DNAK_LISW6
ID DNAK_LISW6 Reviewed; 613 AA.
AC A0AIS4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=lwe1488;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(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; AM263198; CAK20906.1; -; Genomic_DNA.
DR RefSeq; WP_011702279.1; NC_008555.1.
DR AlphaFoldDB; A0AIS4; -.
DR SMR; A0AIS4; -.
DR STRING; 386043.lwe1488; -.
DR EnsemblBacteria; CAK20906; CAK20906; lwe1488.
DR GeneID; 61189364; -.
DR KEGG; lwe:lwe1488; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000779; 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; 2.
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..613
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059594"
FT REGION 577..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 66152 MW; 2C8968481DD7C236 CRC64;
MSKIIGIDLG TTNSAVAVLE GGEAKIIPNP EGARTTPSVV GFKNGERQVG EVAKRAAITN
PNTISSIKRY MGTNHKETIE GKDYSPQEIS AIILQYLKSY AEDYLGETVD KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGMDKTET DQTILVFDLG GGTFDVSILE
LGDGVFEVHS TAGDNELGGD DFDKKIIDYL VAEFKKDNGV DLSQDKMALQ RLKDAAEKAK
KDLSGVTSTQ ISLPFITAGE AGPLHLEVTL TRAKFDELTH DLVERTIAPT RQALKDANLS
ASDIDQVILV GGSTRIPAVQ ETIKKELGKE PHKGVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVMTP LIERNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAKD
NKTLGRFQLA DIPPAPRGIP QIEVLFDIDK NGIVTVRAKD LGTGKEQNIV IKSSSGLTDE
EIEKMVQDAE ANAEEDKKNK ENAELRNNAD QLVFTVDKTL KELEGKIDEE EVKKAEAARD
ELQEALKGED FDAIKEKTES LNEIVQNLSV KLYEQAAAEQ QAAGGAEGQE APQNDDVVDA
EFEEVNDDDK ENK