ID A0A1H4KQK9_9MICC Unreviewed; 616 AA.
AC A0A1H4KQK9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04489745_0742 {ECO:0000313|EMBL:SEB60378.1};
OS Arthrobacter woluwensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=156980 {ECO:0000313|EMBL:SEB60378.1, ECO:0000313|Proteomes:UP000182652};
RN [1] {ECO:0000313|EMBL:SEB60378.1, ECO:0000313|Proteomes:UP000182652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10495 {ECO:0000313|EMBL:SEB60378.1,
RC ECO:0000313|Proteomes:UP000182652};
RA de Groot N.N.;
RL Submitted (OCT-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; FNSN01000003; SEB60378.1; -; Genomic_DNA.
DR RefSeq; WP_066216172.1; NZ_JAUSXR010000001.1.
DR AlphaFoldDB; A0A1H4KQK9; -.
DR STRING; 156980.SAMN04489745_0742; -.
DR Proteomes; UP000182652; 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 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:UP000182652};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 581..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..255
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 616 AA; 65696 MW; 2CA6411FE7454466 CRC64;
MSRAVGIDLG TTNSVVSVLE GGEPTVIANA EGGRTTPSVV AFSKNGEVLV GEIAKRQAVN
NIDRTIASVK RHMGTDWSVD VDGKKYTAQE ISARTLMKLK NDAEAYLGEK VTDAVITVPA
YFNDAERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDEDGF STIQVRATAG DNRLGGDDWD DRIVQYLLGQ LKAKGIDLSK DKIALQRLRE
AAEQAKKELS SSTSTNISLQ YLSVTADGPV HLDEHLTRAK FQDLTKDLLE RTKKPFHDVI
KEAGIKVSDI DHIVLVGGST RMPAVTELVK ELAGGKEPNK GVNPDEVVAV GAALQAGVLK
GERKDVLLID VTPLSLGIET KGGVMTKLIE RNTAIPTKRS ETFTTADDNQ PSVSIQVFQG
EREFTRDNKP LGTFELTGIA PAPRGVPQIE VTFDIDANGI VHVSAKDKGT GVEQSMTISG
GSALSKEDIE RMVADAEAHA AEDKKRREAA DTRNAAEQLA YATDKLIADN DDKLPEEVKT
EVKADVDALK AALEGTDDDA VKAAFEKLQA SQTKLGEAIY AQSQAPAGGE EAAGASAGAP
EEDIVDAEII DEDEKK
//
