DNAK_MARMM
ID DNAK_MARMM Reviewed; 636 AA.
AC Q0AKB1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Mmar10_3001;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-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; CP000449; ABI67282.1; -; Genomic_DNA.
DR RefSeq; WP_011644926.1; NC_008347.1.
DR AlphaFoldDB; Q0AKB1; -.
DR SMR; Q0AKB1; -.
DR STRING; 394221.Mmar10_3001; -.
DR PRIDE; Q0AKB1; -.
DR EnsemblBacteria; ABI67282; ABI67282; Mmar10_3001.
DR KEGG; mmr:Mmar10_3001; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001964; 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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059598"
FT REGION 600..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="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 636 AA; 68735 MW; 5161A17B9ACF1D5E CRC64;
MSKVIGIDLG TTNSCVAVME SGQPKVIENS EGVRTTPSVV AFTEDGERLI GQPAKRQAVT
NPDYTFFAIK RLIGRMMDDP TVKKDIDMVP YKIVPSDSND AWVQGRDKKY SPSEISAFTL
QKMKETAESY LGEKVEKAVI TVPAYFDDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKGENKTIA VFDLGGGTFD VSVLEIGDGV FEVKATNGDT FLGGEDFDMR IVQYLADEFK
KENGIDLKSD KLALQRLKEE AEKAKKELSS ATSYEVNLPF ITADASGPKH LNIKLSRAKL
EALVEDLVKR TLEPCKKALK DAGLSPSDID DIVLVGGMTR MPKVQEAVKG FFGKDPHKGV
NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQT
FSTADDNQTA VTIRVSQGER EMAADNKLLG QFDLVGIPPS PRGLPQIEVT FDIDANGIVN
VSAKDKATGK EQQIRIQASG GLSDDDIEQM VKDAEANADA DKKKKELVEA HNGAEAMIHQ
TEKQLEEFGD KVPGEDKDAI DAALTELKEV KDGEDLEAIQ QKTQALVQAA MKLGEAMYAA
QQTEAAEADA KSDAEGDEDV VDAEFSEVDD DKKKDA