CBPM_SALPB
ID CBPM_SALPB Reviewed; 101 AA.
AC A9N6S3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-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}; OrderedLocusNames=SPAB_02439;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX67820.1; -; Genomic_DNA.
DR RefSeq; WP_001284251.1; NC_010102.1.
DR AlphaFoldDB; A9N6S3; -.
DR SMR; A9N6S3; -.
DR KEGG; spq:SPAB_02439; -.
DR PATRIC; fig|1016998.12.peg.2307; -.
DR HOGENOM; CLU_144710_3_1_6; -.
DR OMA; YVIEIVE; -.
DR BioCyc; SENT1016998:SPAB_RS09905-MON; -.
DR Proteomes; UP000008556; 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_1000085348"
SQ SEQUENCE 101 AA; 11595 MW; 284862957B761E7C CRC64;
MANITVTFTI TEFCLHTGVT EEELNEIVGL GVIEPYEDDN ADWQFDDRAA SVVQRALRLR
EELALDWPGI AVALTLLEEN SRLREENRLL LQRLSRFISH P