ID A0A077JEQ5_9CYAN Unreviewed; 637 AA.
AC A0A077JEQ5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:BAP17412.1};
GN ORFNames=ETSB_0571 {ECO:0000313|EMBL:BAP17412.1};
OS cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP17412.1, ECO:0000313|Proteomes:UP000031625};
RN [1] {ECO:0000313|EMBL:BAP17412.1, ECO:0000313|Proteomes:UP000031625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP17412.1};
RX PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA Archibald J.M., Inagaki Y.;
RT "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT recent adaptations to an intracellular lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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; AP012549; BAP17412.1; -; Genomic_DNA.
DR RefSeq; WP_044106105.1; NZ_AP012549.1.
DR AlphaFoldDB; A0A077JEQ5; -.
DR STRING; 1228987.ETSB_0571; -.
DR KEGG; ceo:ETSB_0571; -.
DR HOGENOM; CLU_005965_2_4_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000031625; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 598..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 623..637
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 637 AA; 68007 MW; 5A8FD6F745302F02 CRC64;
MGKIVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNGERLV GQIAKRQAVM
NPENTFYSVK RFIGSKYSEV KTETTEVSYK VDKDSNGNIK LDSPSQGKQF APEEISAQVL
RKLVDDASKY LGETVTEAVI TVPAYFNDSQ RQATKDAGKI AGIEVKRIIN EPTAASLAYG
LDKKSNETIL VFDLGGGTFD VSILEVGDGV FEVLATSGDT HLGGDDFDKK IVDYLAAEFK
AKEGVDLRQD KQALQRLTEA AEKAKIELSG VTQSEINLPF ITATQEGPKH LDTTLTRAKF
EDLCSDLIDR CGIPVKNSMK DAKVSNSDID EVVLVGGSTR IPAVQELVKK ILGKDPNQGV
NPDEVVAVGA AIQGGVLAGD VKDILLLDVT PLSLGVETLG GVMTKIIPRN TTIPTKKSEV
FSTAQDGQAN VEISVLQGER EMSRDNKSLG TFRLDGIPPA PRGVPQIEVT FDINADGILN
VTAKDKGTGK EQSISITGAS TLADTEVDRM IQEAEVNAAA DKERREKIDC KNEADSLVYQ
ADKQLKELGD KIPAADKTKA EGLISQLREA INKEDEDTIK TVMPNLQQLL YSIGTSVYQQ
AGGPTSPEGA TPGGGKGSRG SSEGGDDVID AEFSETK
//
