DNAK_THEM4
ID DNAK_THEM4 Reviewed; 596 AA.
AC A6LM32;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Tmel_1128;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000716; ABR30983.1; -; Genomic_DNA.
DR RefSeq; WP_012057342.1; NC_009616.1.
DR AlphaFoldDB; A6LM32; -.
DR SMR; A6LM32; -.
DR STRING; 391009.Tmel_1128; -.
DR PRIDE; A6LM32; -.
DR EnsemblBacteria; ABR30983; ABR30983; Tmel_1128.
DR KEGG; tme:Tmel_1128; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_0; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001110; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..596
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059691"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 596 AA; 66239 MW; 046AA84372D5E4EB CRC64;
MSSKKEYVVG IDLGTTNSVI AWMKPDSSVE VIPNAEGART TPSIVAFSKS GEILVGEPAK
RQLILNSDRT IKSIKRKMGT DYKVKIDDKE YSPQEISAFI LKKLKKDAEE YLGGEIKRAV
ITCPAYFNDA QRQATKEAGI IAGFDVLRII NEPTAAALAY GLDRKGKEEK VLVYDLGGGT
FDVSILEIGD GVIQVIATSG NNHLGGDDFD QRIIDWLAEE FKKQHGVDLK EDKQALQRLR
DAAEKAKIEL SSKLETDISL PYITATAEGP LHLEMRLTRS MFESLTRDLV EMTRKPIEQA
LSDAKLKPED IDEIILVGGM TRVPMIQNFI KEIFGKEPNK RVNPDEAVAM GAAIQAAILA
GEEGAQGKDI VLVDVTPLTL GIEVKGGLFE PIIPRNSTIP IKKSKVFTTA EDGQTEVEIR
VFQGERPIAA DNILLGSFRL VGIPPAPRGV PQIEVTFDID SDGIVHVSAK DLGTGKEQTM
VVSGRHKLSE EDINKIIEDA KKYEEQDKRR KEEVELKNKA DDLAYYIDKS LKEYGDKIPQ
DEKQKLETLV NDLRDAINKN DIARIKMLFD ELEREKTKIG EYIYKQNQGN QQAENQ
