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Database: UniProt
Entry: DNAK_CLOAB
LinkDB: DNAK_CLOAB
Original site: DNAK_CLOAB 
ID   DNAK_CLOAB              Reviewed;         615 AA.
AC   P30721;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
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=CA_C1282;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4259 / DSM 1731 / NCIB 619;
RX   PubMed=1577695; DOI=10.1128/jb.174.10.3290-3299.1992;
RA   Narberhaus F., Giebeler K., Bahl H.;
RT   "Molecular characterization of the dnaK gene region of Clostridium
RT   acetobutylicum, including grpE, dnaJ, and a new heat shock gene.";
RL   J. Bacteriol. 174:3290-3299(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M74569; AAA23246.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK79253.1; -; Genomic_DNA.
DR   PIR; B41873; B41873.
DR   PIR; B97058; B97058.
DR   RefSeq; NP_347913.1; NC_003030.1.
DR   RefSeq; WP_010964594.1; NC_003030.1.
DR   AlphaFoldDB; P30721; -.
DR   SMR; P30721; -.
DR   STRING; 272562.CA_C1282; -.
DR   GeneID; 44997788; -.
DR   KEGG; cac:CA_C1282; -.
DR   PATRIC; fig|272562.8.peg.1483; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000000814; 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; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078448"
FT   REGION          578..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   615 AA;  65649 MW;  3D014929157F7567 CRC64;
     MSKVIGIDLG TTNSCVAVME GGDPAVIANS EGARTTPSVV SFQKNGERLV GQVAKRQSIT
     NPDKTIISIK RKMGTAEKVA IDDKNYTPQE ISAMILQKLK ADAEAYLGET VTQAVITVPA
     YFNDSQRQAT KDAGKIAGLE VLRIINEPTA ASLAYGLDKM DTNQKILVYD LGGGTFDVSV
     LELGDGVFEV KSTNGNTHLG GDDFDEKIMD YIAEEFKKDN GIDLRNDKMA LQRLKEAAEK
     AKIELSSSTQ TNINLPFITA DATGPKHIDM NLTRAKFNEL TEGLVQDTIE PMKKALSDAG
     LSINDIDKIV LVGGSTRIPA VQEAVKNYTG KDPSKGVNPD ECVAIGAAIQ AGVLTGDVKD
     VLLLDVSPLT LGIETLGGVA TPLIERNTTI PTRKSQVFST AADNQPSVEI NIVQGERKMA
     ADNKSLGRFT LDGIAPAPRG VPQIEVTFDI DANGIVNVSA KDKGTGKESH ITITASTNLS
     DEEIDKAVKD AEKFAEEDKK KKENIEVKNN ADQIVFQTDK ALKDLGDKVS AEDKSNIEAK
     KEALSKVKDG DDIEAIKKAT EDLTQALYAI TTKMYEQSGA QGAPGADPNA GASQKTNGGA
     DDNVVDADFK VDNDK
//
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