DNAK_LISMF
ID DNAK_LISMF Reviewed; 613 AA.
AC Q71ZJ7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
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};
GN OrderedLocusNames=LMOf2365_1492;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT04267.1; -; Genomic_DNA.
DR RefSeq; WP_003726023.1; NC_002973.6.
DR AlphaFoldDB; Q71ZJ7; -.
DR SMR; Q71ZJ7; -.
DR KEGG; lmf:LMOf2365_1492; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
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_0000078483"
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:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 66158 MW; 66F429D2DA6CF662 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
ELQEALKGED FEAIKEKTES LNEIVQNLSV KLYEQAAAEQ QAAGGAEGQE APQNDDVVDA
EFEEVNDDDK ENK