ID   CBPM_SHISS              Reviewed;         101 AA.
AC   Q3Z3C4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN   Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=SSON_1007;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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; CP000038; AAZ87738.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z3C4; -.
DR   SMR; Q3Z3C4; -.
DR   EnsemblBacteria; AAZ87738; AAZ87738; SSON_1007.
DR   KEGG; ssn:SSON_1007; -.
DR   HOGENOM; CLU_144710_3_1_6; -.
DR   OMA; YVIEIVE; -.
DR   Proteomes; UP000002529; 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_0000286896"
SQ   SEQUENCE   101 AA;  11512 MW;  387BBBBD577FDDB7 CRC64;
     MANVTVTFTI TEFCLHTGIS EEELNEIVGL GVVEPREIQE TTWVFDDHAA IVVQRAVRLR
     HELALDWPGI AVALTLMDDI AHLKQENRLL RQRLSRFVAH P