ID   DNAK_RHOCS              Reviewed;         640 AA.
AC   B6IVA4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=RC1_2858;
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW;
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000613; ACJ00228.1; -; Genomic_DNA.
DR   RefSeq; WP_012568008.1; NC_011420.2.
DR   AlphaFoldDB; B6IVA4; -.
DR   SMR; B6IVA4; -.
DR   STRING; 414684.RC1_2858; -.
DR   EnsemblBacteria; ACJ00228; ACJ00228; RC1_2858.
DR   KEGG; rce:RC1_2858; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001591; 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   Reference proteome; Stress response.
FT   CHAIN           1..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119747"
FT   REGION          600..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   640 AA;  68509 MW;  769E8CD2A8F2856C CRC64;
     MSKVIGIDLG TTNSCVAIME GTQAKVIENA EGARTTPSMV AFTQGGERLV GQPAKRQAVT
     NPENTFFAIK RLIGRRYDDP LTQKDKGLVP YRIVGGKNGD AWVESHGKQY SPSEISAFIL
     QKMKETAENY LGEKVTQAVI TVPAYFNDSQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     MEKKGTGTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDAK IIDYLAEEFQ
     KEQGIDLRKD RLALQRLKEA AEKAKIELSA SMQTEVNLPF ITADASGPKH LNIKLTRSKL
     EALVDDLVRR TIEPCKAALK DAGLKASEID EVILVGGMTR MPKIIETVKQ FFGREPHRGV
     NPDEVVAVGA AIQGGVLKGE VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
     FSTAEDNQTA VTIRVFQGER EMAADNKMLG QFDLMGIPSA PRGVPQIEVT FDIDANGIVN
     VSAKDKATGK EQTIRIQASG GLSDADIDRM VKDAEAHAAE DKKRRELVEA RNQADGLIHT
     TERTLSENGD KLPGAEKSAA EAAIAELRTA MAADDVADIK AKTDALAQAS MKLGEALYKA
     GQETGGPGAP GGDSGASEAG GEKVVDADFE EVDDDRKKSA