ID   DNAK_RHOP2              Reviewed;         633 AA.
AC   Q2J320;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=RPB_0429;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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; CP000250; ABD05140.1; -; Genomic_DNA.
DR   RefSeq; WP_011439330.1; NC_007778.1.
DR   AlphaFoldDB; Q2J320; -.
DR   SMR; Q2J320; -.
DR   STRING; 316058.RPB_0429; -.
DR   PRIDE; Q2J320; -.
DR   EnsemblBacteria; ABD05140; ABD05140; RPB_0429.
DR   KEGG; rpb:RPB_0429; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008809; 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..633
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059643"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   633 AA;  68384 MW;  6C3F6184074C7077 CRC64;
     MGKVIGIDLG TTNSCVAVMD GKNSKVIENA EGMRTTPSIV AFSDDGERLV GQPAKRQAVT
     NPERTFFAVK RLVGRRYDDP MVEKDKKLVP YKIVKASNGD AWVEADGQTY SPSQVSAFIL
     QKMKETAEAH LGQKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKTKAGTIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVSYLADEFQ
     KEQGINLRND KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQSGPKH LTMKLTRAKF
     EALVDDLVQK TIEPCRKALK DAGLTAGEIG EVVLVGGMTR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIERN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKILG QFDLMGIPPA PRGMPQIEVT FDIDANGIVN
     VSAKDKATGK EQQIRIQASG GLSDSDIDKM VKDAEANAAE DKKRREAVDA KNHADALVHS
     TEKALAEHGS KVAEPERRAI EDALSDLRES LKSDDAEVIK AKTNTLAQAS MKLGEAMYTQ
     QAESDAAKHA AKDDIVDADF TEVDDDKNNK KSA