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1.A.33.1.2
Heat shock protein-70 homologue, DnaK.  A transport function in eukaryotes, but not prokaryotes has been demonstrated.

Accession Number:P0A6Y8
Protein Name:Chaperone DnaK aka GRPF aka GROP aka SEG aka B0014
Length:638
Molecular Weight:69115.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cytoplasm1 / Peripheral membrane protein2
Substrate NONE, ions

Cross database links:

Genevestigator: P0A6Y8
EchoBASE: EB0237
EcoGene: EG10241
eggNOG: COG0443
HEGENOM: HBG334976
DIP: DIP-35751N
RefSeq: AP_000678.1    NP_414555.1   
Entrez Gene ID: 944750   
Pfam: PF00012   
BioCyc: EcoCyc:EG10241-MONOMER    ECOL168927:B0014-MONOMER   
KEGG: ecj:JW0013    eco:b0014   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0051082 F:unfolded protein binding
GO:0008270 F:zinc ion binding
GO:0006260 P:DNA replication
GO:0006457 P:protein folding
GO:0009408 P:response to heat

References (18)

[1] “Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.”  Bardwell J.C.A.et.al.   6322174
[2] “Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.”  Yura T.et.al.   1630901
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK.”  Schmid D.et.al.   1396676
[6] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[7] “Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.”  Ohki M.et.al.   3003084
[8] “The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.”  Bardwell J.C.A.et.al.   3003085
[9] “DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts).”  Miyazaki T.et.al.   1592823
[10] “Involvement of DnaK protein in mini-F plasmid replication: temperature-sensitive seg mutations are located in the dnaK gene.”  Ezaki B.et.al.   2674651
[11] “Identification of phosphoproteins in Escherichia coli.”  Freestone P.et.al.   7783627
[12] “DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.”  McCarty J.S.et.al.   1835085
[13] “Inhibition of DnaK autophosphorylation by heat shock proteins and polypeptide substrates.”  Panagiotidis C.A.et.al.   8206983
[14] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137
[15] “Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.”  Zhang J.et.al.   18723842
[16] “Structural analysis of substrate binding by the molecular chaperone DnaK.”  Zhu X.et.al.   8658133
[17] “NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.”  Wang H.et.al.   9609686
[18] “Structural insights into substrate binding by the molecular chaperone DnaK.”  Pellecchia M.et.al.   10742174
Structure:
1BPR   1DG4   1DKG   1DKX   1DKY   1DKZ   1Q5L   2BPR   2KHO   3DPO   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT 
61:	NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL 
121:	KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG 
181:	LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL 
241:	VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 
301:	TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE 
361:	PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT 
421:	KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA 
481:	DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD 
541:	HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 
601:	IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK