DNAK_RHIL3
ID DNAK_RHIL3 Reviewed; 638 AA.
AC Q1MN11;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=RL0152;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK05641.1; -; Genomic_DNA.
DR RefSeq; WP_011649970.1; NC_008380.1.
DR AlphaFoldDB; Q1MN11; -.
DR SMR; Q1MN11; -.
DR STRING; 216596.RL0152; -.
DR EnsemblBacteria; CAK05641; CAK05641; RL0152.
DR KEGG; rle:RL0152; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006575; 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..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059641"
FT REGION 514..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
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 638 AA; 68448 MW; 0CD59E60DB1587E4 CRC64;
MAKVIGIDLG TTNSCVAVMD GKDAKVIENA EGARTTPSMV AFSDDGERLV GQPAKRQAVT
NPTNTLFAVK RLIGRRYEDP TVEKDKHLVP FTIVKGDNGD AWVEANGKGY SPAQISAMIL
QKMKETAESY LGEKVEKAVI TVPAYFNDAQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
LDKKEGKTIA VYDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDMR LVEYLVGEFK
RDNGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADASGPKH LTLKLTRAKL
ESLVDDLVQR TIAPCKAALK DAGVTAAEID EVVLVGGMSR MPKVQEVVKQ LFGKEPHKGV
NPDEVVALGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQT
FSTAEDNQQA VTIRVSQGER EMAADNKLLG QFDLVGLPPS PRGMPQIEVT FDIDANGIVQ
VSAKDKGTGK EQQIRIQASG GLSDADIEKM VKDAEAHATE DKKRREAVEA RNQAESLIHS
SEKSLKDYGD KVSEADRTAI SDAIAALKTA SEASEPDADD IKAKTQTLME VSMKLGQAIY
EAQQAEGGAA GDASAESGDN VVDADYEEIK DDDRKKSA