CBPM_SALPC
ID CBPM_SALPC Reviewed; 101 AA.
AC C0Q894;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=SPC_2638;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN46739.1; -; Genomic_DNA.
DR RefSeq; WP_001284251.1; NC_012125.1.
DR AlphaFoldDB; C0Q894; -.
DR SMR; C0Q894; -.
DR EnsemblBacteria; ACN46739; ACN46739; SPC_2638.
DR KEGG; sei:SPC_2638; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR OMA; YVIEIVE; -.
DR Proteomes; UP000001599; 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_1000164292"
SQ SEQUENCE 101 AA; 11595 MW; 284862957B761E7C CRC64;
MANITVTFTI TEFCLHTGVT EEELNEIVGL GVIEPYEDDN ADWQFDDRAA SVVQRALRLR
EELALDWPGI AVALTLLEEN SRLREENRLL LQRLSRFISH P