DNAK_WOLWR
ID DNAK_WOLWR Reviewed; 640 AA.
AC C0R3W7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=WRi_008800;
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=66084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wRi;
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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; CP001391; ACN95609.1; -; Genomic_DNA.
DR RefSeq; WP_012673300.1; NZ_MKIF01000055.1.
DR AlphaFoldDB; C0R3W7; -.
DR SMR; C0R3W7; -.
DR STRING; 66084.WRi_008800; -.
DR PRIDE; C0R3W7; -.
DR EnsemblBacteria; ACN95609; ACN95609; WRi_008800.
DR KEGG; wri:WRi_008800; -.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001293; 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 Stress response.
FT CHAIN 1..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133172"
FT REGION 537..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..640
FT /note="Basic and 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 640 AA; 69391 MW; 0DC0273B0787AA0C CRC64;
MGRAIGIDLG TTNSCVAIMQ GKDTKVIENK EGARTTPSIV ALTSSGERLI GAPAKRQATT
NASNTFFATK RLIGRQYSDP EMKNLSVPYK VFAAKSGDAW VKTTDNKEYS PSQIGAFILQ
NMKEAAEAYL GEEVKDAVIT VPAYFNDSQR QATKDAGKIA GLNVLRIVNE PTAAALAYGL
DKKHGHTIVV YDLGGGTFDV SILEIGDGVF EVKATNGDTH LGGEDFDNGV VSYLLDEFKK
SNGIDLKNDP MAMQRIKEAA EKAKIELSSA METEINLPFI TADASGPKHL NMKLTRAKLE
SLVNDLIERT MAPCKKALED AGLSASQIGE VVLVGGMTRM PKVIEKVKEF FGKDPHRGVN
PDEVVAIGAA IQAGIIQGDV RDVLLLDVTP LSLGIETLGG VFTPLIERNT TIPTKKSQVF
STAEDNQTAV TIKVHQGERK LAVDNKLLGQ FSLEGIPPAP RGRPQIEVTF DIDANGIAHV
SAKDKATGKE QKIRIQSSGG LSDDEINRMV KEAEEKAQED EKRKKFIEVK NQADSLVHST
EKSLTEYGDK VSPEDRSAIE NAVNELKEVS KSDNIDDADS IQQKVTNLSQ LSMKLGEAMY
QASQQNSAEN GFSSEGNPND KEEKVVDSDY QDIDNKEENK