P36659 (CBPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Curved DNA-binding protein | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 306 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. Ref.6 Ref.7 |
| Subcellular location | |
| Induction | In late stationary phase, by phosphate-starvation conditions. Ref.5 Ref.11 |
| Miscellaneous | It binds to curved DNA in a sequence-nonspecific fashion. HAMAP-Rule MF_01154 |
| Sequence similarities | Contains 1 J domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | DNA-binding |
| Molecular function | Chaperone |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | protein folding Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: HAMAP nucleoidInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | bent DNA binding Inferred from direct assay Ref.8. Source: EcoliWiki |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||
Molecule processing | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 306 | 306 | Curved DNA-binding protein HAMAP-Rule MF_01154 | PRO_0000169988 | |||||||||||||||
Regions | |||||||||||||||||||
| Domain | 5 – 69 | 65 | J | ||||||||||||||||
Experimental info | |||||||||||||||||||
| Sequence conflict | 294 – 306 | 13 | QSSFD…DWGKA → PVVF in BAA03950. Ref.1 | ||||||||||||||||
Secondary structure | |||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||
| Helix | 6 – 9 | 4 | |||||||||||||||||
| Helix | 18 – 32 | 15 | |||||||||||||||||
| Beta strand | 39 – 41 | 3 | |||||||||||||||||
| Helix | 42 – 57 | 16 | |||||||||||||||||
| Helix | 59 – 68 | 10 | |||||||||||||||||
| Turn | 69 – 71 | 3 | |||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "An analogue of the DnaJ molecular chaperone in Escherichia coli." Ueguchi C., Kakeda M., Yamada H., Mizuno T. Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, SUBCELLULAR LOCATION. Strain: K12. |
| [2] | "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T.DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "An analogue of the DnaJ molecular chaperone whose expression is controlled by sigma S during the stationary phase and phosphate starvation in Escherichia coli." Yamashino T., Kakeda M., Ueguchi C., Mizuno T. Mol. Microbiol. 13:475-483(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [6] | "A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli." Ueguchi C., Shiozawa T., Kakeda M., Yamada H., Mizuno T. J. Bacteriol. 177:3894-3896(1995) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE FUNCTION. |
| [7] | "The cbpA chaperone gene function compensates for dnaJ in lambda plasmid replication during amino acid starvation of Escherichia coli." Wegrzyn A., Taylor K., Wegrzyn G. J. Bacteriol. 178:5847-5849(1996) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE FUNCTION. |
| [8] | "Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity." Azam T.A., Ishihama A. J. Biol. Chem. 274:33105-33113(1999) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING AFFINITY FOR DNA. |
| [9] | "Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid." Azam T.A., Hiraga S., Ishihama A. Genes Cells 5:613-626(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [10] | "CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM." Chae C., Sharma S., Hoskins J.R., Wickner S. J. Biol. Chem. 279:33147-33153(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / DH5-alpha. |
| [11] | "In vivo modulation of a DnaJ homolog, CbpA, by CbpM." Chenoweth M.R., Trun N., Wickner S. J. Bacteriol. 189:3635-3638(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION BY CBPM. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D16500 Genomic DNA. Translation: BAA03950.1. U00096 Genomic DNA. Translation: AAC74085.1. AP009048 Genomic DNA. Translation: BAA36142.1. | ||||||||||||
| PIR | F64841. | ||||||||||||
| RefSeq | NP_415520.1. NC_000913.2. YP_489273.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P36659. | ||||||||||||
| SMR | P36659. Positions 2-72, 114-303. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-9249N. | ||||||||||||
| IntAct | P36659. 49 interactions. | ||||||||||||
| MINT | MINT-1219908. | ||||||||||||
| STRING | 511145.b1000. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P36659. | ||||||||||||
| PRIDE | P36659. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC74085; AAC74085; b1000. BAA36142; BAA36142; BAA36142. | ||||||||||||
| GeneID | 12932265. 947572. | ||||||||||||
| KEGG | ecj:Y75_p0973. eco:b1000. | ||||||||||||
| PATRIC | 32117225. VBIEscCol129921_1036. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2110. | ||||||||||||
| EcoGene | EG12193. cbpA. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG2214. | ||||||||||||
| HOGENOM | HOG000226716. | ||||||||||||
| KO | K05516. | ||||||||||||
| OMA | KVANDST. | ||||||||||||
| ProtClustDB | PRK10266. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG12193-MONOMER. ECOL316407:JW0985-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P36659. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.287.110. 1 hit. | ||||||||||||
| HAMAP | MF_01154. CbpA. | ||||||||||||
| InterPro | IPR023859. DNA-bd_curved-DNA. IPR002939. DnaJ_C. IPR001623. DnaJ_domain. IPR018253. DnaJ_domain_CS. IPR008971. HSP40/DnaJ_pept-bd. [Graphical view] | ||||||||||||
| Pfam | PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00625. JDOMAIN. | ||||||||||||
| SMART | SM00271. DnaJ. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF46565. DnaJ_N. 1 hit. SSF49493. HSP40_DnaJ_pep. 2 hits. | ||||||||||||
| PROSITE | PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P36659. | ||||||||||||
Entry information
| Entry name | CBPA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P36659 Secondary accession number(s): P77250 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
