DNAK_ONYPE
ID DNAK_ONYPE Reviewed; 615 AA.
AC Q6YPM1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=PAM_704;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD04789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP006628; BAD04789.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6YPM1; -.
DR SMR; Q6YPM1; -.
DR STRING; 262768.PAM_704; -.
DR EnsemblBacteria; BAD04789; BAD04789; PAM_704.
DR KEGG; poy:PAM_704; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; OYEL262768:G1G26-857-MON; -.
DR Proteomes; UP000002523; 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; 2.
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..615
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225988"
FT REGION 567..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 615 AA; 66958 MW; 5D3E814EE4073CD2 CRC64;
MTKTNKIIGI DLGTTNSCVA VMEGGEAKVI PNAEGGRTTP SVVSFKGDEI MVGEIAKRQV
ITNPNTISSI KRHMGEANYT VNVGGKKYTP QEISAMILAN LKKTAEDYLG AQVSEAVITV
PAYFNDAQRQ ATKDAGKIAG LNVKRIINEP TAAALSYGVD KGDKEQTILV FDLGGGTFDV
SILTLVDGTF EVLSTSGDNA LGGDDFDLRI VDFLVQEFKK ENSVDLSKDK MAMQRLKDAA
EKAKKELSGV TSSQISLPFL TMSEAGPLHL EYNMTRAKFN ELTKDLIDRC LAPVKRALGD
AKLDIEKIDQ VLLVGGSTRI PAVQDLVKNE LKKTPNKSIN PDEVVGIGAA IQGGILSGDV
KDILTLLDVT PLSLGIETLG NVFTKLIERN STIPTSEKQV FSTAADNLPA VDIHVLQGER
PLAADNKTLG RFQLTDRPPH RAEFLKLKIT FDLDANGIVS VKAKDLGTNK EQKITISGSG
ALKEEEIQRM IREAEENAEV DRVKKESIDA RNEAENMIFH TKKSLEDLKA DVTPEEKDKV
ETQIKELEEA LKGDDTALIK EKTASLTKES QGIAMKAYQK AQEKQAQEKG TQENTTAKNE
KPQDEVVDAD FEEKK