DNAK_FLAJ1
ID DNAK_FLAJ1 Reviewed; 627 AA.
AC A5FGL1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Fjoh_2631;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ05658.1; -; Genomic_DNA.
DR RefSeq; WP_012024697.1; NZ_MUGZ01000009.1.
DR AlphaFoldDB; A5FGL1; -.
DR SMR; A5FGL1; -.
DR STRING; 376686.Fjoh_2631; -.
DR EnsemblBacteria; ABQ05658; ABQ05658; Fjoh_2631.
DR KEGG; fjo:Fjoh_2631; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006694; 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 Stress response.
FT CHAIN 1..627
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079226"
FT REGION 596..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..616
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 627 AA; 67395 MW; 7CEB178DE4D253E0 CRC64;
MGKIIGIDLG TTNSCVSVME GNEAVVIPNA EGKRTTPSII AFVEGGEIKV GDPAKRQAVT
NPTKTIASIK RFMGHTFAET QDEAKRVPYS VVKGDNNTPR VDIDGRLYTA QELSAMTLQK
MKKTAEDYLG QTVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVMRIINEP TAAALAYGLD
KKGNDQKIAV YDLGGGTFDI SVLELGDGVF EVLSTNGDTH LGGDDFDQVI IDWLADEFKT
EEGIDLRLDP MSLQRLKEAA EKAKIELSSS AETEINLPYV TATASGPKHL VKKLSRAKFE
QLSDTLVKRS MEPVAKALKD AGLSTSDIDE VILVGGSTRM PRIADEVEKF FGKKASKGVN
PDEVVAIGAA IQGGVLSGDV KDVLLLDVTP LSLGIETMGG VLTKLIESNT TIPTKKSQVF
STAADSQPSV EIHVLQGERA MAADNKTIGR FHLDGIPPAP RGVPQIEVTF DIDANGIIKV
SATDKGTGKS HDIRIEASSG LTAEEIEKMK KDAEANADAD RIAKERAEKL NEADSTIFQT
ESQLKELGDK LTDDQKTAIE YALTELRMAH QSQDLDAIQK GLDNVNAAWK TATEAMYAQG
GDQGQQAAPQ QEQSGDNVED VEFEEVK