CBPM_SALPK
ID CBPM_SALPK Reviewed; 101 AA.
AC B5BBH3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Chaperone modulatory protein CbpM {ECO:0000255|HAMAP-Rule:MF_01155};
GN Name=cbpM {ECO:0000255|HAMAP-Rule:MF_01155}; OrderedLocusNames=SSPA1616;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(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; FM200053; CAR59805.1; -; Genomic_DNA.
DR RefSeq; WP_001284253.1; NC_011147.1.
DR AlphaFoldDB; B5BBH3; -.
DR SMR; B5BBH3; -.
DR KEGG; sek:SSPA1616; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR OMA; YVIEIVE; -.
DR Proteomes; UP000001869; 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_1000137781"
SQ SEQUENCE 101 AA; 11625 MW; 343862956E631E69 CRC64;
MANITVTFTI TEFCLHTGVT EEELNEIVGL GVIEPYEDDN TDWQFDDRAA SVVQRALRLR
EELALDWPGI AVALTLLEEN SRLREENRLL LQRLSRFISH P