ID   CBPM_ECO5E              Reviewed;         101 AA.
AC   B5YU42;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN   Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN   OrderedLocusNames=ECH74115_1235;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(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; CP001164; ACI37630.1; -; Genomic_DNA.
DR   RefSeq; WP_000024560.1; NC_011353.1.
DR   AlphaFoldDB; B5YU42; -.
DR   SMR; B5YU42; -.
DR   GeneID; 66670723; -.
DR   KEGG; ecf:ECH74115_1235; -.
DR   HOGENOM; CLU_144710_3_1_6; -.
DR   OMA; YVIEIVE; -.
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_1000137767"
SQ   SEQUENCE   101 AA;  11512 MW;  387BBBBD577FDDB7 CRC64;
     MANVTVTFTI TEFCLHTGIS EEELNEIVGL GVVEPREIQE TTWVFDDHAA IVVQRAVRLR
     HELALDWPGI AVALTLMDDI AHLKQENRLL RQRLSRFVAH P