DNAK_VARPS
ID DNAK_VARPS Reviewed; 645 AA.
AC C5CU12;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Vapar_1712;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS18362.1; -; Genomic_DNA.
DR RefSeq; WP_012746854.1; NC_012791.1.
DR AlphaFoldDB; C5CU12; -.
DR SMR; C5CU12; -.
DR STRING; 543728.Vapar_1712; -.
DR EnsemblBacteria; ACS18362; ACS18362; Vapar_1712.
DR GeneID; 45056018; -.
DR KEGG; vap:Vapar_1712; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
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..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205201"
FT REGION 608..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 645 AA; 69013 MW; B5F01127E85D18AA CRC64;
MAKIIGIDLG TTNSCVSIME GNTTRVIENS EGARTTPSIV AYQEDGEVLV GASAKRQAVT
NPKNTLYAIK RLIGRKFEEK EVQKDIDLMP YTIAKADNGD AWVEVRGKKI APQQVSADIL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKQDKADRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
IIAEFKKEQG VDLGKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
LTRAKLESLV DELVERTIAP CRLAIKDAGI SVSDINDVIL VGGMTRMPKV QEKVKAFFGK
EPRKDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETMGGVMT KMITKNTTIP
TKFAQTFSTA EDNQPAVTIK VFQGEREIAS GNKLLGEFNL EGIPPAARGT PQIEVSFDID
ANGILHVGAK DKGTGKENKI TIKANSGLSE DEIQKMVKDA ELNAAEDKKK VELAQARNQG
EAMVHSVKKS LGEHGASLDA GEKEKIEAAI KDLEEALKGE DKASIEEKTN TLMTASQKLG
EKMYADAQAA AGAAGGPGAA AGPEAASAPA DDNVVDAEVK EVKKG