DNAK_CHESB
ID DNAK_CHESB Reviewed; 636 AA.
AC Q11KJ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Meso_0679;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
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., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-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; CP000390; ABG62079.1; -; Genomic_DNA.
DR RefSeq; WP_011580022.1; NC_008254.1.
DR AlphaFoldDB; Q11KJ6; -.
DR SMR; Q11KJ6; -.
DR STRING; 266779.Meso_0679; -.
DR PRIDE; Q11KJ6; -.
DR EnsemblBacteria; ABG62079; ABG62079; Meso_0679.
DR KEGG; mes:Meso_0679; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
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 Stress response.
FT CHAIN 1..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059599"
FT REGION 603..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 636 AA; 68648 MW; 2EF0C44427EB4177 CRC64;
MAKVIGIDLG TTNSCVAVMD GKDAKVIENA EGARTTPSIV AFTDSDERLV GQPAKRQAVT
NPENTFFAIK RLIGRRFEDP MVEKDKKLVP YKIVKADNGD AWVESHGTKY SPSQISAMIL
QKMKETAESY LGEKVEKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKKEGKTIA VYDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDMR LVNYLADEFK
KEQGIDLKND KLALQRLKEA AEKAKIELSS SSQTEINLPF ITADQTGPKH LAIKLTRAKF
ESLVEDLVTR TIEPCRAALK DAGLSAGEID EVVLVGGMTR MPKVQETVKN FFGKEPHKGV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
FSTAEDNQNA VTIRVFQGER EMAADNKLLG QFDLVGIPPA PRGMPQIEVT FDIDANGIVN
VSAKDKGTGK EQQIRIQASG GLSDAEIEKM VKDAEANAEA DKKRRETVEV KNQAEALIHS
TEKSLKDYGD KVSEDDRKAI ENAIAELKTA TEGEDADAIR AKTTALAEAS MKLGQAVYEA
SQAENAAGGT EETGGAKDDV VDADFEEIDE DDKKSA