DNAK_ALIB4
ID DNAK_ALIB4 Reviewed; 628 AA.
AC A8EWT6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Abu_2195;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV68409.1; -; Genomic_DNA.
DR RefSeq; WP_004511080.1; NC_009850.1.
DR AlphaFoldDB; A8EWT6; -.
DR SMR; A8EWT6; -.
DR STRING; 367737.Abu_2195; -.
DR EnsemblBacteria; ABV68409; ABV68409; Abu_2195.
DR GeneID; 56464320; -.
DR KEGG; abu:Abu_2195; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001136; 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; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..628
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059505"
FT REGION 595..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 628 AA; 67497 MW; CEA1DE3D0BB169A1 CRC64;
MSKVIGIDLG TTNSCVAVYE NGEAKIIPNK EGKNTTPSIV AYTDKGEVLV GDPAKRQAIT
NPEKTIYSIK RIMGLMMNEP NAKEAQSKVG YKIVDRNGAA AVEIAGKVYT PQEISAKILG
KLKADAEEYL GDKVTDAVIT VPAYFNDAQR KATQEAGTIA GLNVLRIINE PTAASLAYGL
DKKGEEKVLV YDLGGGTFDV TVLEIGDGTF EVLSTDGNAF LGGDDFDNAI IDWLAKEFKD
ENGFDIKNDK MALQRLKDAA ENAKKELSSA ESTEINLPFI SMGNAGPIHL VKSLTRAKFE
SMTEKLIDET LDHIKIALKE AGLSKGDIDE IIMVGGSTRL PKANQVVKEF FGKDLNKGVN
PDEVVAAGAA VQAGVLRGDV KDVLLLDVTP LSLGIETLGG VMTKLIDKGT TIPVKKSQVF
STADDNQPAV SIHVCQGERE FAKDNKSLGM FELSDIPAAP RGVPQIEVTF DIDANGVLNV
SAKDKGTGKE NKITISGSSG LSDAEIEKMV AEAEANKEAD AKKKAVIEVR NQADALLHST
RKTLEENENA ISEDEKKAII DAAADLEETL KDENATKEQI EEKLKTLTDK SHKLAEAMYK
KEQGEQAGAQ PNQKAKKDDD DVIDAEVE