DNAK_CALBD
ID DNAK_CALBD Reviewed; 607 AA.
AC B9MJZ1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, 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=Athe_1551;
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS (Anaerocellum thermophilum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=521460;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001393; ACM60649.1; -; Genomic_DNA.
DR RefSeq; WP_015907996.1; NC_012034.1.
DR AlphaFoldDB; B9MJZ1; -.
DR SMR; B9MJZ1; -.
DR STRING; 521460.Athe_1551; -.
DR EnsemblBacteria; ACM60649; ACM60649; Athe_1551.
DR GeneID; 31772904; -.
DR KEGG; ate:Athe_1551; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000007723; 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 Stress response.
FT CHAIN 1..607
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133126"
FT REGION 577..607
FT /note="Disordered"
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 607 AA; 66547 MW; DA89A4EF2914AED4 CRC64;
MAHILGIDLG TTNSCMAVIE GGQPVVIPNA EGFRTTPSVV AFTKTGERLV GHAAKRQAIT
NPERTIISIK RDMGTNKRIK IDDKEYSPEE ISAMILMKLK ADAEAYLGEK ITQAVITVPA
YFTDSQRQAT KNAGRIAGLE VLRIINEPTA AALAYGLDKE GHQKIMVYDL GGGTFDVSIL
EIGDGVIEVL ATSGNNRLGG DDFDQRIIDY IADEFMKEHG IDLRQDKVAL QRLKDAAERA
KIELSSALQT TINLPFITAD ANGPKHIDMV LTRAKFEELI KDLVEKTREP VETALSDAKL
TPEQIDKVIL VGGSTRIPYV QEFVKKLTGK EPFKGINPDE CVAIGAAIQA GVLAGQVKDI
LLLDVTPLSL GIETLGGVFT KIIERNTTIP TRKSQIFTTA VDGQTQVEIH VLQGERPLAK
DNKTLGRFIL DGIPPAPRGV PQIEVTFDID ANGIVHVSAK DLGTGREQKI TITSQTHLSE
EEIQRAIKEA EMYAEQDRKR KELIEARNRA DSIIYQTEKL LRELGDKMTE TEKQQIESKL
KALKDVMNGE DKEQIERAID ELTKSFYDVS TRLYQQGYTA SGPQGGPNPG GGQSGPDGNV
NTDYKVY