ID G6FNC1_9CYAN Unreviewed; 697 AA.
AC G6FNC1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, 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 ORFNames=FJSC11DRAFT_0368 {ECO:0000313|EMBL:EHC19551.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC19551.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC19551.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC19551.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC19551.1}.
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DR EMBL; AGIZ01000001; EHC19551.1; -; Genomic_DNA.
DR RefSeq; WP_009454181.1; NZ_AGIZ01000001.1.
DR AlphaFoldDB; G6FNC1; -.
DR GeneID; 60764618; -.
DR PATRIC; fig|741277.3.peg.429; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
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; 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.
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:UP000004344};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 646..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..271
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 646..670
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 697 AA; 77621 MW; 2147A0F4F54B7ACD CRC64;
MGKVVGIDLG TTNSVVAVME GGKPVVIANA EGMRTTPSVV GFSKDGERLV GQMARRQTVL
NPQNTFFAIK RFMGRRYSEL SPESKRVPYT IRKDEVGNIK VVCPRLNKDF APEEISAMIL
KKLAEDASKY LGEPVTGAVI TVPAYFNDSQ RQATRDAGRI AGLEVLRILN EPTAASLAYG
LDRGETETIL VFDLGGGTFD VSILDVGDGV FEVKATSGDT QLGGNDFDKK IVDWLAEQFL
EQEKVDLRRE RQSLQRLMEA AEKAKIELSA VSVTEINLPF IAATEQGPVH LETRLTRSQF
EGLCDDLLGR LRVPVKRALK DAGLTPNDID EVVLVGGSTR MPMVQQLVRA MIGIEPNQNV
NPDEVVAVGA AIQAGILAGE LKDVLLLDVT PLSLGLETIG GVKKVLIPRN TTIPVRRSDI
FSTSENNQNT VEIHVVQGER EMAADNKSLG RFKLYGIPPA PRGIPQIQVA FDIDANGILQ
VTALDRTTGR EQSITIQGAS TLSESEVQQA IREAEKFADV DRQRKEKVEK RTRAEALILQ
AERQLREVAL DFGMAFARNR RQQIDNICRE LRESLKENDD RGIDQAYADL QDALYDLNRE
VRQYYAEEED DDLLGAIKDI FTGGGDKDRD YPRDTFRDRD YYDKDYDRGY GRDYDRSPSR
DHDKSYGRDS RSSAFDGGSS RRSRPTYQDN WDDDDDW
//
