ID   DNAK_PSEA7              Reviewed;         637 AA.
AC   A6VCL8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=PSPA7_5481;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR86569.1; -; Genomic_DNA.
DR   RefSeq; WP_012077495.1; NC_009656.1.
DR   AlphaFoldDB; A6VCL8; -.
DR   SMR; A6VCL8; -.
DR   PRIDE; A6VCL8; -.
DR   EnsemblBacteria; ABR86569; ABR86569; PSPA7_5481.
DR   KEGG; pap:PSPA7_5481; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001582; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059631"
FT   REGION          604..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..637
FT                   /note="Basic and acidic residues"
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   637 AA;  68333 MW;  56E8FDD507D486A2 CRC64;
     MGKIIGIDLG TTNSCVAILE NGNVKVIENA EGARTTPSII AYTNDGETLV GQPAKRQAVT
     NPQNTLYAVK RLIGRRFEEN VVQKDIQMVP YSIVKADNGD AWVEVKGQKM APPQISAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     LDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDIRLIDYL
     VDEFKKESGI NLKGDPLAMQ RLKEAAEKAK IELSSTQQTD VNLPYVTADA SGPKHLNVKV
     SRAKLESLVE DLVQRTIEPC RTALKDAGLD VSDIHEVILV GGQTRMPLVQ KTVAEFFGKE
     ARKDVNPDEA VAVGAAIQGA VLAGDVKDVL LLDVTPLTLG IETLGGVMTG LIEKNTTIPT
     KKSQVFSTAD DNQGAVTIHV LQGERKQAAQ NKSLGKFDLA DIPPAPRGVP QIEVTFDIDA
     NGILHVSAKD KATGKQQSIV IKASSGLSED EIQQMVRDAE ANAEEDRKFE ELAAARNQGD
     ALVHATRKMI TEAGDKATAE DKATIEKALG ELEVAVKGDD KAEIEAKMNA LSQASAPLAQ
     KMYAEQAQQG EGAAQGEQAK SADDVVDAEF EEVKDNK