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Database: UniProt
Entry: A0A081XRY4_STRTO
LinkDB: A0A081XRY4_STRTO
Original site: A0A081XRY4_STRTO 
ID   A0A081XRY4_STRTO        Unreviewed;       616 AA.
AC   A0A081XRY4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:KES06307.1};
GN   ORFNames=BU52_14660 {ECO:0000313|EMBL:KES06307.1};
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=55952 {ECO:0000313|EMBL:KES06307.1, ECO:0000313|Proteomes:UP000028341};
RN   [1] {ECO:0000313|EMBL:KES06307.1, ECO:0000313|Proteomes:UP000028341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES06307.1,
RC   ECO:0000313|Proteomes:UP000028341};
RA   Hong H.-J., Kwun M.J.;
RT   "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL   Submitted (FEB-2014) 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:KES06307.1}.
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DR   EMBL; JFCB01000011; KES06307.1; -; Genomic_DNA.
DR   RefSeq; WP_037933546.1; NZ_JFCB01000011.1.
DR   AlphaFoldDB; A0A081XRY4; -.
DR   STRING; 55952.BU52_14660; -.
DR   eggNOG; COG0443; Bacteria.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000028341; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028341};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          492..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          222..249
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        492..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..616
FT                   /note="Basic and acidic residues"
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   616 AA;  65911 MW;  E84181D5729EF1F8 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVITNA EGARTTPSVV AFAKNGEVLV GEVAKRQAVT
     NVDRTIRSVK RHMGTDWKIE LDGKPFNPQQ ISAFVLQKLK RDAESYLGEK VTDAVITVPA
     YFNDAERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKD EQVILVFDLG GGTFDVSLLE
     IGDGVVEVKA TNGDNNLGGD DWDQRVVDYL VKQFQSGHGV DLAKDKMALQ RLREAAEKAK
     IELSSSTETT INLPYITASA EGPLHLDEKL TRAQFQQLTA DLLERCKTPF HNVIKDAGIS
     VNEIDHVVLV GGSTRMPAVA ELVKELTGGK EANKGVNPDE VVSIGAALQA GVLKGEVKDV
     LLLDVTPLSL GIETKGGIMT KLIERNTTIP TKRSEIFTTA EDNQPSVQIQ VYQGEREIAA
     YNKKLGMFEL TGLPPAPRGV PQIEVSFDID ANGIMHVTAK DLGTGKEQKM TVTGGSSLPK
     DEVDRMRQEA EKYAEEDHAR REAAEARNQG EQLVYQTEKF LGDNADKVPA DIKTEVEGAV
     AELKEKLKGD DTAEIRTATE KVAAVSQKLG QAMYADAQGA QAAGGASAGA DAGQAKADDD
     VVDAEIVDED RKDGAA
//
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