ID A0A1A9B1M0_9ACTN Unreviewed; 622 AA.
AC A0A1A9B1M0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=GA0070622_0330 {ECO:0000313|EMBL:SBT63380.1};
OS Micromonospora sediminicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=946078 {ECO:0000313|EMBL:SBT63380.1, ECO:0000313|Proteomes:UP000199558};
RN [1] {ECO:0000313|EMBL:SBT63380.1, ECO:0000313|Proteomes:UP000199558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45794 {ECO:0000313|EMBL:SBT63380.1,
RC ECO:0000313|Proteomes:UP000199558};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FLRH01000003; SBT63380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9B1M0; -.
DR STRING; 946078.GA0070622_0330; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000199558; 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 467..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 481..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 622 AA; 66460 MW; 283D1D8F9EF40ACD CRC64;
MARAVGIDLG TTNSCVSVLE GGEPTVIANA EGSRTTPSIV AFARNGEVLV GEVAKRQAVT
NPDRTIRSVK REIGTNWTVD IDGKKYTPQE ISARTLMKLK RDAEAYLGEQ ITDAVITVPA
YFNDGQRQAT KEAGEIAGFN VLRIVNEPTA AALAYGLDKG SKEQTVLVFD LGGGTFDVSL
LELAEGVVEV KSTSGDNQLG GDDWDQRIID HLVKTFRGEH GIDLSQDKMA MQRLKEAAEK
AKIELSAATT SNINLPYITA GSAGPLHLDV TLSRAEFQRM TQDLLDRCKG PFEQAVKDAG
IKISDVDHVI LVGGSTRMPA VTDLVKQLTG RDPNKGVNPD EVVAVGAALQ AGVLKGEVKD
VLLLDVTPLS LGIETKGGIF TKLIERNTTI PTKRSEVFTT ADDNQPSVLI QVFQGEREIA
AYNKKLGTFE LTGLPPAPRG VPQIEVTFDI DANGIVNVHA KDLGTGKEQK MTITGGSSLP
KDDIERMRRD AEEHADEDKR RREEAETRNV AEALQWQTEK FLAESGDKLP SENRDQLNEA
LGELRSALGG QDIEKIKSAH EKLAQVSQQA GSLLYAQQQE GEQTAPGAAG PGAGAGAGAA
GGPQAGGADD VVDAEIVDED KK
//
