DNAK_FLAPJ
ID DNAK_FLAPJ Reviewed; 626 AA.
AC A6GXZ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=FP0864;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; AM398681; CAL42964.1; -; Genomic_DNA.
DR RefSeq; WP_011963020.1; NC_009613.3.
DR RefSeq; YP_001295780.1; NC_009613.3.
DR AlphaFoldDB; A6GXZ1; -.
DR SMR; A6GXZ1; -.
DR STRING; 402612.FP0864; -.
DR PRIDE; A6GXZ1; -.
DR EnsemblBacteria; CAL42964; CAL42964; FP0864.
DR GeneID; 66552514; -.
DR KEGG; fps:FP0864; -.
DR PATRIC; fig|402612.5.peg.879; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000006394; 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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059559"
FT REGION 598..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 626 AA; 67361 MW; 611055F632DF38B5 CRC64;
MGKIIGIDLG TTNSCVSVME GQEAVVIPNA EGKRTTPSII AFVEGGEIKV GDPAKRQAVT
NPTKTVASIK RFMGHSFSET TDEAKRVPYS VVKGDNNTPR VDIDGRLYTA QELSAMTLQK
MKKTAEDYLG QTVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVMRIINEP TAAALAYGLD
KKGIDQKIAV YDLGGGTFDI SILELGDGVF EVLSTNGDTH LGGDDFDQTI IDWLADEFKA
EEGIDLRLDP MSLQRIKEAA EKAKIELSSS AETEINLPYV TATASGPKHL VKKLTRAKFE
QLSDTLVKRS MEPVAKALKD AGLTVKDIDE VILVGGSTRM PRIADEVEKF FGKKASKGVN
PDEVVAIGAA IQGGVLSGDV KDVLLLDVTP LSLGIETMGG VMTILIESNT TIPTKKSQIF
STAADSQPTV ELHVLQGARA MAVDNKTIGR FNLDGIPPAP RGVPQIEVAF DIDANGIIKV
SATDKGTGKS HDIRIEASSG LTSEEIERMK KDAEANAGAD KIARERVEKI NEADSLIFQT
ETQLKELGDK ITDEHKTAIE YALTELRMAH QSQDLEAIQK GLDNVNAAWK TATEAMYAQG
EQGQAAQPQA ETQGDDVQDV EFEEVK