CBPM_SALCH
ID CBPM_SALCH Reviewed; 101 AA.
AC Q57QP3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=SCH_1062;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- FUNCTION: Interacts with CbpA and inhibits both the DnaJ-like co-
CC chaperone activity and the DNA binding activity of CbpA. Together with
CC CbpA, modulates the activity of the DnaK chaperone system. Does not
CC inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-
CC Rule:MF_01155}.
CC -!- SIMILARITY: Belongs to the CbpM family. {ECO:0000255|HAMAP-
CC Rule:MF_01155}.
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DR EMBL; AE017220; AAX64968.1; -; Genomic_DNA.
DR RefSeq; WP_001284251.1; NC_006905.1.
DR AlphaFoldDB; Q57QP3; -.
DR SMR; Q57QP3; -.
DR EnsemblBacteria; AAX64968; AAX64968; SCH_1062.
DR KEGG; sec:SCH_1062; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR OMA; YVIEIVE; -.
DR Proteomes; UP000000538; Chromosome.
DR HAMAP; MF_01155; CbpM; 1.
DR InterPro; IPR022835; CbpM.
PE 3: Inferred from homology;
FT CHAIN 1..101
FT /note="Chaperone modulatory protein CbpM"
FT /id="PRO_0000286892"
SQ SEQUENCE 101 AA; 11595 MW; 284862957B761E7C CRC64;
MANITVTFTI TEFCLHTGVT EEELNEIVGL GVIEPYEDDN ADWQFDDRAA SVVQRALRLR
EELALDWPGI AVALTLLEEN SRLREENRLL LQRLSRFISH P