ID A0A345XJG8_9ACTN Unreviewed; 630 AA.
AC A0A345XJG8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=DVA86_03100 {ECO:0000313|EMBL:AXK31784.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK31784.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK31784.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK31784.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) 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; CP031320; AXK31784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XJG8; -.
DR Proteomes; UP000254425; Chromosome.
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; 2.
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 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:UP000254425};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 582..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 67227 MW; E0276A337149393A CRC64;
MARAVGIDLG TTNSVVSVLE GGEPTVITNA EGARTTPSVV AFAKNGEVLV GEVAKRQAVT
NVDRTVRSVK RHMGTDWKIN LDGKDFNPQQ MSAFVLQKLK RDAEAYLGEK VADAVITVPA
YFNDHERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLEKE DQTILVFDLG GGTFDVSLLE
IGDGVVEVKA TNGDNQLGGD DWDQRVVDHL VKQFQSGHGV DLGKDKMALQ RLREAAEKAK
IELSSSTETG INLPYITASA EGPLHLDEKL TRAQFQQLTQ DLLERCKTPF HNVIKDAGIQ
LSEIDHVVLV GGSTRMPAVA ELVKELTAGK EANKSVNPDE VVAIGASLQA GVLKGEVKDV
LLLDVTPLSL GIETKGGIMT KLIERNTTIP TKRSEIFTTA EDNQPSVQIQ VYQGEREIAA
YNKKLGMFEL TGLPPAPRGV PQIEVTFDID ANGIMHVAAK DLGTGKEQKM TVTGGSALPK
DDIERMMRDA EQYADEDSKR REAAETRNQA EQLVYTTEKF LKDNDEKVPA DVKSEVETAL
ADLKEKLKGG ETAEGEDTAA IREASEKVAA TSQKLGQALY ADAQAAQAAG GPEGAQAGAG
EAGAAGAPGA EEDVVDAEIV DDDKPKDGAA
//
