DNAK_VIBVY
ID DNAK_VIBVY Reviewed; 636 AA.
AC Q7MN85;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=VV0832;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93596.1; -; Genomic_DNA.
DR RefSeq; WP_011078453.1; NC_005139.1.
DR AlphaFoldDB; Q7MN85; -.
DR SMR; Q7MN85; -.
DR STRING; 672.VV93_v1c07730; -.
DR EnsemblBacteria; BAC93596; BAC93596; BAC93596.
DR KEGG; vvy:VV0832; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002675; Chromosome I.
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; SSF100934; SSF100934; 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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078586"
FT REGION 600..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 636 AA; 68793 MW; CB5D7A042158B24F CRC64;
MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTPSVI AYTDGETLVG QPAKRQAVTN
PENTLFAIKR LIGRRFEDEE VQRDIEIMPY KIVKADNGDA WVEAKGQKMA APQVSAEVLK
KMKKTAEDFL GEEVTGAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
DKQGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLAT NGDTHLGGED FDNRLINYLV
AEFKKDQGID LKNDPLAMQR VKEAAEKAKI ELSSTNQTDV NLPYITADAT GPKHMNIKVT
RAKLESLVED LVQRSLEPLK VALADADLSV GDITDVILVG GQTRMPMVQA KVTEFFGKEP
RRDVNPDEAV AVGAAVQGGV LAGDVKDVLL LDVTPLSLGI ETMGGVMTKL VEKNTTIPTK
ANQVFSTAED NQSAVTIHVL QGERKQAMYN KSLGQFNLEG INPAPRGMPQ IEVTFDLDAD
GILHVSAKDK QTGKEQKITI QASGGLSDAE IEKMVQEAEA NKEADKKFEE LATARNQADQ
IIHGTRKQVE EAGEALPADE KAKIETAISE LEEARKGEDK EAIEAKIQAL MAAAQKLMEI
AQQQAQAQQG SAEAGAQSQE DDVVDAEFEE VKDDKK