DNAK_THIDA
ID DNAK_THIDA Reviewed; 639 AA.
AC Q3SIN4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Tbd_1538;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000116; AAZ97491.1; -; Genomic_DNA.
DR RefSeq; WP_011312050.1; NC_007404.1.
DR AlphaFoldDB; Q3SIN4; -.
DR SMR; Q3SIN4; -.
DR STRING; 292415.Tbd_1538; -.
DR PRIDE; Q3SIN4; -.
DR EnsemblBacteria; AAZ97491; AAZ97491; Tbd_1538.
DR KEGG; tbd:Tbd_1538; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008291; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226024"
FT REGION 600..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68996 MW; 7EBDE7CEA719043B CRC64;
MGRIIGIDLG TTNSCVAVME NGSPKVIENA EGARTTPSIV AYAEDGEILV GAPAKRQAVT
NPKNTIFAVK RLIGRRFEEK EVQKDIGLMP YKIVKADNGD AWVEVRDKKM AAQQVSAEIL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
MDKKEGDRKI AVYDLGGGTF DISIIEIAEM DGEHQFEVLS TNGDTFLGGE DFDQRLIDYI
AEEFKKEQGV DLKKDVLALQ RLKEAAEKAK IELSSGQQTE VNLPYITADA SGPKHLAVKI
TRAKFESLVE ELITRTIEPC KLALKDAGLT TSQIDDVILV GGQTRMPKVM DAVKDFFGKE
PRRDVNPDEA VAVGAAIQGG VLQGEVKDVL LLDVTPLSLG IETLGGVMTK LIPKNTTIPT
KASQVFSTAD DNQSAVTVHV LQGEREMASG NKSLGQFNLS DIPPAPRGMP QIEVTFDIDA
NGILHVSAKD KATGKENKIR IQASSGLSEE EIQRMVKDAE ANAAEDHKAF ELAGARNAAD
AMIHSVKKSL AEYGDKVSAD EKATIESALK EAEDAVREGD KETIETKTNA LATASHKLAE
QMYQAEQAKA QPAGETGNQS TGPGNDDVVD AEFEEVKDK