ID A5GTQ4_SYNR3 Unreviewed; 661 AA.
AC A5GTQ4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
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:CAK28263.1};
GN OrderedLocusNames=SynRCC307_1360 {ECO:0000313|EMBL:CAK28263.1};
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28263.1, ECO:0000313|Proteomes:UP000001115};
RN [1] {ECO:0000313|EMBL:CAK28263.1, ECO:0000313|Proteomes:UP000001115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG Genoscope;
RL Submitted (MAY-2006) 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; CT978603; CAK28263.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GTQ4; -.
DR STRING; 316278.SynRCC307_1360; -.
DR KEGG; syr:SynRCC307_1360; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000001115; 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; 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 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.
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:UP000001115};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 634..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 524..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 636..661
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 661 AA; 72460 MW; 77021533C2AA7616 CRC64;
MGRIVGIDLG TTNSVLAVLE GGRPVVVANA EGLRTTPSVV GFSREKELLV GQAARRQLVL
NPRDSFSNLK RLIGRQWQEL DEASQAVAYT IRANDLGQVR VVCPATEREY APEELVACLL
RKLVDDAATY LGEEVEAAVV TVPAYFDDSQ RQATRDAGRL AGLTIERILN EPTAAALAYG
FDRSRSQTVL VFDLGGGTFD VSLLRIANGV FDVKATSGDT QLGGNDFDQR IVDWLAEGFQ
QANGVDLRRD RQALQRLLEV AEKAKQELSG TLKTTISLPF IATAESGPLH LETSLDRRTF
ESLCPDLLDR LLRPVQAALR DARLAPEDVD EVVLVGGSSR MPMVQQLVRT LVPREPSQNV
NPDEVVAVGA AVQAGILTGE LRDLMLNDVT PLSVGLETIG GLMKTIIPRN TPIPVRRSDV
FSTSEANQSS VEVHVLQGER PMGGDNKSLG RFRLAGIPPA PRGVPQVQVS FDVDANGILE
VSATDRTTGR RQSVTVQGSA NLNQQEIDQL IAEAASQSME DRRKRSAVDR RNRAETLIAQ
AERRLRDAAL ELGPYGAERQ QRAVEMALRD LRDGLEQADE RELDLLTSQL EEALYGLNRR
LTAERRELDG GAGPLEGIKS TLGSLKDELF AEDDWDDWDR PGGGRGRYDR YDRSDDPWGR
Y
//
