CBPM_SALSV
ID CBPM_SALSV Reviewed; 101 AA.
AC B4TSM2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=SeSA_A1175;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF91973.1; -; Genomic_DNA.
DR RefSeq; WP_001284251.1; NC_011094.1.
DR AlphaFoldDB; B4TSM2; -.
DR SMR; B4TSM2; -.
DR EnsemblBacteria; ACF91973; ACF91973; SeSA_A1175.
DR KEGG; sew:SeSA_A1175; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR OMA; YVIEIVE; -.
DR Proteomes; UP000001865; 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_1000137782"
SQ SEQUENCE 101 AA; 11595 MW; 284862957B761E7C CRC64;
MANITVTFTI TEFCLHTGVT EEELNEIVGL GVIEPYEDDN ADWQFDDRAA SVVQRALRLR
EELALDWPGI AVALTLLEEN SRLREENRLL LQRLSRFISH P