DNAK_WOLTR
ID DNAK_WOLTR Reviewed; 635 AA.
AC Q5GSE1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, 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=Wbm0495;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(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; AE017321; AAW71083.1; -; Genomic_DNA.
DR RefSeq; WP_011256693.1; NC_006833.1.
DR AlphaFoldDB; Q5GSE1; -.
DR SMR; Q5GSE1; -.
DR STRING; 292805.Wbm0495; -.
DR PRIDE; Q5GSE1; -.
DR EnsemblBacteria; AAW71083; AAW71083; Wbm0495.
DR KEGG; wbm:Wbm0495; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000534; 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; 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 Stress response.
FT CHAIN 1..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226029"
FT REGION 533..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 635 AA; 68938 MW; F369F0AC0C51804A CRC64;
MGRAIGIDLG TTNSCVAIQG KIIENKEGAR TTPSVVAFTS SGERLIGAPA KRQATTNASN
TFFATKRLIG RQYGDPEMKD LNVPYKVFAA KNGDAWIKTT DGKEYSPSQI GAFILQNLKE
AAEAYLGEEV KDAVITVPAY FNDSQRQATK DAGKIAGLNV LRIVNEPTAA ALAYGLDKKH
GHTIVVYDLG GGTFDVSILE IGDGVFEVKA TNGDTHLGGE DFDNAIVSYL LDEFKKSNGI
GLKNDPMAMQ RIKEAAEKAK IELSSAMETE INLPFITADA NGPKHLNMKL TRAKLESLVN
DLIERTMTPC KKALEDTGLS ANQIGEVVLV GGMTRMPRVI EKVKEFFGKD PHRGVNPDEV
VAIGAAIQAG IVQGDVRDVL LLDVTPLSLG IETLGGVFTP LIERNTTIPT KKSQVFSTAE
DNQTAVTIKV HQGERKLAVD NKLLGQFSLE GIPPAPRGIP QIEVTFDIDA NGIVHVSAKD
KATGKEQKIR IQSSGGLSES EINRMIREAE EKAQEDEKRK KFVEVKNQAD SLVHSTEKSL
KEYGDKVSPE DKSAIENAVN ELKEASKSDN IDDVDSIQQK ITNLSQLSMK LGETIYKESQ
QQQGKESSAG SSTTNEEEKV VDSDYQDIDN KEENK