DNAK2_THEVB
ID DNAK2_THEVB Reviewed; 640 AA.
AC Q8DI58;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Chaperone protein dnaK2;
DE AltName: Full=HSP70-2;
DE AltName: Full=Heat shock 70 kDa protein 2;
DE AltName: Full=Heat shock protein 70-2;
GN Name=dnaK2; OrderedLocusNames=tlr1733;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC09285.1; -; Genomic_DNA.
DR RefSeq; NP_682523.1; NC_004113.1.
DR RefSeq; WP_011057570.1; NC_004113.1.
DR AlphaFoldDB; Q8DI58; -.
DR SMR; Q8DI58; -.
DR STRING; 197221.22295459; -.
DR PRIDE; Q8DI58; -.
DR EnsemblBacteria; BAC09285; BAC09285; BAC09285.
DR KEGG; tel:tlr1733; -.
DR PATRIC; fig|197221.4.peg.1814; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; AYTKNQD; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000440; 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; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 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..640
FT /note="Chaperone protein dnaK2"
FT /id="PRO_0000078561"
FT REGION 605..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 640 AA; 68927 MW; 9109BC3523AABEAC CRC64;
MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNGDRLV GQIAKRQAVM
NPENTFYSVK RFIGRRFDEV THEATEVSYK VLNVNGNVKL DCPALGKQFA PEEISAQVLR
KLKEDASKYL GEEVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAASLAYGL
DKKANETILV FDLGGGTFDV SILEVGDGVF EVLATSGDTH LGGDDFDKKI VDYLAESFRA
QEGIDLRKDR QALQRLTEAA EKAKIELSSV MQTEINLPFI TATQDGPKHL DMTLTRAKFE
ELCSDLIDRC RVPVEQALKD AKLSKDQIDE VVLVGGSTRI PAIQELVKRL LGKDPNQSVN
PDEVVAVGAA IQAGVLAGEV KDILLLDVTP LSLGVETLGG VMTKIIPRNT TIPTKKSEVF
STAVDGQTNV EIHVLQGERE MAADNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILNV
TARDKGTGKQ QSISITGAST LPKEEVERMV REAEMNAAAD KAKREKIETK NQAEQLCYQA
EKQLNELGDK VSTSDKDRLT SLIANLRSEI GTEAEKKPID AIDFGRVKSL MQDLQQALYS
VGSSVYQSAQ SSDGTGSSSS GGSGSGGDDE VIDAEFSETK