DNAK_XANC5
ID DNAK_XANC5 Reviewed; 641 AA.
AC Q3BVB8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=XCV1564;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ23196.1; -; Genomic_DNA.
DR RefSeq; WP_011346955.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BVB8; -.
DR SMR; Q3BVB8; -.
DR STRING; 456327.BJD11_14810; -.
DR EnsemblBacteria; CAJ23196; CAJ23196; XCV1564.
DR GeneID; 63990792; -.
DR KEGG; xcv:XCV1564; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000007069; 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..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226031"
FT REGION 606..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 68752 MW; 07C415B64A368719 CRC64;
MGKIIGIDLG TTNSCVSIMD GGKARVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
NPKNTFYAVK RLIGRKFTDG EVQKDISHVP YGILAHDNGD AWVQTSDAKR MAPQEISARV
LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
GLDKNGGDRK IAVYDLGGGT FDVSIIEIAE VDGEKQFEVL ATNGDTFLGG EDFDNRVIEY
LVDEFNKDQG IDLRKDPLAL QRLKDAAERA KIELSSSQQT EVNLPYVTAD ASGPKHLNIK
LTRAKLEALV EDLVKKSIEP CRTALNDAGL RASDINEVIL VGGQTRMPKV QQAVADFFGK
EPRKDVNPDE AVAVGAAIQG GVLAGDVKDV LLLDVTPLSL GIETMGGVFT KIIEKNTTIP
TKASQTFSTA EDNQSAVTVH VLQGEREQAR FNKSLAKFDL SGIEPAPRGM PQVEVSFDID
ANGILHVSAK DKKTNKEQKV EIKAGSGLSD EEIQRMVADA EANREEDKKF QELVQARNQA
DGLIHATRTA ITEHGSKVGG DVIGKVEAAL SDLETAMKGD DKAQIEARTK TLEEAGQSLY
AAAAAAEQGG NADAASGNAQ ASKAADDVVD AEFTEVKDDK K