DNAK3_THEVB
ID DNAK3_THEVB Reviewed; 680 AA.
AC Q8DH10;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein dnaK3;
DE AltName: Full=HSP70-3;
DE AltName: Full=Heat shock 70 kDa protein 3;
DE AltName: Full=Heat shock protein 70-3;
GN Name=dnaK3; OrderedLocusNames=tll2150;
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; BAC09702.1; -; Genomic_DNA.
DR RefSeq; NP_682940.1; NC_004113.1.
DR AlphaFoldDB; Q8DH10; -.
DR SMR; Q8DH10; -.
DR STRING; 197221.22295877; -.
DR EnsemblBacteria; BAC09702; BAC09702; BAC09702.
DR KEGG; tel:tll2150; -.
DR PATRIC; fig|197221.4.peg.2252; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; PCQSVNP; -.
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; 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; 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..680
FT /note="Chaperone protein dnaK3"
FT /id="PRO_0000078562"
FT REGION 640..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 680 AA; 75980 MW; ACCE3E25E3142CF2 CRC64;
MRSRSNGMGK IVGIDLGTTN SVIAVLEGGK PVVIANAEGS RTTPSVVAFG KDGERLVGQL
ARRQAVLNPQ NTFYAVKRFI GREYSELTAE SKRVPYTIRR DESGKVRIKC PRLQREFAPE
EISAMVLRKL VEDASRYLGE PVTDAVITVP AYFNDSQRQA TRDAGRIAGL NVRRIINEPT
AAALAYGLDR QQEQTILVFD LGGGTFDVSI LEVGDGVFEV KATSGDTQLG GNDFDKLIVD
WLAEDFLAKE GIDLRRDRQS LQRLTDAAEK AKIELSGLLE TNIDLPFVTA TAEGPKHIET
TLSRRQFEDL SQGLLQRLRY PVEQALMDAH LTPSQIDAVV LVGGATRMPM VQDLVRQMIG
REPKQNVNPD EVVAVGAAIQ AGILAGDVKD ILLLDVTPLS LGVETIGGVT KVLIPRNTTI
PVRRSDIFST SENNQSQVEI HVVQGERELA AHNKSLGRFK LTGIPPAPRG VPQIQVSFDL
DANGLLQVVA LDRFSGREQS VVIQGASTLS EEEIQQMLLD AESNAAGDRQ RRARIEKRNR
SQDLINRAER QLREAAQEFG YQFAAEQRRG IEALVRQLQE AIRNEDDRQI DLTYAALEER
LYDFIRQLRL REEEAEDDEE VFKLPNLREA VNKGLDVVRG RERRRDDDED EWAEPPRTRR
SRSYSQRADS APWDDWDDDW