DNAK_PSEU2
ID DNAK_PSEU2 Reviewed; 638 AA.
AC Q4ZNP7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-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=Psyr_4195;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY39225.1; -; Genomic_DNA.
DR RefSeq; WP_003400158.1; NC_007005.1.
DR RefSeq; YP_237263.1; NC_007005.1.
DR AlphaFoldDB; Q4ZNP7; -.
DR SMR; Q4ZNP7; -.
DR STRING; 205918.Psyr_4195; -.
DR PRIDE; Q4ZNP7; -.
DR EnsemblBacteria; AAY39225; AAY39225; Psyr_4195.
DR KEGG; psb:Psyr_4195; -.
DR PATRIC; fig|205918.7.peg.4322; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000426; 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..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225999"
FT REGION 605..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68775 MW; AD429D7BFC54DFCE CRC64;
MGRIIGIDLG TTNSCVSILE NGNVKVIENA EGTRTTPSII AYANDGEILV GQSAKRQAVT
NPHNTLYAVK RLIGRKFEED VVQKDIQMVP YKIVKADNGD AWVEVNGQKM APPQISAEIL
KKMKKTAEDY LGEAVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDIRLIDYF
VDEFKKESGM NLKGDPLAMQ RLKEAAEKAK IELSSSTQTE VNLPYITADA TGPKHLVVKI
SRSKLESLVE DLVQRTIAPC EMALKDAGID RSKINDVILV GGQTRMPLVQ KLVTEFFGKE
ARKDVNPDEA VAMGAAIQGA VLAGDVKDVL LLDVSPLTLG IETMGGVMTA LIEKNTTIPT
KKSQVFSTAD DNQNAVTIHV LQGERKQAAQ NKSLGKFDLA EIPPAPRGVP QIEVTFDIDA
NGILHVGAKD KATGKQQSIV IKANSGLSEE EIQQMVRDAE VNSEEDRKFE ELASARNQGD
ALVHSTRKMI ADAGDKVTAE EKTAVEAALV ALEAAIKGDD KAAIEAKVEE LSKVSAPIAQ
KMYAEQAENP DAAAKPAEET AKADDVVDAE FEEVKDHK