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Protein

Curved DNA-binding protein

Gene

cbpA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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 – 105Combined sources
Helixi18 – 3215Combined sources
Turni34 – 363Combined sources
Beta strandi39 – 413Combined sources
Helixi42 – 5615Combined sources
Helixi59 – 7012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP36659.
KOiK05516.
OMAiEREIPRT.
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

        10         20         30         40         50
MELKDYYAIM GVKPTDDLKT IKTAYRRLAR KYHPDVSKEP DAEARFKEVA
60 70 80 90 100
EAWEVLSDEQ RRAEYDQMWQ HRNDPQFNRQ FHHGDGQSFN AEDFDDIFSS
110 120 130 140 150
IFGQHARQSR QRPATRGHDI EIEVAVFLEE TLTEHKRTIS YNLPVYNAFG
160 170 180 190 200
MIEQEIPKTL NVKIPAGVGN GQRIRLKGQG TPGENGGPNG DLWLVIHIAP
210 220 230 240 250
HPLFDIVGQD LEIVVPVSPW EAALGAKVTV PTLKESILLT IPPGSQAGQR
260 270 280 290 300
LRVKGKGLVS KKQTGDLYAV LKIVMPPKPD ENTAALWQQL ADAQSSFDPR

KDWGKA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP36659.
PRIDEiP36659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB2110.
EcoGeneiEG12193. cbpA.

Phylogenomic databases

eggNOGiCOG2214.
HOGENOMiHOG000226716.
InParanoidiP36659.
KOiK05516.
OMAiEREIPRT.
OrthoDBiEOG6BPDKP.
PhylomeDBiP36659.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP36659.
PROiP36659.

Gene expression databases

GenevestigatoriP36659.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.