DNAK_XANC8
ID DNAK_XANC8 Reviewed; 642 AA.
AC Q4UT11;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=XC_2763;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(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; CP000050; AAY49812.1; -; Genomic_DNA.
DR RefSeq; WP_011036660.1; NC_007086.1.
DR AlphaFoldDB; Q4UT11; -.
DR SMR; Q4UT11; -.
DR EnsemblBacteria; AAY49812; AAY49812; XC_2763.
DR KEGG; xcb:XC_2763; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000420; 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..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226030"
FT REGION 603..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 642 AA; 68837 MW; 404DE445E1EA364C CRC64;
MGKIIGIDLG TTNSCVAIMD GGKARVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
NPKNTFYAVK RLIGRKFTDG EVQKDISHVP YGILAHDNGD AWVQTSDSKR MAPQEISARV
LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
GLDKNGGDRK IAVYDLGGGT FDVSIIEIAE VDGEKQFEVL ATNGDTFLGG EDFDNRVIEY
LVDEFNKDQG IDLRKDPLAL QRLKDAAERA KIELSTSQQT 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 QELVQTRNQA
DGLIHATRTA ITEHGSKVGG DVIGKVEAAL ADLETAMKGD DKAQIEARSK TLEEAGQSLY
AAAAAAEQGG NADAASGNAQ ASKAADDVVD AEFTEVKDDK KA