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Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)

 DNAK_ECOLI              Reviewed;         638 AA.
P0A6Y8; P04475;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-DEC-2017, entry version 135.
RecName: Full=Chaperone protein DnaK;
AltName: Full=HSP70;
AltName: Full=Heat shock 70 kDa protein;
AltName: Full=Heat shock protein 70;
Name=dnaK; Synonyms=groP, grpF, seg; OrderedLocusNames=b0014, JW0013;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6322174; DOI=10.1073/pnas.81.3.848;
Bardwell J.C.A., Craig E.A.;
"Major heat shock gene of Drosophila and the Escherichia coli heat-
inducible dnaK gene are homologous.";
Proc. Natl. Acad. Sci. U.S.A. 81:848-852(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-15.
PubMed=1396676; DOI=10.1111/j.1432-1033.1992.tb17237.x;
Schmid D., Jaussi R., Christen P.;
"Precursor of mitochondrial aspartate aminotransferase synthesized in
Escherichia coli is complexed with heat-shock protein DnaK.";
Eur. J. Biochem. 208:699-704(1992).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 590-638.
PubMed=3003084;
Ohki M., Tamura F., Nishimura S., Uchida H.;
"Nucleotide sequence of the Escherichia coli dnaJ gene and
purification of the gene product.";
J. Biol. Chem. 261:1778-1781(1986).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-638.
PubMed=3003085;
Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M.,
Georgopoulos C.;
"The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A
gene that encodes a heat shock protein.";
J. Biol. Chem. 261:1782-1785(1986).
[9]
MUTAGENESIS OF GLY-32; GLY-455 AND GLY-468.
STRAIN=B;
PubMed=1592823; DOI=10.1128/jb.174.11.3715-3722.1992;
Miyazaki T., Tanaka S., Fujita H., Itikawa H.;
"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).";
J. Bacteriol. 174:3715-3722(1992).
[10]
MUTAGENESIS OF GLY-32 AND VAL-436.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=2674651; DOI=10.1007/BF00331267;
Ezaki B., Ogura T., Mori H., Niki H., Hiraga S.;
"Involvement of DnaK protein in mini-F plasmid replication:
temperature-sensitive seg mutations are located in the dnaK gene.";
Mol. Gen. Genet. 218:183-189(1989).
[11]
PHOSPHORYLATION, AND PROTEIN SEQUENCE OF 2-11.
PubMed=7783627; DOI=10.1111/j.1365-2958.1995.tb02270.x;
Freestone P., Grant S., Toth I., Norris V.;
"Identification of phosphoproteins in Escherichia coli.";
Mol. Microbiol. 15:573-580(1995).
[12]
PHOSPHORYLATION AT THR-199.
PubMed=1835085; DOI=10.1073/pnas.88.21.9513;
McCarty J.S., Walker G.C.;
"DnaK as a thermometer: threonine-199 is site of autophosphorylation
and is critical for ATPase activity.";
Proc. Natl. Acad. Sci. U.S.A. 88:9513-9517(1991).
[13]
PHOSPHORYLATION AT THR-199.
PubMed=8206983;
Panagiotidis C.A., Burkholder W.F., Gaitanaris G.A., Gragerov A.,
Gottesman M.E., Silverstein S.J.;
"Inhibition of DnaK autophosphorylation by heat shock proteins and
polypeptide substrates.";
J. Biol. Chem. 269:16643-16647(1994).
[14]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[15]
DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=14726952; DOI=10.1038/sj.embor.7400067;
Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S.,
Hartl F.U., Georgopoulos C.;
"In vivo analysis of the overlapping functions of DnaK and trigger
factor.";
EMBO Rep. 5:195-200(2004).
[16]
SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304;
LYS-421 AND LYS-556, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[18]
SUCCINYLATION AT LYS-70; LYS-245; LYS-246; LYS-304; LYS-359; LYS-502;
LYS-528 AND LYS-587.
STRAIN=K12;
PubMed=21151122; DOI=10.1038/nchembio.495;
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
"Identification of lysine succinylation as a new post-translational
modification.";
Nat. Chem. Biol. 7:58-63(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 389-607.
PubMed=8658133; DOI=10.1126/science.272.5268.1606;
Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M.,
Gottesman M.E., Hendrickson W.A.;
"Structural analysis of substrate binding by the molecular chaperone
DnaK.";
Science 272:1606-1614(1996).
[20]
STRUCTURE BY NMR OF 387-562.
PubMed=9609686; DOI=10.1021/bi9800855;
Wang H., Kurochkin A.V., Pang Y., Hu W., Flynn G.C., Zuiderweg E.R.P.;
"NMR solution structure of the 21 kDa chaperone protein DnaK substrate
binding domain: a preview of chaperone-protein interaction.";
Biochemistry 37:7929-7940(1998).
[21]
STRUCTURE BY NMR OF 394-508.
PubMed=10742174; DOI=10.1038/74062;
Pellecchia M., Montgomery D.L., Stevens S.Y., Vander Kooi C.W.,
Feng H.P., Gierasch L.M., Zuiderweg E.R.P.;
"Structural insights into substrate binding by the molecular chaperone
DnaK.";
Nat. Struct. Biol. 7:298-303(2000).
-!- 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.
-!- INTERACTION:
P0AC38:aspA; NbExp=3; IntAct=EBI-542092, EBI-544200;
P36659:cbpA; NbExp=5; IntAct=EBI-542092, EBI-546131;
P04233:CD74 (xeno); NbExp=8; IntAct=EBI-542092, EBI-2622890;
P63284:clpB; NbExp=8; IntAct=EBI-542092, EBI-546182;
P08622:dnaJ; NbExp=8; IntAct=EBI-542092, EBI-545285;
P0AAI5:fabF; NbExp=3; IntAct=EBI-542092, EBI-542783;
P0AB71:fbaA; NbExp=3; IntAct=EBI-542092, EBI-370916;
P0AC81:gloA; NbExp=3; IntAct=EBI-542092, EBI-551143;
P09372:grpE; NbExp=10; IntAct=EBI-542092, EBI-547441;
P13760:HLA-DRB1 (xeno); NbExp=5; IntAct=EBI-542092, EBI-1033104;
Q30134:HLA-DRB1 (xeno); NbExp=7; IntAct=EBI-542092, EBI-13952091;
P0A6Z3:htpG; NbExp=3; IntAct=EBI-542092, EBI-369221;
P45578:luxS; NbExp=2; IntAct=EBI-542092, EBI-562313;
P12282:moeB; NbExp=2; IntAct=EBI-542092, EBI-554435;
P69924:nrdB; NbExp=2; IntAct=EBI-542092, EBI-555196;
P28304:qorA; NbExp=2; IntAct=EBI-542092, EBI-556687;
P21513:rne; NbExp=10; IntAct=EBI-542092, EBI-549958;
P0AGB3:rpoH; NbExp=7; IntAct=EBI-542092, EBI-555342;
P0ADX9:rsmD; NbExp=2; IntAct=EBI-542092, EBI-561207;
P23721:serC; NbExp=2; IntAct=EBI-542092, EBI-557952;
P0A853:tnaA; NbExp=2; IntAct=EBI-542092, EBI-371316;
P0ACX3:ydhR; NbExp=3; IntAct=EBI-542092, EBI-544817;
Q46906:ygcP; NbExp=3; IntAct=EBI-542092, EBI-557727;
P37342:yjjI; NbExp=2; IntAct=EBI-542092, EBI-548519;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}.
Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral
membrane protein {ECO:0000269|PubMed:16079137}.
-!- PTM: Autophosphorylated; GrpE inhibits the autophosphorylation.
{ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:7783627,
ECO:0000269|PubMed:8206983}.
-!- DISRUPTION PHENOTYPE: Non-essential; synthetic lethality is seen
in a triple tig-dnaK-dnaJ disruption, although this depends on
temperature (triple disruptions grow slowly at 20 and 34 degrees
Celsius but not at all at 43 degrees) and strain background.
{ECO:0000269|PubMed:14726952}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; K01298; AAA23694.1; -; Genomic_DNA.
EMBL; U00096; AAC73125.1; -; Genomic_DNA.
EMBL; AP009048; BAB96589.1; -; Genomic_DNA.
EMBL; D10765; BAA01595.1; -; Genomic_DNA.
EMBL; M12565; AAA23692.1; -; Genomic_DNA.
PIR; A03311; IQECDK.
RefSeq; NP_414555.1; NC_000913.3.
RefSeq; WP_000516135.1; NZ_LN832404.1.
PDB; 1BPR; NMR; -; A=384-561.
PDB; 1DG4; NMR; -; A=393-507.
PDB; 1DKG; X-ray; 2.80 A; D=1-383.
PDB; 1DKX; X-ray; 2.00 A; A=389-607.
PDB; 1DKY; X-ray; 2.80 A; A/B=389-607.
PDB; 1DKZ; X-ray; 2.00 A; A=389-607.
PDB; 1Q5L; NMR; -; A=393-507.
PDB; 2BPR; NMR; -; A=384-561.
PDB; 2KHO; NMR; -; A=1-605.
PDB; 3DPO; X-ray; 2.10 A; A/B=389-607.
PDB; 3DPP; X-ray; 2.50 A; A/B=389-607.
PDB; 3DPQ; X-ray; 2.60 A; A/B/E/F=389-601.
PDB; 3QNJ; X-ray; 2.28 A; A/B=389-607.
PDB; 4B9Q; X-ray; 2.40 A; A/B/C/D=1-605.
PDB; 4E81; X-ray; 1.90 A; A/B=389-607.
PDB; 4EZN; X-ray; 1.80 A; A/B=389-607.
PDB; 4EZO; X-ray; 1.90 A; A/B=389-607.
PDB; 4EZP; X-ray; 1.65 A; A/B=389-607.
PDB; 4EZQ; X-ray; 2.00 A; A=389-607.
PDB; 4EZR; X-ray; 1.90 A; A=389-607.
PDB; 4EZS; X-ray; 1.90 A; A=389-607.
PDB; 4EZT; X-ray; 2.00 A; A=389-607.
PDB; 4EZU; X-ray; 1.90 A; A=389-607.
PDB; 4EZV; X-ray; 2.10 A; A/B=389-607.
PDB; 4EZW; X-ray; 1.80 A; A/B/C/D=389-607.
PDB; 4EZX; X-ray; 1.70 A; A/B=389-607.
PDB; 4EZY; X-ray; 1.85 A; A=389-607.
PDB; 4EZZ; X-ray; 2.05 A; A=389-607.
PDB; 4F00; X-ray; 1.95 A; A=389-607.
PDB; 4F01; X-ray; 1.40 A; A/B=389-607.
PDB; 4HY9; X-ray; 1.55 A; A/B=389-607.
PDB; 4HYB; X-ray; 1.70 A; A/B=389-607.
PDB; 4JN4; X-ray; 2.30 A; A/B=2-610.
PDB; 4JNE; X-ray; 1.96 A; A/B=2-610.
PDB; 4JNF; X-ray; 1.62 A; A=389-610.
PDB; 4JWC; X-ray; 1.80 A; A/B=389-607.
PDB; 4JWD; X-ray; 1.95 A; A/B=389-607.
PDB; 4JWE; X-ray; 1.95 A; A/B=389-607.
PDB; 4JWI; X-ray; 1.90 A; A/B=389-607.
PDB; 4R5G; X-ray; 3.45 A; A/B=389-607.
PDB; 4R5I; X-ray; 1.97 A; A=389-607.
PDB; 4R5J; X-ray; 2.36 A; A/B/C/D=389-607.
PDB; 4R5K; X-ray; 1.75 A; A/B=389-607.
PDB; 4R5L; X-ray; 2.97 A; A/B/C/D=389-607.
PDBsum; 1BPR; -.
PDBsum; 1DG4; -.
PDBsum; 1DKG; -.
PDBsum; 1DKX; -.
PDBsum; 1DKY; -.
PDBsum; 1DKZ; -.
PDBsum; 1Q5L; -.
PDBsum; 2BPR; -.
PDBsum; 2KHO; -.
PDBsum; 3DPO; -.
PDBsum; 3DPP; -.
PDBsum; 3DPQ; -.
PDBsum; 3QNJ; -.
PDBsum; 4B9Q; -.
PDBsum; 4E81; -.
PDBsum; 4EZN; -.
PDBsum; 4EZO; -.
PDBsum; 4EZP; -.
PDBsum; 4EZQ; -.
PDBsum; 4EZR; -.
PDBsum; 4EZS; -.
PDBsum; 4EZT; -.
PDBsum; 4EZU; -.
PDBsum; 4EZV; -.
PDBsum; 4EZW; -.
PDBsum; 4EZX; -.
PDBsum; 4EZY; -.
PDBsum; 4EZZ; -.
PDBsum; 4F00; -.
PDBsum; 4F01; -.
PDBsum; 4HY9; -.
PDBsum; 4HYB; -.
PDBsum; 4JN4; -.
PDBsum; 4JNE; -.
PDBsum; 4JNF; -.
PDBsum; 4JWC; -.
PDBsum; 4JWD; -.
PDBsum; 4JWE; -.
PDBsum; 4JWI; -.
PDBsum; 4R5G; -.
PDBsum; 4R5I; -.
PDBsum; 4R5J; -.
PDBsum; 4R5K; -.
PDBsum; 4R5L; -.
ProteinModelPortal; P0A6Y8; -.
SMR; P0A6Y8; -.
BioGrid; 4259520; 182.
BioGrid; 849153; 10.
DIP; DIP-35751N; -.
IntAct; P0A6Y8; 380.
MINT; MINT-7259066; -.
STRING; 316385.ECDH10B_0014; -.
TCDB; 1.A.33.1.2; the cation channel-forming heat shock protein-70 (hsp70) family.
iPTMnet; P0A6Y8; -.
SWISS-2DPAGE; P0A6Y8; -.
PaxDb; P0A6Y8; -.
PRIDE; P0A6Y8; -.
EnsemblBacteria; AAC73125; AAC73125; b0014.
EnsemblBacteria; BAB96589; BAB96589; BAB96589.
GeneID; 944750; -.
KEGG; ecj:JW0013; -.
KEGG; eco:b0014; -.
PATRIC; fig|1411691.4.peg.2270; -.
EchoBASE; EB0237; -.
EcoGene; EG10241; dnaK.
eggNOG; ENOG4105CFG; Bacteria.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228136; -.
InParanoid; P0A6Y8; -.
KO; K04043; -.
PhylomeDB; P0A6Y8; -.
BioCyc; EcoCyc:EG10241-MONOMER; -.
BioCyc; MetaCyc:EG10241-MONOMER; -.
EvolutionaryTrace; P0A6Y8; -.
PRO; PR:P0A6Y8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0016887; F:ATPase activity; IDA:CAFA.
GO; GO:0051087; F:chaperone binding; IPI:CAFA.
GO; GO:0044183; F:protein binding involved in protein folding; IDA:EcoCyc.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
GO; GO:0051082; F:unfolded protein binding; IDA:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0034620; P:cellular response to unfolded protein; IDA:EcoCyc.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:CAFA.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006461; P:protein complex assembly; IDA:CAFA.
GO; GO:0043241; P:protein complex disassembly; IDA:EcoCyc.
GO; GO:0009408; P:response to heat; IDA:EcoCyc.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR012725; Chaperone_DnaK.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
TIGRFAMs; TIGR02350; prok_dnaK; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell inner membrane;
Cell membrane; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA replication; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1396676,
ECO:0000269|PubMed:7783627,
ECO:0000269|PubMed:9298646}.
CHAIN 2 638 Chaperone protein DnaK.
/FTId=PRO_0000078458.
MOD_RES 70 70 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 199 199 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:1835085,
ECO:0000269|PubMed:8206983}.
MOD_RES 245 245 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18723842}.
MOD_RES 245 245 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
MOD_RES 246 246 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 304 304 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18723842}.
MOD_RES 304 304 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
MOD_RES 359 359 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 421 421 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 502 502 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 528 528 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 556 556 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 587 587 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MUTAGEN 32 32 G->D: In SEG-1 and dnaK756(TS); confers
temperature sensitivity.
{ECO:0000269|PubMed:1592823,
ECO:0000269|PubMed:2674651}.
MUTAGEN 436 436 V->I: In SEG-2; confers temperature
sensitivity.
{ECO:0000269|PubMed:2674651}.
MUTAGEN 455 455 G->D: In dnaK756(TS); confers temperature
sensitivity.
{ECO:0000269|PubMed:1592823}.
MUTAGEN 468 468 G->D: In dnaK756(TS); confers temperature
sensitivity.
{ECO:0000269|PubMed:1592823}.
STRAND 4 8 {ECO:0000244|PDB:4JNE}.
STRAND 11 20 {ECO:0000244|PDB:4JNE}.
STRAND 23 26 {ECO:0000244|PDB:4JNE}.
STRAND 34 37 {ECO:0000244|PDB:4JNE}.
STRAND 39 42 {ECO:0000244|PDB:4JNE}.
STRAND 48 51 {ECO:0000244|PDB:4JNE}.
HELIX 52 56 {ECO:0000244|PDB:4JNE}.
HELIX 57 60 {ECO:0000244|PDB:4JNE}.
HELIX 62 64 {ECO:0000244|PDB:4JNE}.
STRAND 65 67 {ECO:0000244|PDB:4JNE}.
HELIX 69 71 {ECO:0000244|PDB:4JNE}.
TURN 72 74 {ECO:0000244|PDB:4JNE}.
STRAND 76 79 {ECO:0000244|PDB:2KHO}.
HELIX 80 88 {ECO:0000244|PDB:4JNE}.
STRAND 90 95 {ECO:0000244|PDB:4JNE}.
STRAND 99 105 {ECO:0000244|PDB:4JNE}.
STRAND 108 110 {ECO:0000244|PDB:4JNE}.
HELIX 112 131 {ECO:0000244|PDB:4JNE}.
STRAND 137 142 {ECO:0000244|PDB:4JNE}.
HELIX 148 160 {ECO:0000244|PDB:4JNE}.
STRAND 164 170 {ECO:0000244|PDB:4JNE}.
HELIX 171 181 {ECO:0000244|PDB:4JNE}.
STRAND 187 195 {ECO:0000244|PDB:4JNE}.
STRAND 200 210 {ECO:0000244|PDB:4JNE}.
STRAND 213 224 {ECO:0000244|PDB:4JNE}.
HELIX 229 248 {ECO:0000244|PDB:4JNE}.
HELIX 252 254 {ECO:0000244|PDB:4JNE}.
HELIX 256 272 {ECO:0000244|PDB:4JNE}.
TURN 273 275 {ECO:0000244|PDB:4JNE}.
STRAND 276 289 {ECO:0000244|PDB:4JNE}.
STRAND 292 301 {ECO:0000244|PDB:4JNE}.
HELIX 302 327 {ECO:0000244|PDB:4JNE}.
HELIX 331 333 {ECO:0000244|PDB:4JNE}.
STRAND 335 341 {ECO:0000244|PDB:4JNE}.
HELIX 342 345 {ECO:0000244|PDB:4JNE}.
HELIX 347 357 {ECO:0000244|PDB:4JNE}.
STRAND 363 365 {ECO:0000244|PDB:4JNE}.
TURN 367 369 {ECO:0000244|PDB:4JNE}.
HELIX 370 382 {ECO:0000244|PDB:4JNE}.
STRAND 384 386 {ECO:0000244|PDB:4B9Q}.
STRAND 392 395 {ECO:0000244|PDB:4EZW}.
STRAND 399 403 {ECO:0000244|PDB:4F01}.
TURN 404 406 {ECO:0000244|PDB:4F01}.
STRAND 407 412 {ECO:0000244|PDB:4F01}.
STRAND 414 416 {ECO:0000244|PDB:1Q5L}.
STRAND 417 430 {ECO:0000244|PDB:4F01}.
STRAND 432 434 {ECO:0000244|PDB:4JNE}.
STRAND 436 444 {ECO:0000244|PDB:4F01}.
STRAND 445 447 {ECO:0000244|PDB:1Q5L}.
HELIX 448 450 {ECO:0000244|PDB:4F01}.
STRAND 451 459 {ECO:0000244|PDB:4F01}.
HELIX 466 468 {ECO:0000244|PDB:4JNF}.
STRAND 472 478 {ECO:0000244|PDB:4F01}.
STRAND 480 482 {ECO:0000244|PDB:1BPR}.
STRAND 484 490 {ECO:0000244|PDB:4F01}.
TURN 491 493 {ECO:0000244|PDB:4F01}.
STRAND 496 500 {ECO:0000244|PDB:4F01}.
HELIX 503 505 {ECO:0000244|PDB:4F01}.
HELIX 509 521 {ECO:0000244|PDB:4F01}.
HELIX 523 553 {ECO:0000244|PDB:4F01}.
HELIX 554 556 {ECO:0000244|PDB:4F01}.
HELIX 559 577 {ECO:0000244|PDB:4F01}.
HELIX 581 594 {ECO:0000244|PDB:4F01}.
HELIX 596 600 {ECO:0000244|PDB:4F01}.
SEQUENCE 638 AA; 69115 MW; 5A8589B21D7CD9C1 CRC64;
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD
HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK


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