ID   DNAK3_SYNY3             Reviewed;         771 AA.
AC   P73098;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 137.
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=sll1932;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17123.1; -; Genomic_DNA.
DR   PIR; S75209; S75209.
DR   AlphaFoldDB; P73098; -.
DR   SMR; P73098; -.
DR   STRING; 1148.gene:10497984; -.
DR   PaxDb; 1148-1652199; -.
DR   EnsemblBacteria; BAA17123; BAA17123; BAA17123.
DR   KEGG; syn:sll1932; -.
DR   eggNOG; COG0443; Bacteria.
DR   InParanoid; P73098; -.
DR   PhylomeDB; P73098; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..771
FT                   /note="Chaperone protein dnaK3"
FT                   /id="PRO_0000078570"
FT   REGION          624..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..734
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   771 AA;  86030 MW;  BE715F28B372738C CRC64;
     MGKVVGIDLG TTNSVVAVME GGKPIVIANA EGMRTTPSVV GFNKEGELVV GQMGRRQAVL
     NPQNTFYGVK RFMGRRYTDL TPESKRVAYT IRRDDRDNIK VRCPRLKKDF APEEISAMIL
     RKLAEEASRY LGEKVTGAVI TVPAYFNDSQ RQATRDAGKI AGLEVLRIIN EPTAASLAYG
     LDQGRIQKIL VFDLGGGTFD VSVLEVGDGI FEVKATSGDT QLGGNDFDRR IVDWLAEKFL
     EAEKVDLRQD RQALQRLTEA AEKAKIELSG VGTTEINLPF ITATEDGPKH LETQLSRSEF
     EDLCGDLVTR LQRPVKRVLK DAGLSPVQID EVVLVGGGTR MPMVKGLVRS FIDREPNENV
     NPDEVVAIGA AIQAGILDGE VKDILLLDVT PLSFGLETIG GVMKKLLPRN TTIPVRKSDI
     FSTGENNQTV VEVHVLQGER EMASDNISLG RFKLSGIPPA PRGVPQVQVS FDIDANGILQ
     VTARDKTTGR EQSITVQGAS ILSEGEVNRM IQEAETFAAQ DRERRERIEK RNSAKALTDQ
     AQRRLKEVTL DFGSAFTVSY RRQVDALCSE ILDSLEKDDE RRLDRAQADL QDVLYELNRE
     VRLQYDDKEE GFFEAIKKTF TGDFDDDDDY YNRRPAPRDD YRGGNDYGRY DDYNYNAPSR
     REAPMPRAGA GRGPSLSKDY RSTAYADWDQ SRVTRQRPYQ GESLGGTYDD RRSSPQDDYS
     RGDRQKDYDY RENAPSRSGR GGNGRYGERP AQPGRNAPLQ NGWDDDDDDW F
//