ID B8HWL5_CYAP4 Unreviewed; 630 AA.
AC B8HWL5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Cyan7425_4127 {ECO:0000313|EMBL:ACL46441.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL46441.1};
RN [1] {ECO:0000313|EMBL:ACL46441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL46441.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001344; ACL46441.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HWL5; -.
DR STRING; 395961.Cyan7425_4127; -.
DR KEGG; cyn:Cyan7425_4127; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OrthoDB; 9766019at2; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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}; Oxidoreductase {ECO:0000313|EMBL:ACL46441.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 600..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 600..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 67938 MW; 73E20C6FA07EF007 CRC64;
MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AFTKTGDRLV GQIAKRQAVM
NPENTFYSVK RFIGRRFDEV THETTEVSYK VLNVNGNVKL NCPAAGKQFA PEEISAQVLR
KLVEDASKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GIEVLRIINE PTAASLAYGL
DKKANETILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDKKI VDFLAEEFRK
TEGIDLRKDK QALQRLTEAA EKAKIELSSV TQTEINLPFI TATQDGPKHL DMTLTRAKFE
ELCSDLIDRC RRPVEQALND AKLSKENIDE VVLVGGSTRI PAIQELVKRA LGKDPNQTVN
PDEVVAVGAA IQAGVLAGEV KDILLLDVTP LSLGVETLGG VMTKIIPRNT TIPTKKSEVF
STAVDGQTNV EIHVLQGERE MANDNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILNV
KARDKGTGKE QSISITGAST LPKDDVDRMV REAEMNAAAD KAKREKIEVG NQADSLAYQA
EKQLAELGDK VPANEKEKVE ALIRDLREAK NQENYDRVKT LTTELQQALY NIGANLYQQS
GASEAPSGDG TGSTGTSGDD VIDAEFSESK
//
