ID K9Y839_HALP7 Unreviewed; 641 AA.
AC K9Y839;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN OrderedLocusNames=PCC7418_0893 {ECO:0000313|EMBL:AFZ43106.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ43106.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP003945; AFZ43106.1; -; Genomic_DNA.
DR RefSeq; WP_015224983.1; NC_019779.1.
DR AlphaFoldDB; K9Y839; -.
DR STRING; 65093.PCC7418_0893; -.
DR KEGG; hao:PCC7418_0893; -.
DR PATRIC; fig|65093.3.peg.954; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010481; 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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 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; IPR029048; HSP70_C_sf.
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; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 514..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 514..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
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:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 69161 MW; D5D98E45FFEE05BA CRC64;
MSKVVGIDLG TTNSCVAVME GGKPTVISNA EGFRTTPSVV GYAKNGDRLV GQIAKRQGVM
NPQNTFYSVK RFIGRKYDEI QEEAKEVSYE VKRASDGNVK LECPNQEKEF APEEISAQVL
RKLVEDASKY LGEDISEAVI TVPAYFNDSQ RQATKDAGKI AGLDVKRIIN EPTAASLAYG
LDKKSNETIL VFDLGGGTFD VSILEVGDGV FEVLATSGDT HLGGDDFDKK IVDHLADEFK
KQEGIDLRQD KQALQRLTEA AEKAKIELSS VSQADVNLPF ITATQEGPKH LDTSLTRAKF
EEICSDLIDR CSVPVENALK DAKLDKSKID EIVMVGGSTR IPAIQELVKT KLGKDPNLSV
NPDEVVAVGA AIQGGVLSGE VKDILLLDVT PLSLGVETLG GVMTTMIQRN TTIPTKKAET
FSTAVDGQTN VEIHVLQGER EFAKDNKSLG TFRLDGIPPA PRGVPQIEVT FDIDANGILN
VTAKDKGSGK EQSISITGAS TLPEDEVERM VDEAEKNAEE DKQRREKIER KNQADSLVYQ
AEKQINELGD KVPAEEKTKA EDLISQLKEA VSQEDDDQIQ KLMPELQQVL YSIGSNVYQQ
DGTAAADAAA GDGAASGETG ESSSGKSDGD DVIDAEFSET K
//
