DNAK2_SYNP6
ID DNAK2_SYNP6 Reviewed; 634 AA.
AC Q5N1J4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chaperone protein DnaK 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK2 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=syc1636_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD79826.1; -; Genomic_DNA.
DR RefSeq; WP_011243946.1; NC_006576.1.
DR AlphaFoldDB; Q5N1J4; -.
DR SMR; Q5N1J4; -.
DR STRING; 269084.syc1636_c; -.
DR EnsemblBacteria; BAD79826; BAD79826; syc1636_c.
DR KEGG; syc:syc1636_c; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; AYTKNQD; -.
DR Proteomes; UP000001175; 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 Stress response.
FT CHAIN 1..634
FT /note="Chaperone protein DnaK 2"
FT /id="PRO_0000226019"
FT REGION 600..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 634 AA; 67776 MW; FD2F1A68901E03B7 CRC64;
MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AFAKNQDRLV GQIAKRQAVM
NPENTFYSVK RFIGRRPDEV TNELTEVAYK VDTSGNAVKL DSSNAGKQFA PEEISAQVLR
KLAEDASKYL GETVTQAVIP VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLATSGDTH LGGDDFDKKI VDFLAGEFQK
NEGIDLRKDK QALQRLTEAA EKAKIELSSA TQTEINLPFI TATQDGPKHL DLTLTRAKFE
ELASDLIDRC RIPVEQAIKD AKLALSEIDE IVLVGGSTRI PAVQAIVKQM TGKEPNQSVN
PDEVVAIGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKLIPRNT TIPTKKSETF
STAADGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVIF VIDANGILNV
TAKDKGSGKE QSISITGAST LSDNEVDRMV KDAEANAAAD KERRERIDLK NQADTLVYQS
EKQLSELGDK ISADEKSKVE GFIQELKDAL AAEDYDKIRS IIEQLQQALY AAGSSVYQQA
SAEASANAQA GPSSSSSSSS GDDDVIDAEF SESK