DNAK_TREPS
ID DNAK_TREPS Reviewed; 635 AA.
AC B2S2G4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=TPASS_0216;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD70643.1; -; Genomic_DNA.
DR RefSeq; WP_010881664.1; NC_021508.1.
DR AlphaFoldDB; B2S2G4; -.
DR SMR; B2S2G4; -.
DR EnsemblBacteria; ACD70643; ACD70643; TPASS_0216.
DR GeneID; 57878754; -.
DR KEGG; tpp:TPASS_0216; -.
DR PATRIC; fig|455434.6.peg.220; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001202; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119771"
FT REGION 601..635
FT /note="Disordered"
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 635 AA; 68042 MW; 11244A863A4504CD CRC64;
MGKIIGIDLG TTNSCVAIME GGEPVVIQNA EGGRTTPSII GFTSDGGRVV GQPAKNQMVT
NPEHTIYSIK RFIGSRFNEL TGEAKKVPYK IVPQGDDVRV EVEGKLYSTQ EISAFILQKM
KKTAEDYLGE AVTEAVITVP AYFNDAQRQA TKDAGKIAGL DVKRIINEPT AASLAFGFNK
DSKREKIIAV YDLGGGTFDI SILELGDGVF EVKSTNGDTH LGGDDFDARI VQWLEQGFKS
DTGIDLGNDR MALQRLREAA EKAKIALSSS ASTEINLPFI TADANGPKHL QRTLSRSEFE
KMTDDLFERT KEPCRKALKD AGISADRIDE ILLVGGSTRM PKVAHVIKDV FGKEGSKGVN
PDEAVAIGAA IQGGILGGDV KDVLLLDVTP LSLGIETMGG VFTPLISRNT TIPTRKSQVF
STAADGQTAV SIHVLQGERG MANQNRTLGN FDLVGIPPAP RGVPQIEVTF DIDANGIVHV
SAKDLGTGKE QHIRIESSSG LSESEIDRMV KEAEANAESD KREREKIEAR NVADSLIYQT
EKTLKEAGDG VNAADRARID EAIAELKTVL SGDDVASIKA KTEILQQASY KIAEEMYKRQ
AAAGAAAGKK SDAPSGNEAE GGDVDYEVVK DEDSK
