GenomeNet

Database: UniProt
Entry: A0A0G0SME1_9BACT
LinkDB: A0A0G0SME1_9BACT
Original site: A0A0G0SME1_9BACT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system