ID   DNAK_CLOPE              Reviewed;         619 AA.
AC   P26823;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=CPE2033;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1562596; DOI=10.1016/0167-4781(92)90529-9;
RA   Galley K.A., Singh B., Gupta R.S.;
RT   "Cloning of HSP70 (dnaK) gene from Clostridium perfringens using a general
RT   polymerase chain reaction based approach.";
RL   Biochim. Biophys. Acta 1130:203-208(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; X62915; CAA44698.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB81739.1; -; Genomic_DNA.
DR   PIR; S22355; S22355.
DR   RefSeq; WP_003454824.1; NC_003366.1.
DR   AlphaFoldDB; P26823; -.
DR   SMR; P26823; -.
DR   STRING; 195102.gene:10491303; -.
DR   GeneID; 69449969; -.
DR   KEGG; cpe:CPE2033; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   Proteomes; UP000000818; 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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..619
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078450"
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:0000250"
FT   CONFLICT        86..87
FT                   /note="YT -> LS (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="R -> T (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218..219
FT                   /note="AQ -> GE (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..239
FT                   /note="AAE -> GRQ (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="F -> L (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543
FT                   /note="Missing (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="E -> Q (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589..590
FT                   /note="NN -> II (in Ref. 1; CAA44698)"
FT                   /evidence="ECO:0000305"
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
//