ID A0A0G0SME1_9BACT Unreviewed; 638 AA.
AC A0A0G0SME1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
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=UT58_C0005G0018 {ECO:0000313|EMBL:KKR26842.1};
OS Microgenomates group bacterium GW2011_GWC1_39_7b.
OC Bacteria.
OX NCBI_TaxID=1618516 {ECO:0000313|EMBL:KKR26842.1, ECO:0000313|Proteomes:UP000034178};
RN [1] {ECO:0000313|EMBL:KKR26842.1, ECO:0000313|Proteomes:UP000034178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Acts as a chaperone. {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:KKR26842.1}.
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DR EMBL; LBXI01000005; KKR26842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0SME1; -.
DR PATRIC; fig|1618516.3.peg.181; -.
DR Proteomes; UP000034178; 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; 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; 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 510..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 245..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 510..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68933 MW; DB4546765507BE90 CRC64;
MSKIIGIDLG TTNSCLAVME GGRPKVISAG DTGRNTTPSI VEVVKNLVGD VAKRQMILNG
KNTIYSVKRL MGRRFEDKEV KRTIEMVPYK IIEGKSGMAD VEVEGKTYTP QEISARILMK
LKADAEKYLG EKVDKAVITV PAYFDDAQRQ ATKQAGEIAG LKVERIINEP TAAALAYGLE
KKNAHKIAVY DLGGGTFDIS VLELGDGVFE VKATNGDTHL GGDDFDAVIV DHIVSEFKKE
NSVDLKADSQ ALQRVRDAAE KAKIELSAAN EVEINQPYIT QNNGAPLHLT MKLTRAKLES
LVDDLIQKTI KPVESCLKDA KLDAHDIDEV IMVGGMTRMP KVVETVKNFF GKDLNQSVNP
DEVVAIGAAI QGGVLGGEVK DILLLDVTPL TLAIETMGNI ATPMIPRNTT VPTSKTETFS
TASDNQTQVQ IVVTQGERPM SADNKTLGTF VLDGIPPAPR GVPQVEVTFD MDASGILTVT
AKDKATGKTQ NIKITGAVGL SDDEIKRMQE EAEKHKEEDE KKAETIKSKN TADSMVATAE
KSIKDAGDKV PADVKEKVEE KIKKVKEVAG KEDSSKEDIE TATKELSEEL SKIGEAMYKD
QGAKTDDGSQ KTEGENGGKK SEDGKKDDAK VEEGEVVE
//