(data stored in SCRATCH9089 zone)

SWISSPROT: HSCB_PASMU

ID   HSCB_PASMU              Reviewed;         172 AA.
AC   Q9CNV3;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Co-chaperone protein HscB homolog;
GN   Name=hscB; OrderedLocusNames=PM0321;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; AE004439; AAK02405.1; -; Genomic_DNA.
DR   RefSeq; WP_005725914.1; NC_002663.1.
DR   SMR; Q9CNV3; -.
DR   EnsemblBacteria; AAK02405; AAK02405; PM0321.
DR   GeneID; 29388475; -.
DR   KEGG; pmu:PM0321; -.
DR   eggNOG; ENOG4108SWN; Bacteria.
DR   eggNOG; COG1076; LUCA.
DR   HOGENOM; HOG000262077; -.
DR   KO; K04082; -.
DR   OMA; KFMAKLQ; -.
DR   BioCyc; PMUL272843:G1FZ8-339-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
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; IEA:InterPro.
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;
DR   PRODOM; Q9CNV3.
DR   SWISS-2DPAGE; Q9CNV3.
KW   Chaperone; Reference proteome.
FT   CHAIN           1..172
FT                   /note="Co-chaperone protein HscB homolog"
FT                   /id="PRO_0000070976"
FT   DOMAIN          2..74
FT                   /note="J"
SQ   SEQUENCE   172 AA;  19933 MW;  946C48C34B4C4F70 CRC64;
     MNPFNIFDLP VDFHVDQATL SARYLALQKS LHPDNFTTHS AQEQRLAMQR SAEVNDALQI
     LKDPILRAET IIAIYTGEQQ NIEENSTRDM AFLMQQMQWR EQLENIEAQQ DSDQLVAFSA
     DIEQTQQALL SELADALSSQ QWQQAKVIND KLRFIKKLLL EVERVEEKLL DF
//

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