DNAK2_NOSS1
ID DNAK2_NOSS1 Reviewed; 633 AA.
AC Q8YW74;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=alr1742;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB73441.1; -; Genomic_DNA.
DR PIR; AH2023; AH2023.
DR RefSeq; WP_010995910.1; NZ_RSCN01000019.1.
DR AlphaFoldDB; Q8YW74; -.
DR SMR; Q8YW74; -.
DR STRING; 103690.17130832; -.
DR EnsemblBacteria; BAB73441; BAB73441; BAB73441.
DR KEGG; ana:alr1742; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; AYTKNQD; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002483; 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; 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..633
FT /note="Chaperone protein dnaK2"
FT /id="PRO_0000078408"
FT REGION 513..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 633 AA; 67908 MW; EC2BBE8662690BA7 CRC64;
MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AFAKNGDTLV GQIAKRQAVM
NPENTFYSVK RFIGRRYDEV TNEATEVSYK VLSSGGNVKV DSPGAGKQFA PEEISAKVLR
KLVEDASKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GIEVMRIINE PTAASLAYGF
DKKSNETILV FDLGGGTFDV SVLEVGDGVF EVLATSGDTH LGGDDFDKKI VDFLAEQFRK
DEGIDLRKDK QALQRLTEAA EKAKIELSSV TQAEINLPFI TATQDGPKHL DMTLTRAKFE
ELCADLIDRC RIPVEQALRD AKLKKENIDE VVLVGGSTRI PAVQQLVKNL LGREPNQTVN
PDEVVAVGAA IQAGVLGGEV TGILLLDVTP LSLGVETLGG VMTKIIPRNT TIPTKKSEVF
STAVDGQTNV EIHVLQGERE FANDNKSLGT FRLDGIPPAP RGVPQIEVVF DIDANGILNV
TAKDKGTGKE QSISITGAST LDKTDIDRMV REAEQNASSD KERREKIERK NQADSLAYQA
EKQLQELGDK VPEADKTKVE GLVKDLREAV AKEDDEQIKK LTPELQQALF AVGSNIYQQA
GGGAAPGAAP QDGGTTSSDG GDDVIDADFT ETK