DNAK_VESOH
ID DNAK_VESOH Reviewed; 634 AA.
AC A5CX56;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=COSY_0346;
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA;
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(2007).
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; AP009247; BAF61471.1; -; Genomic_DNA.
DR RefSeq; WP_011929741.1; NC_009465.1.
DR AlphaFoldDB; A5CX56; -.
DR SMR; A5CX56; -.
DR STRING; 412965.COSY_0346; -.
DR EnsemblBacteria; BAF61471; BAF61471; COSY_0346.
DR KEGG; vok:COSY_0346; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000247; 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; 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..634
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059696"
FT REGION 604..634
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 634 AA; 68733 MW; 3D259FD1BE7D1100 CRC64;
MSKIIGIDLG TTNSCVAIMD GGSVKIIENS EGDRTTPSII AYPKDSEEVL VGQAAKRQAV
TNPENTLYAI KRLIGRRFEE DAVQKDIDLV PYKIVKADNG DAWVKVKNKK MAAPEISAKV
IGKMKKTAED YLGEEVTEAV ITVPAYFNDS QRQATKDAGK IAGLNVKRII NEPTAAALAY
GVDKVKGDKT VVVYDLGGGT FDVSIIEMED IDGEKHFEVL STNGDTFLGG EDFDQRMIGY
LVDEFKKDQG VDLTNDPMAL QRLKEAAEKA KIELSSSEQT EVNLPYVTAD ASGPKHLNIK
ITRAKLESLV EDLLKRTIEP CKTALKDADL STGDIDEVIL VGGQTRMPKV TKMVQNFFDK
EPKKDVNPDE AVAMGAAIQA GVLGGDVKDV LLLDVTPLSL GIETMGGVMT KLIEKNTTIP
TNASQIFSTA ADNQSAVTVH VLQGEREISS ANKSLGQFNL EGINSAPKGQ PQIEVTLDID
SDGILNVSAK DKNTGKKQSI TIKASSGLSD EEVEKMVKDA EAHADEDQKF QKLVTSKNMA
DALIHSTKQT LDELKDEISI DEKSVIEASI TDLEKVIKSD NKEAIDTKVK TLSEKAQLLA
EKAQAKAGVK NTPQEEKNSD DVVDADFEEV KDDK