ID A0A097III2_9CORY Unreviewed; 619 AA.
AC A0A097III2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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:AIT61947.1};
GN ORFNames=CDOO_12285 {ECO:0000313|EMBL:AIT61947.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT61947.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT61947.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT61947.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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; CP006764; AIT61947.1; -; Genomic_DNA.
DR RefSeq; WP_018022111.1; NZ_CP006764.1.
DR AlphaFoldDB; A0A097III2; -.
DR STRING; 558173.CDOO_12285; -.
DR KEGG; cdo:CDOO_12285; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000029914; 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; 3.30.30.30; -; 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 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:UP000029914};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 461..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 464..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..544
FT /note="Basic and acidic residues"
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 619 AA; 66454 MW; BD762258367B72AA CRC64;
MGRAVGIDLG TTNSVVSVLE GGEATVIANS EGARTTPSVV AFAKNGEVLV GQSAKNQAVT
NVDRTIRSVK RHMGTDWTVA IDDKNYTAQE ISARTLQKLK RDAEAYLGDE VTDAVITVPA
YFEDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLEKG DKEQTILVFD LGGGTFDVSL
LEIGDGVVEV IATAGDNELG GDDWDQRIVN WLVDKFKSSN GVDLSKDKMA MQRLREAAEK
AKIELSSSQQ ASINLPYITV DSEKNPLFLD ETLTRTEFQK ITQDLLDRTK TPFNQVIKDA
DMSVSDVDHV VMVGGSTRMP AVTDLVKELT GREPNKGVNP DEVVAVGAAL QAGVLRGEVK
DVLLLDVTPL SLGIETKGGV MTKLIERNTT IPTKRSETFT TAEDNQPSVQ IQVFQGEREM
AAANKLLGSF ELSDIAPAPR GIPQIEVTFD IDANGIVSVS AKDKGTGKEN TITISDGSGL
SEDEINRMVK DAEEHADEDK KRREEQETRN SAESTSYQTR KFVEDNADKL SEDDKNKVTE
AADEVDEALK GDDLEAIKSA VEKLSQAAQA AGTSLYEAQA NEGATPGAAG EPTDPNVVDA
EVVEDEAADS TEDTKDGDK
//
