ID A0A0G0MZR7_9BACT Unreviewed; 636 AA.
AC A0A0G0MZR7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=US91_C0005G0056 {ECO:0000313|EMBL:KKQ70351.1};
OS Candidatus Falkowbacteria bacterium GW2011_GWE1_38_31.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1618638 {ECO:0000313|EMBL:KKQ70351.1, ECO:0000313|Proteomes:UP000034022};
RN [1] {ECO:0000313|EMBL:KKQ70351.1, ECO:0000313|Proteomes:UP000034022}
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:KKQ70351.1}.
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DR EMBL; LBUU01000005; KKQ70351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MZR7; -.
DR PATRIC; fig|1618638.3.peg.656; -.
DR Proteomes; UP000034022; 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; 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 599..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..530
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 611..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 636 AA; 69209 MW; 3F2BD73E5B2E5ED3 CRC64;
MSKIIGIDLG TTNSAVAIME GGQPKIIENV EGNRTTPSIV AISKNGERLI GQTAKRQAVT
NPENTVYAVK RLIGRKFEDE EVQRDINHVP YKIVKTGEGV SVKMNDKDYS PQEVSAMILS
KIKADVEAKI GEKITEAVIT VPAYFNDSQR QATKDAGKIA GLDVLRIINE PTAAALAYGF
EKKKGQKIAV YDLGGGTFDV SILDVSEDTV EVKATNGDTH LGGEDFDQII IKWIIEEFKK
DTGLNLGNDK LALQRIKEAA EKAKIELSTT MESEINQPFI TTDENGPKHL VMKITRAKLE
ELVGHLVEKT MHPCREALRD AGFKTSDIEE VILVGGMTRM PLVQQKVKEF FGKEPNLSVN
PDEVVAIGAA VQAGVLRGEV KDVLLLDVTP LSLGIETLGG ISTALIERNT TIPTGKSQVF
STAADSQTSV EIHIVQGERG MAADNKTLGR FMLDGIPPAP RGVPQIEVSF NIDANGILNV
SAKDKATGKQ QSISITASSG LSKEEIERMK KEAEAHAEED KKKKENIEIK NQAETVVFTT
EKLLKESGDK MKAEDKKELE EKLEALKKIK DGDDAEDIKK KMEEMSQVAQ RIGAAMYSAQ
AQADAAGKTE GAAEGEQKAD KKDDPLEGVF TEKKNK
//
