DNAK_LISIN
ID DNAK_LISIN Reviewed; 613 AA.
AC Q92BN8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
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=lin1510;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596168; CAC96741.1; -; Genomic_DNA.
DR PIR; AE1621; AE1621.
DR RefSeq; WP_010991568.1; NC_003212.1.
DR AlphaFoldDB; Q92BN8; -.
DR SMR; Q92BN8; -.
DR STRING; 272626.lin1510; -.
DR EnsemblBacteria; CAC96741; CAC96741; CAC96741.
DR KEGG; lin:dnaK; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002513; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..613
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078482"
FT REGION 578..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 613 AA; 66129 MW; C9A4963C3A6DF6AE CRC64;
MSKIIGIDLG TTNSAVAVLE GGEAKIIPNP EGARTTPSVV GFKNGERQVG EVAKRAAITN
PNTISSIKRH MGTNYKETIE GKDYSPQEIS AIILQYLKSY AEDYLGETVD KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGMDKTET DQTILVFDLG GGTFDVSILE
LGDGVFEVHS TAGDNELGGD DFDKKIIDYL VAEFKKDNGI DLSQDKMALQ RLKDAAEKAK
KDLSGVTSTQ ISLPFITAGE AGPLHLEVTL TRAKFDELTH DLVERTIAPT RQALKDANLS
ASDIDQVILV GGSTRIPAVQ ETIKKELGKE PHKGVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVMTT LIERNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAKD
NKTLGRFQLA DIPPAPRGIP QIEVSFDIDK NGIVTVRAKD LGTGKEQNIV IKSSSGLTDE
EIEKMVQDAE ANAEEDKKNK ENAELRNNAD QLVFTVDKTL KELEGKVEEE EVKKAEAARD
ELQEALKGEN FDAIKEKTDS LNEIVQNLSV KLYEQAAAEQ QAAGGAEGQE APQNDDVVDA
EFEEVNDDDK ENK