ID   DNAK_RHOP5              Reviewed;         633 AA.
AC   Q07US6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=RPE_0349;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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; CP000463; ABJ04308.1; -; Genomic_DNA.
DR   RefSeq; WP_011661802.1; NC_008435.1.
DR   AlphaFoldDB; Q07US6; -.
DR   SMR; Q07US6; -.
DR   STRING; 316055.RPE_0349; -.
DR   EnsemblBacteria; ABJ04308; ABJ04308; RPE_0349.
DR   KEGG; rpe:RPE_0349; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 161217at2; -.
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..633
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059644"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   633 AA;  68351 MW;  150F3260A3433285 CRC64;
     MGKVIGIDLG TTNSCVAVMD GKTPKVIENA EGMRTTPSIV AFSDDGERLV GQPAKRQAVT
     NPERTFFAVK RLIGRRYDDP MVEKDKKLVP YKIVKASNGD AWVEADANTY SPSQVSAFIL
     QKMKETAEAH LGAKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKAKAGVIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVSYLADEFQ
     KEQGINLRND KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQTGPKH LTMKLTRAKF
     EALVDDLVQK TIEPCRKALK DAGLTAGEIG EVVLVGGMTR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIDRN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKVLG QFDLMGIPPS PRGMPQIEVT FDIDANGIVN
     VSARDKATGK EQQIRIQASG GLSEADIDKM VKDAEINAAE DKKRREAVDA KNHADALVHS
     TEKALAEHGA KVEEPERRAI EDALSDLREA LKGDDAEAIK TKTNTLAQAS MKLGEAMYKQ
     QAEADAAKDA AKDDVVDAEF TEVDDDKNTK KSA