMFIE RVASEIGTQI ERLEN