ID CBPM_ECOL5 Reviewed; 101 AA.
AC Q0TJ67;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=ECP_0999;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG69012.1; -; Genomic_DNA.
DR RefSeq; WP_000024569.1; NC_008253.1.
DR AlphaFoldDB; Q0TJ67; -.
DR SMR; Q0TJ67; -.
DR KEGG; ecp:ECP_0999; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR Proteomes; UP000009182; Chromosome.
DR Gene3D; 1.10.1660.10; -; 1.
DR HAMAP; MF_01155; CbpM; 1.
DR InterPro; IPR022835; CbpM.
DR Pfam; PF13591; MerR_2; 1.
PE 3: Inferred from homology;
FT CHAIN 1..101
FT /note="Chaperone modulatory protein CbpM"
FT /id="PRO_0000286890"
SQ SEQUENCE 101 AA; 11443 MW; 387A0A0D56CE6DB7 CRC64;
MANVTVTFTI TEFCLHTGIS EEELNEIVGL GVVEPSEIQE TTWVFDDHAA IVVQRAVRLR
HELALDWPGI AVALTLMDDI AHLKQENRLL RQRLSRFVAH P
//
