Reviewed, UniProtKB/Swiss-Prot P0A6Y8 (DNAK_ECOLI)

Names and origin

Protein names

Recommended name:
    Chaperone protein dnaK
Alternative name(s):
    Heat shock protein 70
    Heat shock 70 kDa protein
    HSP70

Gene names

Name:	dnaK
Synonyms:	groP, grpF, seg
Ordered Locus Names:	b0014, JW0013

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the dnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the dnaA protein. Also participates actively in the response to hyperosmotic shock. HAMAP MF_00332
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein. Ref.14
Post-translational modification	Autophosphorylated; grpE inhibits the autophosphorylation. Ref.11 Ref.12 Ref.13
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	DNA replication Stress response
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aldB	P37685	1	EBI-542092,EBI-1132062
ampC	P00811	1	EBI-542092,EBI-1134803
asd	P0A9Q9	1	EBI-542092,EBI-1132825
aspA	P0AC38	1	EBI-542092,EBI-544200
cysP	P16700	1	EBI-542092,EBI-560567
degP	P0C0V0	1	EBI-542092,EBI-547165
dnaJ	P08622	1	EBI-542092,EBI-545285
fabF	P0AAI5	1	EBI-542092,EBI-542783
fbaA	P0AB71	1	EBI-542092,EBI-370916
glnQ	P10346	1	EBI-542092,EBI-1120383
gloA	P0AC81	1	EBI-542092,EBI-551143
hrpB	P37024	1	EBI-542092,EBI-549226
htpG	P0A6Z3	1	EBI-542092,EBI-369221
ispH	P62623	1	EBI-542092,EBI-554022
luxS	P45578	1	EBI-542092,EBI-562313
metQ	P28635	1	EBI-542092,EBI-1114713
moeB	P12282	1	EBI-542092,EBI-554435
nadC	P30011	1	EBI-542092,EBI-551015
nfsA	P17117	1	EBI-542092,EBI-1120624
nrdB	P69924	1	EBI-542092,EBI-555196
phoA	P00634	1	EBI-542092,EBI-552958
qor	P28304	1	EBI-542092,EBI-556687
rne	P21513	1	EBI-542092,EBI-549958
rplY	P68919	1	EBI-542092,EBI-553087
rsmD	P0ADX9	1	EBI-542092,EBI-561207
serC	P23721	1	EBI-542092,EBI-557952
tnaA	P0A853	1	EBI-542092,EBI-371316
ugpB	P0AG80	1	EBI-542092,EBI-546637
ulaB	P69822	1	EBI-542092,EBI-1113922
ycgK	P76002	1	EBI-542092,EBI-1122554
ydhR	P0ACX3	1	EBI-542092,EBI-544817
ygcP	Q46906	1	EBI-542092,EBI-557727
ygeP	Q46796	1	EBI-542092,EBI-1130615
yhdN	P36677	1	EBI-542092,EBI-1124572
yhhX	P46853	1	EBI-542092,EBI-1132804
yjjI	P37342	1	EBI-542092,EBI-548519

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.5 Ref.6

Chain

2 – 638

637

Chaperone protein dnaK HAMAP MF_00332

PRO_0000078458

Amino acid modifications

Modified residue

109

1

N6-acetyllysine Ref.15

Modified residue

199

1

Phosphothreonine; by autocatalysis Ref.12 Ref.13

Modified residue

245

1

N6-acetyllysine Ref.15

Modified residue

304

1

N6-acetyllysine Ref.15

Modified residue

421

1

N6-acetyllysine Ref.15

Modified residue

556

1

N6-acetyllysine Ref.15

Experimental info

Mutagenesis

32

1

G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. Ref.9 Ref.10

Mutagenesis

436

1

V → I in mutant SEG-2; confers temperature sensitivity. Ref.10

Mutagenesis

455

1

G → D in mutant dnaK756(TS); confers temperature sensitivity. Ref.9

Mutagenesis

468

1

G → D in mutant dnaK756(TS); confers temperature sensitivity. Ref.9

Secondary structure

1

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638

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

11 – 20

10

Beta strand

23 – 26

4

Beta strand

34 – 37

4

Beta strand

39 – 42

4

Beta strand

48 – 51

4

Helix

52 – 55

4

Helix

62 – 64

3

Beta strand

65 – 67

3

Helix

69 – 71

3

Turn

72 – 74

3

Helix

80 – 85

6

Turn

86 – 88

3

Beta strand

90 – 95

6

Beta strand

97 – 105

9

Beta strand

108 – 110

3

Helix

112 – 131

20

Beta strand

137 – 140

4

Helix

148 – 160

13

Beta strand

164 – 166

3

Helix

171 – 179

9

Beta strand

187 – 195

9

Beta strand

200 – 208

9

Beta strand

217 – 226

10

Helix

229 – 248

20

Helix

256 – 272

17

Beta strand

275 – 289

15

Beta strand

292 – 301

10

Helix

302 – 308

7

Helix

310 – 325

16

Turn

326 – 328

3

Turn

331 – 333

3

Beta strand

336 – 341

6

Helix

342 – 345

4

Helix

347 – 357

11

Turn

367 – 369

3

Helix

370 – 378

9

Turn

379 – 382

4

Beta strand

392 – 394

3

Beta strand

399 – 403

5

Turn

404 – 406

3

Beta strand

407 – 412

6

Beta strand

417 – 430

14

Beta strand

435 – 444

10

Helix

448 – 450

3

Beta strand

451 – 460

10

Beta strand

472 – 478

7

Beta strand

484 – 490

7

Turn

491 – 493

3

Beta strand

496 – 501

6

Helix

509 – 521

13

Helix

523 – 553

31

Helix

554 – 556

3

Helix

559 – 576

18

Helix

581 – 594

14

Helix

596 – 605

10

Sequences

	Sequence		Length	Mass (Da)
	P0A6Y8-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5A8589B21D7CD9C1	FASTA	638	69,115
	10 20 30 40 50 60 MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT 70 80 90 100 110 120 NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL 130 140 150 160 170 180 KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG 190 200 210 220 230 240 LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL 250 260 270 280 290 300 VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 310 320 330 340 350 360 TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE 370 380 390 400 410 420 PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT 430 440 450 460 470 480 KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA 490 500 510 520 530 540 DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD 550 560 570 580 590 600 HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 610 620 630 IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous." Bardwell J.C.A., Craig E.A. Proc. Natl. Acad. Sci. U.S.A. 81:848-852(1984) [PubMed: 6322174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK." Schmid D., Jaussi R., Christen P. Eur. J. Biochem. 208:699-704(1992) [PubMed: 1396676] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product." Ohki M., Tamura F., Nishimura S., Uchida H. J. Biol. Chem. 261:1778-1781(1986) [PubMed: 3003084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 590-638.
[8]	"The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein." Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C. J. Biol. Chem. 261:1782-1785(1986) [PubMed: 3003085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-638.
[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., Tanaka S., Fujita H., Itikawa H. J. Bacteriol. 174:3715-3722(1992) [PubMed: 1592823] [Abstract] Cited for: MUTAGENESIS OF GLY-32; GLY-455 AND GLY-468. Strain: B.
[10]	"Involvement of DnaK protein in mini-F plasmid replication: temperature-sensitive seg mutations are located in the dnaK gene." Ezaki B., Ogura T., Mori H., Niki H., Hiraga S. Mol. Gen. Genet. 218:183-189(1989) [PubMed: 2674651] [Abstract] Cited for: MUTAGENESIS OF GLY-32 AND VAL-436. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]	"Identification of phosphoproteins in Escherichia coli." Freestone P., Grant S., Toth I., Norris V. Mol. Microbiol. 15:573-580(1995) [PubMed: 7783627] [Abstract] Cited for: PHOSPHORYLATION, PROTEIN SEQUENCE OF 2-11.
[12]	"DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity." McCarty J.S., Walker G.C. Proc. Natl. Acad. Sci. U.S.A. 88:9513-9517(1991) [PubMed: 1835085] [Abstract] Cited for: PHOSPHORYLATION AT THR-199.
[13]	"Inhibition of DnaK autophosphorylation by heat shock proteins and polypeptide substrates." Panagiotidis C.A., Burkholder W.F., Gaitanaris G.A., Gragerov A., Gottesman M.E., Silverstein S.J. J. Biol. Chem. 269:16643-16647(1994) [PubMed: 8206983] [Abstract] Cited for: PHOSPHORYLATION AT THR-199.
[14]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3.
[15]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304; LYS-421 AND LYS-556, MASS SPECTROMETRY.
[16]	"Structural analysis of substrate binding by the molecular chaperone DnaK." Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M., Gottesman M.E., Hendrickson W.A. Science 272:1606-1614(1996) [PubMed: 8658133] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 389-607.
[17]	"NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction." Wang H., Kurochkin A.V., Pang Y., Hu W., Flynn G.C., Zuiderweg E.R.P. Biochemistry 37:7929-7940(1998) [PubMed: 9609686] [Abstract] Cited for: STRUCTURE BY NMR OF 387-562.
[18]	"Structural insights into substrate binding by the molecular chaperone DnaK." Pellecchia M., Montgomery D.L., Stevens S.Y., Vander Kooi C.W., Feng H.P., Gierasch L.M., Zuiderweg E.R.P. Nat. Struct. Biol. 7:298-303(2000) [PubMed: 10742174] [Abstract] Cited for: STRUCTURE BY NMR OF 394-508.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K01298 Genomic DNA. Translation: AAA23694.1.
U00096 Genomic DNA. Translation: AAC73125.1.
AP009048 Genomic DNA. Translation: BAB96589.1.
D10765 Genomic DNA. Translation: BAA01595.1.
M12565 Genomic DNA. Translation: AAA23692.1.

PIR

IQECDK. A03311.

RefSeq

AP_000678.1.
NP_414555.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BPR	NMR	-	A	386-561	[»]
1DG4	NMR	-	A	393-507	[»]
1DKG	X-ray	2.80	D	1-383	[»]
1DKX	X-ray	2.00	A	389-607	[»]
1DKY	X-ray	2.80	A/B	389-607	[»]
1DKZ	X-ray	2.00	A	389-607	[»]
1Q5L	NMR	-	A	393-506	[»]
2BPR	NMR	-	A	386-561	[»]
2KHO	NMR	-	A	1-605	[»]
3DPO	X-ray	2.10	A/B	389-607	[»]
3DPP	X-ray	2.50	A/B	389-607	[»]
3DPQ	X-ray	2.60	A/B/E/F	389-607	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6Y8. 365 interactions.

Protein family/group databases

TCDB

1.A.33.1.2. cation channel-forming heat shock protein-70 (Hsp70) family.

PTM databases

PhosSite

P0A6Y8.

2-D gel databases

SWISS-2DPAGE

P0A6Y8.

2DBase-Ecoli

P0A6Y8.

ECO2DBASE

B066.0. 6TH EDITION.

Genome annotation databases

GeneID

944750.

GenomeReviews

Gene locus JW0013 in contig AP009048_GR.
Gene locus b0014 in contig U00096_GR.

KEGG

ecj:JW0013.
eco:b0014.

Organism-specific databases

EchoBASE

EB0237.

EcoGene

EG10241. dnaK.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6Y8.

OMA

P0A6Y8. ANNGDAW.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10241-MON.

Family and domain databases

HAMAP

MF_00332.
[Tree]

InterPro

IPR012725. DnaK_prok.
IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

ProDom

PD000089. Hsp70. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR02350. prok_dnaK. 1 hit.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DNAK_ECOLI

Accession

Primary (citable) accession number: P0A6Y8
Secondary accession number(s): P04475

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)