DNAK_LACH4
ID DNAK_LACH4 Reviewed; 608 AA.
AC A8YVQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=lhv_1336;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX27340.1; -; Genomic_DNA.
DR RefSeq; WP_012211996.1; NC_010080.1.
DR AlphaFoldDB; A8YVQ3; -.
DR SMR; A8YVQ3; -.
DR STRING; 405566.lhv_1336; -.
DR EnsemblBacteria; ABX27340; ABX27340; lhv_1336.
DR KEGG; lhe:lhv_1336; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000790; 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..608
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000072036"
FT REGION 577..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Polar residues"
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 608 AA; 65701 MW; 3E0DC94D4E3CE4F2 CRC64;
MSKVIGIDLG TTNSAVAVLE GKEPKIITNP EGNRTTPSVV AFKDGEIQIG EVAKRQAITN
PNTIVSIKRH MGEADYKVKV GDKEYTPQEI SAFILQYIKK FSEDYLGEKV TDAVITVPAY
FNDAQRQATK DAGKIAGLNV QRIINEPTAS ALAFGLNKDQ DEKVLVYDLG GGTFDVSVLQ
LGDGVFQVLS TNGDTHLGGD DFDNRIMDWL IKNFKDENGV DLSKDKMAMQ RLKDAAEKAK
KDLSGVSSTH ISLPFISAGE AGPLHLEADL TRAKFDELTS DLVEKTKVPF DNALKDAGLT
VNDIDKVILN GGSTRIPAVQ KAVKEWAGKE PDHSINPDEA VALGAAIQGG VISGDVKDIV
LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQIFSTAA DNQPAVDIHV LQGERPMAAD
DKTLGRFELT DIPPAPRGVP QIQVTFDIDK NGIVNVSAKD MGTGKEQKIT IKSSSGLSDE
EIKRMQKDAE EHAEEDKKRK EEVDLRNEVD QLIFTTDKTL KDTKDKLSDS DRKPVEDALE
ALKKAQKDNN LDEMKEKKDA LSKAAQDLAV KLYQQNGGAQ GAAGQAGPQG GNNGGAQDGE
FHKVDPNK