DNAK_LACLM
ID DNAK_LACLM Reviewed; 607 AA.
AC P0A3J1; A2RLI1; P42368; Q9CGY8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=llmg_1574;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8126443; DOI=10.1099/00221287-139-12-3253;
RA Eaton T.J., Shearman C.A., Gasson M.J.;
RT "Cloning and sequence analysis of the dnaK gene region of Lactococcus
RT lactis subsp. lactis.";
RL J. Gen. Microbiol. 139:3253-3263(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; X76642; CAA54089.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL98149.1; -; Genomic_DNA.
DR PIR; S39342; S39342.
DR RefSeq; WP_011835408.1; NZ_WJVF01000018.1.
DR AlphaFoldDB; P0A3J1; -.
DR SMR; P0A3J1; -.
DR STRING; 416870.llmg_1574; -.
DR EnsemblBacteria; CAL98149; CAL98149; llmg_1574.
DR KEGG; llm:llmg_1574; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR PhylomeDB; P0A3J1; -.
DR BioCyc; LLAC416870:LLMG_RS07930-MON; -.
DR Proteomes; UP000000364; 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 Stress response.
FT CHAIN 1..607
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078474"
FT REGION 577..607
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 607 AA; 64948 MW; 567FA7160313310E CRC64;
MSKIIGIDLG TTNSAVAVLE GTESKIIPNP EGNRTTPSVV AFKNGEIIVG DAAKRQAVTN
PETIISIKSK MGTSEKVSAN GKEYTPQEIS AMILQNLKAT AESYLGEKVE KAVITVPAYF
NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTDK DEKILVFDLG GGTFDVSILE
LGDGVFDVLA TAGNNKLGGD DFDQKIIDWM VAEFKKENGI DLGQDKMALQ RLKDAAEKAK
KDLSGVTTTQ ISLPFITAGA AGPLHLEMAL TRAKFDELTH DLVEATRQPV RQALSDAGLS
TSDIDEVLLV GGSTRIPAVV ELVRHETNKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVSVKAKD LGTQKEQTIV IKSNSGLSDE
EIDKMMKDAE ANADADAKRK EEVDTRNEAD ALVFQTEKTL KDLEGKVEEA EVKKAEDAKE
ELKKALEGED IDDIKAKSEA LSEIAQNLAV KLYEQANAAQ GEASEATDAQ EGPKDANTFD
GDFEESK