DNAK1_SYNP6
ID DNAK1_SYNP6 Reviewed; 749 AA.
AC Q5N1V0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chaperone protein DnaK 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein 1 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 1 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK1 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=syc1530_d;
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; BAD79720.1; -; Genomic_DNA.
DR RefSeq; WP_011243840.1; NC_006576.1.
DR AlphaFoldDB; Q5N1V0; -.
DR SMR; Q5N1V0; -.
DR STRING; 269084.syc1530_d; -.
DR EnsemblBacteria; BAD79720; BAD79720; syc1530_d.
DR KEGG; syc:syc1530_d; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; PCQSVNP; -.
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; 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..749
FT /note="Chaperone protein DnaK 1"
FT /id="PRO_0000226021"
FT REGION 643..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
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:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 749 AA; 84194 MW; DE83C1EC2B6E94C3 CRC64;
MGRVVGIDLG TTNSVIAVME GGKPMVIANA EGVRTTPSVV GVSKTGERLV GELARRQLVL
NPRNTFANIK RFIGRRYDEL TDESKRVPYT VRRDPEGNVR IVCPQLSREF APEEVAAMIL
RKLAEEASRY LGEPVTGAVI TVPAYFNDSQ RQATRDAGRI AGLEVKRILN EPTAASLAYG
LDRRDNQTIL VFDLGGGTFD VSVLEVGNGV FEVKATSGDT QLGGNDFDRR IVDWLAEQFL
EAEGIDLRRD RQALQRLIEA AEKAKIELSG VSVTDINLPF ITATEDEPKH LETRLTRSEF
EALCEDLLER MMRPLRRALK DARLQPQDID EVVLVGGSTR MPMVQQLVRS LIGREPNQNV
NPDEVVAIGA AIQAGILAGE VKDILLLDVT PLSLGLETIG GVMKKLIPRN TAIPVRRSDI
FSTAENNQTM VEIHILQGER QLAEGNKSLG RFKLTGIPPA PRGVPQVQVS FDIDANGILQ
VSALDKTTGR EQTVTIQGAS TLSQEEVKRM MKDAELYAQQ DRQLKARIEK RNRAQTLIAQ
SERRLREISL DFGLYFAESK RRRIESTIRE LKDYLERQDD RGLDLALAEL QDALFDLNQE
TAARLRDEEG EGFFEPLKQT FASLRGDGNR DFERSWDDRG GDRWDADPWD RSRRSTPSYG
YDDRRSPVSD PYRGERWVEE QTSMSRREPV RDRNGGNGSV RPEPAPRRGR PTWEEDQPPR
RDRSSQPPAK PASGRRWNDG WDDDDDEWF