(data stored in ACNUC30630 zone)

SWISSPROT: DNAK_RHOPT

ID   DNAK_RHOPT              Reviewed;         631 AA.
AC   B3Q972;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=Rpal_0336;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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}.
DR   EMBL; CP001096; ACE98896.1; -; Genomic_DNA.
DR   RefSeq; WP_011155901.1; NC_011004.1.
DR   SMR; B3Q972; -.
DR   PRIDE; B3Q972; -.
DR   EnsemblBacteria; ACE98896; ACE98896; Rpal_0336.
DR   GeneID; 41374744; -.
DR   KEGG; rpt:Rpal_0336; -.
DR   HOGENOM; HOG000228136; -.
DR   KO; K04043; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; RPAL395960:RPAL_RS01685-MONOMER; -.
DR   Proteomes; UP000001725; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
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   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;
DR   PRODOM; B3Q972.
DR   SWISS-2DPAGE; B3Q972.
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119748"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   631 AA;  67947 MW;  D7E1D678BA6A63EE CRC64;
     MGKVIGIDLG TTNSCVAVMD GKSAKVIENA EGMRTTPSIV AITDDGERLV GQPAKRQAVT
     NPERTFFAVK RLIGRRYDDP MVEKDKGLVP YKIVKASNGD AWVEADGKTY SPSQVSAFIL
     QKMKETAEAH LGQKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKAKTGTIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVNYLADEFQ
     KEQGIDLRKD KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQSGPKH LTMKLTRAKF
     EALVDDLVQK TIEPCRKALK DAGLTAGEIS EVVLVGGMTR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIDRN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKMLG QFDLMGIPPA PRGMPQIEVT FDIDANGIVN
     VSAKDKATGK EQQIRIQASG GLSDSEIDKM VKDAEANAAE DKKRREAVDA KNHADALVHS
     TEKALAEHGS KVDESERRSI EDALSDLREA LKGDDAEAIK AKSNTLAQAS MKLGEAMYKQ
     AEAAGGAQQA GKDDVVDAEF TEVDDDKKKS A
//

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