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Database: UniProt
Entry: A0A2T0LUP3_9PSEU
LinkDB: A0A2T0LUP3_9PSEU
Original site: A0A2T0LUP3_9PSEU 
ID   A0A2T0LUP3_9PSEU        Unreviewed;       621 AA.
AC   A0A2T0LUP3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=B0I33_105116 {ECO:0000313|EMBL:PRX47538.1};
OS   Prauserella shujinwangii.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=1453103 {ECO:0000313|EMBL:PRX47538.1, ECO:0000313|Proteomes:UP000238362};
RN   [1] {ECO:0000313|EMBL:PRX47538.1, ECO:0000313|Proteomes:UP000238362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7125 {ECO:0000313|EMBL:PRX47538.1,
RC   ECO:0000313|Proteomes:UP000238362};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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}.
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:PRX47538.1}.
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DR   EMBL; PVNH01000005; PRX47538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0LUP3; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000238362; 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; -; 3.
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   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:UP000238362};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          583..621
FT                   /note="Disordered"
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   621 AA;  66441 MW;  A61AA8A689F9FDCC CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVIANS EGSRTTPSVV AFAKNGEVLT GQSAKNQAVT
     NVDRTIRSVK RHMGTDWKTE IDGKAYTPQE ISARVLMKLK RDAESYLGEE VTDAVITVPA
     YFEDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG EKEQTILVFD LGGGTFDVSL
     LEIGEGVVEV RATSGDNHLG GDDWDERIVN WLVDKFKASH GIDLTKDKMA LQRIKEAAEK
     AKIELSSSTT ANINLPYITV DADKNPLFLD ETLSRAEFQR ITSDLLDRTK SPFHNVIRDA
     GIAVGDIDHV VLVGGSTRMP AVTDLVKELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
     KDVLLLDVTP LSLGIETKGG VFTKLIERNT TIPTKRSEIF STADDNQPSV QIQVFQGERE
     IAAQNKKLGM FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDLGTGNE QSIRITGGSA
     LPQDEIDRMV KDAEAHAEED RKRREEAETR NQAETLVYQT EKFLTDNDEK LPEDLKGKVK
     TAIDEANEAL KGTDTAKIKE SMEKLNSASQ ELATALYANT GAQAGAEGAA GAAGGAAGDT
     SGSQKADDVV DAEIVDEDDK K
//
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