DNAK_HALHL
ID DNAK_HALHL Reviewed; 647 AA.
AC A1WX31;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Hhal_1476;
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-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; CP000544; ABM62243.1; -; Genomic_DNA.
DR RefSeq; WP_011814265.1; NC_008789.1.
DR AlphaFoldDB; A1WX31; -.
DR SMR; A1WX31; -.
DR STRING; 349124.Hhal_1476; -.
DR PRIDE; A1WX31; -.
DR EnsemblBacteria; ABM62243; ABM62243; Hhal_1476.
DR KEGG; hha:Hhal_1476; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000647; 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..647
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059575"
FT REGION 545..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..647
FT /note="Basic and acidic 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 647 AA; 69957 MW; CEC7A925D5DDC404 CRC64;
MGKIIGIDLG TTNSCVAVME GNKTRVIENA EGDRTTPSVV AFAEDGEVLT GAPAKRQSVT
NPENTIHAVK RLIGRRFDED VVQRDIKEMP YKIVKADNGD AWVEAQGKKM APPEVSARTL
QKMKSTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
LDKEGGDKKV AVYDLGGGTF DVSIIEIAEV DGEKQFEVLS TSGDTFLGGE DFDKRIIDYL
IQEFKKDQGI DLAQDHLALQ RLREAAEKAK VELSSSQQTE INLPYITADQ SGPKHMAIKL
TRAKLESLVE DLVERTIEPC KTALKDAGLA AGDIQDVILV GGQTRMPKVQ EKVKEYFGQD
PRKDVNPDEA VAVGAAIQAG VLGGDVKDVL LLDVTPLSLG IETLGGVMTK IIEKNTTIPT
KGTQTFSTAE DNQTAVTVHV LQGEREMAKD NKSLGRFDLT DIPPSPRGVP QIEVAFDIDA
NGILNVSAKD KATGKETGIE IKASSGLTED EIERMVKEAE ENAEEDRRQR ELVEARNQAE
NMIHSTRKSL SDLGEQVGDA EKQEIESAIS ELEQVKDGED KDAIEQKTQE LATKAGELAQ
KAYQQAGGGD EASADAGAGE TASGEQKEDV VDADFEEVKD EDGNSRK