DNAK_CLOPE
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 03-AUG-2022, entry version 139.
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; Firmicutes; 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 EnsemblBacteria; BAB81739; BAB81739; BAB81739.
DR GeneID; 29570603; -.
DR KEGG; cpe:CPE2033; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
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 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..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