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DNAK_CLOP1
ID   DNAK_CLOP1              Reviewed;         619 AA.
AC   Q0TNS7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CPF_2290;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000246; ABG85010.1; -; Genomic_DNA.
DR   RefSeq; WP_003454824.1; NC_008261.1.
DR   AlphaFoldDB; Q0TNS7; -.
DR   SMR; Q0TNS7; -.
DR   STRING; 195103.CPF_2290; -.
DR   EnsemblBacteria; ABG85010; ABG85010; CPF_2290.
DR   GeneID; 29570603; -.
DR   KEGG; cpf:CPF_2290; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001823; 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..619
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059544"
FT   REGION          578..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   619 AA;  66482 MW;  88990A19444079BE CRC64;
     MSKIIGIDLG TTNSCVAVME GGEPVVITNS EGARTTPSVV SFQANGERLV GQVAKRQAIT
     NPDKTIMSIK RHMGTDYKVN IDGKDYTPQE ISAMILQKLK ADAEAYLGEK VTEAVITVPA
     YFNDAERQAT KDAGRIAGLD VKRIINEPTA ASLAYGLDKM DSAHKILVYD LGGGTFDVSI
     LDLGDGVFEV VSTNGDARLG GDDFDQRIID YIAEDFKAQN GIDLRQDKMA LQRLKEAAEK
     AKIELSSSTQ TLINLPFITA DATGPKHIDM TLTRAKFNEL THDLVERTIN IMKEALKSGN
     VSLNDIDKVI LVGGSTRIPA VQEAVKNFTG KEPSKGVNPD ECVAMGAAIQ AGVLTGDVKD
     VLLLDVTPLT LGIETLGGVA TPLIERNTTI PARKSQIFST AADNQTSVEI HVVQGERQMA
     ADNKTLGRFT LSGIAPAPRG IPQIEVAFDI DANGIVKVSA TDKATGKEAN ITITASTNLS
     DAEIDKAVKE AEQFAEEDKK RKEAIEVKNN AEQTVYQTEK TLNELGDKVS AEEKSEIEAK
     IEEVKKVKDG DDIEAIKKAM EDLTQAFYKV SEKLYQQNGG AQGQGFDPNN MGGANAGAGA
     TNNNDDNVVD ADFEVQDDK
 
 
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