DNAK_HELPY
ID DNAK_HELPY Reviewed; 620 AA.
AC P55994; O05733;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=HP_0109;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9712748; DOI=10.1128/iai.66.9.4061-4067.1998;
RA Huesca M., Goodwin A., Bhagwansingh A., Hoffman P., Lingwood C.A.;
RT "Characterization of an acidic-pH-inducible stress protein (hsp70), a
RT putative sulfatide binding adhesin, from Helicobacter pylori.";
RL Infect. Immun. 66:4061-4067(1998).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07178.1; -; Genomic_DNA.
DR EMBL; U96271; AAB53800.1; -; Genomic_DNA.
DR PIR; E64533; E64533.
DR RefSeq; NP_206909.1; NC_000915.1.
DR RefSeq; WP_000521014.1; NC_018939.1.
DR AlphaFoldDB; P55994; -.
DR SMR; P55994; -.
DR DIP; DIP-3190N; -.
DR IntAct; P55994; 9.
DR MINT; P55994; -.
DR STRING; 85962.C694_00540; -.
DR PaxDb; P55994; -.
DR EnsemblBacteria; AAD07178; AAD07178; HP_0109.
DR KEGG; hpy:HP_0109; -.
DR PATRIC; fig|85962.47.peg.118; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; DKMVLQR; -.
DR PhylomeDB; P55994; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..620
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078470"
FT REGION 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 26..29
FT /note="IIAN -> DLLRI (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="V -> I (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="K -> Q (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> D (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> L (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="MK -> VE (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> G (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="D -> E (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="S -> SS (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..435
FT /note="VSIMVL -> GVPYGF (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 502..507
FT /note="SDSEIE -> TIAK (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="K -> R (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 570..580
FT /note="VKNDNATKAEL -> IKTITLLKRI (in Ref. 2; AAB53800)"
FT /evidence="ECO:0000305"
FT CONFLICT 586..600
FT /note="LLAQAAQKLGEAMAN -> ALKGSKIRRNGE (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 67052 MW; 8C5E42ECC0558481 CRC64;
MGKVIGIDLG TTNSAMAVYE GNEAKIIANK EGKNTTPSIV AFTDKGEILV GESAKRQAVT
NPEKTIYSIK RIMGLMFNED KAKEAEKRLP YKIVDRNGAC AIEISGKVYT PQEISAKILM
KLKEDAESYL GESVTEAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
DKKESEKIMV YDLGGGTFDV TVLETGDNVV EVLATGGDAF LGGDDFDNRV IDFLASEFKS
ETGIEIKNDV MALQRLKEAA ENAKKELSSA METEINLPFI TADATGPKHL VKKLTRAKFE
SLTEDLMKET ISKIESVIKD AGLTKNEISE VVMVGGSTRI PKVQERVKAF INKDLNKSVN
PDEVVAVGAS IQGGVLKGDV KDVLLLDVTP LSLGIETLGG VMTKVIDRGT TIPAKKSQVF
STAEDNQPAV SIMVLQGERE LARDNKSLGK FDLQGIAPAP RGVPQIEVTF DIDANGILTV
SAQDKNTGKS QEIKISGSSG LSDSEIEKMV KDAELHKEED AKKKEVIEAR NHADSLAHQT
QKSLDEHKTN LNENDANEIQ NAINALKDCV KNDNATKAEL EDKTKLLAQA AQKLGEAMAN
KNNAEQPKKK DDDVIDAEVE
