DNAK_LATSS
ID DNAK_LATSS Reviewed; 613 AA.
AC Q38W93;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=LCA_1236;
OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS subsp. sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=314315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23K;
RX PubMed=16273110; DOI=10.1038/nbt1160;
RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA Zagorec M.;
RT "The complete genome sequence of the meat-borne lactic acid bacterium
RT Lactobacillus sakei 23K.";
RL Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI55540.1; -; Genomic_DNA.
DR RefSeq; WP_011374933.1; NC_007576.1.
DR AlphaFoldDB; Q38W93; -.
DR SMR; Q38W93; -.
DR STRING; 314315.LCA_1236; -.
DR EnsemblBacteria; CAI55540; CAI55540; LCA_1236.
DR KEGG; lsa:LCA_1236; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; LSAK314315:LCA_RS06150-MON; -.
DR Proteomes; UP000002707; 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; 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.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..613
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225972"
FT REGION 577..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 613 AA; 66290 MW; 9D920D1E612C0627 CRC64;
MSKVIGIDLG TTNSAVAVLE GGQPKIITNP EGARTTPSVV SFKNGEIQVG EVAKRQAITN
PDTIASIKRH IGEAGYKVTV GDKSYTPQEV SAMILQYIKK FAEDYLGEEV TEAVITVPAY
FNDSQRQATK DAGKIAGLDV KRIINEPTAS ALAYGLDKTE TDEKVLVYDL GGGTFDVSVL
ELGDGVFQVL STNGDTRLGG DDFDEAIMNW LVENFKSDNG IDLSKDKMAM QRLKDAAEKA
KKDLSGVTST QISLPFISAG ENGPLHLEMT LSRTEFDRLT SDLVDRTKAP VMNALKDAGL
DANEIDKVIL NGGSTRIPAV QEAVKNWTGK EPDHSINPDE AVALGAAVQG GVISGDVKDV
VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKAQTFSTA ADNQPAVDIH VLQGERPMAA
DNKTLGRFQL TDIPAAPRGV PQIEVKFDID KNGIVNVSAK DLGTNKEQKI TIKSNSGLSD
EEIDRMMKEA QENEEADTKR KEEVDLKNDV DQLIFQTDKT LKELEGKVSD EELQKAKDAK
EELVKAQQEN NLEDMKTKRD ALSEIVQELT VKLYQQAQEA QQAAGGAEGN ATDAKTDDGT
VDGDFEEVKD DKE