DNAK_SYMTH
ID DNAK_SYMTH Reviewed; 612 AA.
AC Q67S54;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=STH504;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(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}.
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DR EMBL; AP006840; BAD39489.1; -; Genomic_DNA.
DR RefSeq; WP_011194638.1; NC_006177.1.
DR AlphaFoldDB; Q67S54; -.
DR SMR; Q67S54; -.
DR STRING; 292459.STH504; -.
DR PRIDE; Q67S54; -.
DR EnsemblBacteria; BAD39489; BAD39489; STH504.
DR KEGG; sth:STH504; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000417; 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..612
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226018"
FT REGION 579..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 612 AA; 65740 MW; B353A99FCAAA9599 CRC64;
MAKVIGIDLG TTNSVVAVMD GSEPTVLENR EGDRTTPSVV AFTKTGERLV GKVAKRQAIT
NPDRTIISIK RHMGSDYKVR IDDKAYTPQE ISAMILSKLK ADAEEKLGEK ITQAVITVPA
YFTDAQRQAT KDAGTIAGLE VLRIINEPTA AALAYGLDKG EDQRILVFDL GGGTFDVSIL
ELGGGTFQVI ATAGNNKLGG DDFDERIVNY LADRFQREHG IDLRKDKQAL QRLREAAEKA
KIELSSVTTT NINLPFISMT ADGPVHMDET LTRAKFEELT ADLVEATMGP TRQALQDAGL
EPGEIDKVLL VGGSTRIPAV QEAVRRFFGK EPYKGINPDE VVAMGAAIQA AVIKGDVKDV
LLLDVTPLSL GIETLGGVFT KLIERNTTIP TRKSQIFSTA ADGQTQVEIH VLQGEREMAA
YNKTLGRFIL DGIPPAPRGV PKIEVTFDID VNGIVHVSAK DLGTGKEQKI TIQSQTSMSK
EEIERAIKEA EAMAAEDKKR REEAEIRNNA DAAVYNAEKL IKESEGKGID PSLIDAVKGA
IEPVKEALKG TDVNAVKQAT EKLTEAVYKL SSAIYEKTGS AGTGAGSQAG SAAGSGDGQS
MDAEFKVKDE DK