DNAK_JANSC
ID DNAK_JANSC Reviewed; 639 AA.
AC Q28VY3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Jann_0212;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000264; ABD53129.1; -; Genomic_DNA.
DR RefSeq; WP_011453338.1; NC_007802.1.
DR AlphaFoldDB; Q28VY3; -.
DR SMR; Q28VY3; -.
DR STRING; 290400.Jann_0212; -.
DR PRIDE; Q28VY3; -.
DR EnsemblBacteria; ABD53129; ABD53129; Jann_0212.
DR KEGG; jan:Jann_0212; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008326; 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_1000059582"
FT REGION 514..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68930 MW; 74C71FD0CE39EC37 CRC64;
MAKVIGIDLG TTNSCVAIMD GSQPRVIENA EGARTTPSIV AFTDDERLAG QSAKRQAVTN
PENTIFGVKR LIGRRINDEH LEKDKKNLPF EIVDGGNGDA WVKAKGETYS PSQISAFILQ
KMKETAESYL GEDVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKKETRTIAV YDLGGGTFDV TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLAEEFKK
ENSVDLTQDK MALQRLKEAA EKAKIELSSA SQTEINQPFI SMGSNGQPLH MVMKLTRAKL
ESLVGDLIKA SIKPCAAALK DAGLSKGDID EVVLVGGMTR MPKVIDEVTK FFGKEPHKGV
NPDEVVAMGA AIQAGVLQGD VKDVVLLDVT PLSMGIETLG GVFTRLIDRN TTIPTKKSQI
FSTADDNQSA VTLRVFQGER EMAADNKILG QFNLEGIPPA PRGVPQIEVT FDIDANGIVS
VGAKDKGTGK EQQITIQASG GLSDDDIEAM VREAEENAEA DKDRKDLVET RNQAESLVHG
TEKSLEEHGE KVDPSTVEAI ELALGALKET LETDDTAKIK GGIQNVTEAA MRLGEAIYKA
EADKAEAAQD GAPEEEERGV DEDIVDADFE DLDDDRKRG