DNAK_TRIV2
ID DNAK_TRIV2 Reviewed; 688 AA.
AC O05714; Q3MEP3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=Ava_0919;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pohl B., Masepohl B., Spieker R.L., Boehme H.;
RT "Nucleotide sequence of the dnaK-gene from the heterocyst-forming
RT cyanobacterium Anabaena variabilis ATCC 29413.";
RL (er) Plant Gene Register PGR97-097(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; Y13044; CAA73479.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA20543.1; -; Genomic_DNA.
DR AlphaFoldDB; O05714; -.
DR SMR; O05714; -.
DR STRING; 240292.Ava_0919; -.
DR PRIDE; O05714; -.
DR EnsemblBacteria; ABA20543; ABA20543; Ava_0919.
DR KEGG; ava:Ava_0919; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_0_3; -.
DR OMA; PCQSVNP; -.
DR Proteomes; UP000002533; 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; 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 Stress response.
FT CHAIN 1..688
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078410"
FT REGION 630..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 688 AA; 76719 MW; 2CE3C6A0D6C4A425 CRC64;
MGKVVGIDLG TTNSVVAVME GGKPVVIANA EGMRTTPSVV GFSKDGERVV GQMARRQTVL
NPQNTFFAVK RYIGRRYNEL SPESKRVPYT IRKDDVGNIK VACPRLNKEF AAEEISAMVL
KKLADDASAY LGAAVTGAVI TVPAYFNDSQ RQATRDAGRI AGLEVLRILN EPTAASLAYG
LDRGDTETIL VFDLGGGTFD VSILEVGDGV FEVKATSGDT QLGGNDFDKK IVDWLAEQFL
ETEGVDLRRD RQALQRLMEA AEKAKIELSA VSITDINLPF ITATEDGPKH LETRLTRSQF
EGLCADLLGR VRNPVKRALK DAGLRPDDIE EVVLVGGSTR MPMVKQLVRD LIGIEPSENV
NPDEVVAMGA AIQAGILAGE FKDVLLLDVT PLSLGLEAIG GVMKKLIPRN TTIPVRRSDI
FSTSENNQNS VEIHVVQGER EMAGDNKSLG RFKLYGIPPA PRGIPQIQVA FDIDANGILQ
VTALDRTTGR EQSITIQGAS TLSESEVNRM IQEAQKYADV DRERKERVEK RTRSEALILQ
GERQLREVAL EFGMQFARNR RQRIDNISRE LKESLKENDD RGIDQAYADL QDALYELNRE
VRQYYAEDED DDLFATIKDI FVGDKDKERD LPRDSYRERD SYNNRDYGRD YGRDYGRDSR
PSYDSNRPPR KSPRPSYQDN WDDDDDWL