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P36659

- CBPA_ECOLI

UniProt

P36659 - CBPA_ECOLI

Protein

Curved DNA-binding protein

Gene

cbpA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. bent DNA binding Source: EcoliWiki
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12193-MONOMER.
    ECOL316407:JW0985-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Curved DNA-binding protein
    Gene namesi
    Name:cbpA
    Ordered Locus Names:b1000, JW0985
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12193. cbpA.

    Subcellular locationi

    Cytoplasmnucleoid 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-HAMAP
    2. nucleoid Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 306306Curved DNA-binding proteinPRO_0000169988Add
    BLAST

    Proteomic databases

    PaxDbiP36659.
    PRIDEiP36659.

    Expressioni

    Inductioni

    In late stationary phase, by phosphate-starvation conditions.1 Publication

    Gene expression databases

    GenevestigatoriP36659.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaKP0A6Y84EBI-546131,EBI-542092

    Protein-protein interaction databases

    DIPiDIP-9249N.
    IntActiP36659. 49 interactions.
    MINTiMINT-1219908.
    STRINGi511145.b1000.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 105
    Helixi18 – 3215
    Turni34 – 363
    Beta strandi39 – 413
    Helixi42 – 5615
    Helixi59 – 7012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KQXNMR-A2-72[»]
    3UCSX-ray1.87C/D2-73[»]
    ProteinModelPortaliP36659.
    SMRiP36659. Positions 2-73, 114-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36659.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 6965JAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.Curated

    Phylogenomic databases

    eggNOGiCOG2214.
    HOGENOMiHOG000226716.
    KOiK05516.
    OMAiTEQTRSI.
    OrthoDBiEOG6BPDKP.
    PhylomeDBiP36659.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    HAMAPiMF_01154. CbpA.
    InterProiIPR023859. DNA-bd_curved-DNA.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view]
    PfamiPF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P36659-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA    50
    EAWEVLSDEQ RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS 100
    IFGQHARQSR QRPATRGHDI EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG 150
    MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG TPGENGGPNG DLWLVIHIAP 200
    HPLFDIVGQD LEIVVPVSPW EAALGAKVTV PTLKESILLT IPPGSQAGQR 250
    LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR 300
    KDWGKA 306
    Length:306
    Mass (Da):34,455
    Last modified:November 1, 1997 - v2
    Checksum:iA3893D2BFDE75803
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 30613QSSFD…DWGKA → PVVF in BAA03950. (PubMed:8302830)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16500 Genomic DNA. Translation: BAA03950.1.
    U00096 Genomic DNA. Translation: AAC74085.1.
    AP009048 Genomic DNA. Translation: BAA36142.1.
    PIRiF64841.
    RefSeqiNP_415520.1. NC_000913.3.
    YP_489273.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74085; AAC74085; b1000.
    BAA36142; BAA36142; BAA36142.
    GeneIDi12932265.
    947572.
    KEGGiecj:Y75_p0973.
    eco:b1000.
    PATRICi32117225. VBIEscCol129921_1036.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16500 Genomic DNA. Translation: BAA03950.1 .
    U00096 Genomic DNA. Translation: AAC74085.1 .
    AP009048 Genomic DNA. Translation: BAA36142.1 .
    PIRi F64841.
    RefSeqi NP_415520.1. NC_000913.3.
    YP_489273.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KQX NMR - A 2-72 [» ]
    3UCS X-ray 1.87 C/D 2-73 [» ]
    ProteinModelPortali P36659.
    SMRi P36659. Positions 2-73, 114-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9249N.
    IntActi P36659. 49 interactions.
    MINTi MINT-1219908.
    STRINGi 511145.b1000.

    Proteomic databases

    PaxDbi P36659.
    PRIDEi P36659.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74085 ; AAC74085 ; b1000 .
    BAA36142 ; BAA36142 ; BAA36142 .
    GeneIDi 12932265.
    947572.
    KEGGi ecj:Y75_p0973.
    eco:b1000.
    PATRICi 32117225. VBIEscCol129921_1036.

    Organism-specific databases

    EchoBASEi EB2110.
    EcoGenei EG12193. cbpA.

    Phylogenomic databases

    eggNOGi COG2214.
    HOGENOMi HOG000226716.
    KOi K05516.
    OMAi TEQTRSI.
    OrthoDBi EOG6BPDKP.
    PhylomeDBi P36659.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12193-MONOMER.
    ECOL316407:JW0985-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P36659.
    PROi P36659.

    Gene expression databases

    Genevestigatori P36659.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    HAMAPi MF_01154. CbpA.
    InterProi IPR023859. DNA-bd_curved-DNA.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. 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.

    Entry informationi

    Entry nameiCBPA_ECOLI
    AccessioniPrimary (citable) accession number: P36659
    Secondary accession number(s): P77250
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It binds to curved DNA in a sequence-nonspecific fashion.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3