CBPA_ECOLI
ID CBPA_ECOLI Reviewed; 306 AA.
AC P36659; P77250;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Curved DNA-binding protein;
GN Name=cbpA; OrderedLocusNames=b1000, JW0985;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=8302830; DOI=10.1073/pnas.91.3.1054;
RA Ueguchi C., Kakeda M., Yamada H., Mizuno T.;
RT "An analogue of the DnaJ molecular chaperone in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INDUCTION.
RX PubMed=7997164; DOI=10.1111/j.1365-2958.1994.tb00442.x;
RA Yamashino T., Kakeda M., Ueguchi C., Mizuno T.;
RT "An analogue of the DnaJ molecular chaperone whose expression is controlled
RT by sigma S during the stationary phase and phosphate starvation in
RT Escherichia coli.";
RL Mol. Microbiol. 13:475-483(1994).
RN [6]
RP POSSIBLE FUNCTION.
RX PubMed=7601860; DOI=10.1128/jb.177.13.3894-3896.1995;
RA Ueguchi C., Shiozawa T., Kakeda M., Yamada H., Mizuno T.;
RT "A study of the double mutation of dnaJ and cbpA, whose gene products
RT function as molecular chaperones in Escherichia coli.";
RL J. Bacteriol. 177:3894-3896(1995).
RN [7]
RP POSSIBLE FUNCTION.
RX PubMed=8824642; DOI=10.1128/jb.178.19.5847-5849.1996;
RA Wegrzyn A., Taylor K., Wegrzyn G.;
RT "The cbpA chaperone gene function compensates for dnaJ in lambda plasmid
RT replication during amino acid starvation of Escherichia coli.";
RL J. Bacteriol. 178:5847-5849(1996).
RN [8]
RP BINDING AFFINITY FOR DNA.
RX PubMed=10551881; DOI=10.1074/jbc.274.46.33105;
RA Azam T.A., Ishihama A.;
RT "Twelve species of the nucleoid-associated protein from Escherichia coli.
RT Sequence recognition specificity and DNA binding affinity.";
RL J. Biol. Chem. 274:33105-33113(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10947847; DOI=10.1046/j.1365-2443.2000.00350.x;
RA Azam T.A., Hiraga S., Ishihama A.;
RT "Two types of localization of the DNA-binding proteins within the
RT Escherichia coli nucleoid.";
RL Genes Cells 5:613-626(2000).
RN [10]
RP CHARACTERIZATION.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=15184371; DOI=10.1074/jbc.m404862200;
RA Chae C., Sharma S., Hoskins J.R., Wickner S.;
RT "CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is
RT modulated by CbpM.";
RL J. Biol. Chem. 279:33147-33153(2004).
RN [11]
RP REGULATION BY CBPM.
RX PubMed=17337578; DOI=10.1128/jb.01757-06;
RA Chenoweth M.R., Trun N., Wickner S.;
RT "In vivo modulation of a DnaJ homolog, CbpA, by CbpM.";
RL J. Bacteriol. 189:3635-3638(2007).
CC -!- FUNCTION: DNA-binding protein that preferentially recognizes a curved
CC DNA sequence. It is probably a functional analog of DnaJ; displays
CC overlapping activities with DnaJ, but functions under different
CC conditions, probably acting as a molecular chaperone in an adaptive
CC response to environmental stresses other than heat shock. Lacks
CC autonomous chaperone activity; binds native substrates and targets them
CC for recognition by DnaK. Its activity is inhibited by the binding of
CC CbpM.
CC -!- INTERACTION:
CC P36659; P0A6Y8: dnaK; NbExp=5; IntAct=EBI-546131, EBI-542092;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:10947847,
CC ECO:0000269|PubMed:8302830}.
CC -!- INDUCTION: In late stationary phase, by phosphate-starvation
CC conditions. {ECO:0000269|PubMed:7997164}.
CC -!- MISCELLANEOUS: It binds to curved DNA in a sequence-nonspecific
CC fashion.
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DR EMBL; D16500; BAA03950.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74085.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36142.1; -; Genomic_DNA.
DR PIR; F64841; F64841.
DR RefSeq; NP_415520.1; NC_000913.3.
DR RefSeq; WP_000420621.1; NZ_SSZK01000002.1.
DR PDB; 2KQX; NMR; -; A=2-72.
DR PDB; 3UCS; X-ray; 1.87 A; C/D=2-73.
DR PDBsum; 2KQX; -.
DR PDBsum; 3UCS; -.
DR AlphaFoldDB; P36659; -.
DR SMR; P36659; -.
DR BioGRID; 4261259; 672.
DR BioGRID; 851888; 1.
DR DIP; DIP-9249N; -.
DR IntAct; P36659; 50.
DR STRING; 511145.b1000; -.
DR jPOST; P36659; -.
DR PaxDb; P36659; -.
DR PRIDE; P36659; -.
DR EnsemblBacteria; AAC74085; AAC74085; b1000.
DR EnsemblBacteria; BAA36142; BAA36142; BAA36142.
DR GeneID; 947572; -.
DR KEGG; ecj:JW0985; -.
DR KEGG; eco:b1000; -.
DR PATRIC; fig|1411691.4.peg.1271; -.
DR EchoBASE; EB2110; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_0_6; -.
DR InParanoid; P36659; -.
DR OMA; WDAGFEF; -.
DR PhylomeDB; P36659; -.
DR BioCyc; EcoCyc:EG12193-MON; -.
DR EvolutionaryTrace; P36659; -.
DR PRO; PR:P36659; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003681; F:bent DNA binding; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01154; CbpA; 1.
DR InterPro; IPR023859; DNA-bd_curved-DNA.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome.
FT CHAIN 1..306
FT /note="Curved DNA-binding protein"
FT /id="PRO_0000169988"
FT DOMAIN 5..69
FT /note="J"
FT CONFLICT 294..306
FT /note="QSSFDPRKDWGKA -> PVVF (in Ref. 1; BAA03950)"
FT /evidence="ECO:0000305"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:3UCS"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:3UCS"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3UCS"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2KQX"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:3UCS"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:3UCS"
SQ SEQUENCE 306 AA; 34455 MW; A3893D2BFDE75803 CRC64;
MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA EAWEVLSDEQ
RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS IFGQHARQSR QRPATRGHDI
EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG
TPGENGGPNG DLWLVIHIAP HPLFDIVGQD LEIVVPVSPW EAALGAKVTV PTLKESILLT
IPPGSQAGQR LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR
KDWGKA
