DNAK_LACP7
ID DNAK_LACP7 Reviewed; 620 AA.
AC A9KKU0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Cphy_2311;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) 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; CP000885; ABX42672.1; -; Genomic_DNA.
DR RefSeq; WP_012200326.1; NC_010001.1.
DR AlphaFoldDB; A9KKU0; -.
DR SMR; A9KKU0; -.
DR STRING; 357809.Cphy_2311; -.
DR PRIDE; A9KKU0; -.
DR EnsemblBacteria; ABX42672; ABX42672; Cphy_2311.
DR KEGG; cpy:Cphy_2311; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000370; 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; 2.
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..620
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079221"
FT REGION 590..620
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 620 AA; 66127 MW; 63B591497FF51E91 CRC64;
MGKIIGIDLG TTNSCVAVME GGKPVVIANT EGSRTTPSVV AFTKTGERIV GEPAKRQAVT
NADKTISSIK RHMGTDFRVS IDDKKFTPQE ISAMVLQKLK ADAEGYLGEK ISEAVITVPA
YFNDAQRQAT KDAGKIAGLD VKRIINEPTA AALAYGLDNE HEQKIMVYDL GGGTFDVSII
EIGDGVIEVL ATSGDNRLGG DDFDERVTRY FIDEFKKAEG VDLSTDKMAL QRLREAAEKA
KKELSSATTT NINLPFITAT SEGPKHFDLN LTRAKFDELT HDLVERTAIP VQNALRDAGL
APSELGKVLL VGGSTRIPAV QDKVKQLTGH EPSKSLNPDE CVAIGASVQG GKLAGDTGAG
DILLLDVTPL SLSIETMGGI ATRLIERNTT IPSKKSQIFS TAADNQTAVD INVVQGERQF
AKDNKSLGQF RLDGIPPARR GIPQIEVTFD IDANGIVNVS AKDLGTGKEQ HITITAGSNM
SDSDIDKAVR EAAEYEAQDK KRKDAVDTRN DADSIVFQTE KALSEVGDKV SADEKTAVEA
DLNHLKDLVA KANPEVMSEG EVEDMKAAKE KLMNSAQALF AKLYESAQGA AGAGPDMSGA
GPQGDTYAGD DVVDGDYREV