ID A0A0X3W8A7_9ACTN Unreviewed; 642 AA.
AC A0A0X3W8A7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ECO:0000313|EMBL:KUL53091.1};
GN ORFNames=ADL30_21175 {ECO:0000313|EMBL:KUL53091.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL53091.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL53091.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL53091.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
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:KUL53091.1}.
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DR EMBL; LLZK01000210; KUL53091.1; -; Genomic_DNA.
DR RefSeq; WP_062777603.1; NZ_LLZK01000210.1.
DR AlphaFoldDB; A0A0X3W8A7; -.
DR Proteomes; UP000053420; 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 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:UP000053420};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 584..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 179
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 642 AA; 68783 MW; 462A375ACBFD226C CRC64;
MARAVGIDLG TTNSVVAVLE GGEPTVVANA EGARTTPSVV AFAKSGDVLV GEVAKRQAVT
NVERTARSVK RHMGDGGWRF PESGSVDGTR YTAQELSARV LQKLKRDAES YLGEDVTDAV
VTVPAYFDDT QRQATKEAGE IAGLNVLRII NEPTAAALAY GLDKGDDQTV LVFDLGGGTF
DVSLLEMGEG VIEVKATNGD TQLGGDDWDQ RIVEHLVRQF KNAHGVDLGK DKMALQRLRE
GAEKAKIELS SSSETDINLP YITASADGPL HLAEKLTRAR FQELTADLLE RCKAPFHQAV
DDAGVELSNV DHVILVGGST RMPAVTELVR ELTGKDPHKG VNPDEVVALG AALQAGVIRG
DVKDVLLLDV TPLSLGIETK GGIMTKLIER NTTIPTRRSE TFSTAEDNQP SVGIQVFQGE
REIAAYNKKL GVFDLTGLPP APRGVPKIEV TFDIDANGIM HVSAKDEATG REQRMTVTGG
SALPEDDINR MVREAEEHAE EDRRRREAAE TRNQAEQLLC QTERFLKDNA ANLANVPAET
RTEVETAAAE LKDTLKDNAD DTAALRAGAE KLATVSQKLG QALYANAGST SKEQPPPPGA
TPGSSAEEGV VDAEIVDEDD QNQSRNQDQD KDKDKGGKGE TL
//
