ID A0A239ACR5_9FLAO Unreviewed; 627 AA.
AC A0A239ACR5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04487979_13218 {ECO:0000313|EMBL:SNR93415.1};
OS Flavobacterium sp. ov086.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1761785 {ECO:0000313|EMBL:SNR93415.1, ECO:0000313|Proteomes:UP000198291};
RN [1] {ECO:0000313|EMBL:SNR93415.1, ECO:0000313|Proteomes:UP000198291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV086 {ECO:0000313|EMBL:SNR93415.1,
RC ECO:0000313|Proteomes:UP000198291};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNL01000032; SNR93415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ACR5; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000198291; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 599..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 627 AA; 67402 MW; 8B6A0EBE8D9045D5 CRC64;
MGKIIGIDLG TTNSCVSVME GNEAVVIPNA EGKRTTPSII AFVEGGEIKV GDPAKRQAVT
NPTKTIASIK RFMGHTFAET QEEAKRVPYS VVKGDNNTPR VDIDGRLYTA QELSAMTLQK
MKKTAEDYLG QTVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVMRIINEP TAAALAYGLD
KKGTDQKIAV YDLGGGTFDI SVLELGDGVF EVLSTNGDTH LGGDDFDQVI IDWLADEFKS
EEGIDLRLDP MSLQRLKEAA EKAKIELSSS AETEINLPYV TATASGPKHL VKKLTRAKFE
QLSDTLVKRS MEPVAKALKD AGLSTSDIDE VILVGGSTRM PRIADEVEKF FGKKASKGVN
PDEVVAIGAA IQGGVLSGDV KDVLLLDVTP LSLGIETMGG VMTILIEANT TIPTKKSQVF
STASDSQPSV ELHVLQGARA MAVDNKTIGR FHLDGIPPAP RGVPQIEVAF DIDANGIIKV
TATDKGTGKS HDIRIEASSG LTSEEIEKMK QDAEANAESD KIARERAEKL NEADGMIFQT
ESQLKELGSK LADDHKVAVE YALTELRMAH QSQDIPAIQT ALDNINAAWK TATEAMYAQG
EQGQQAAPQQ EQSQGDNVED VEFEEVK
//
