DNAK_METPP
ID DNAK_METPP Reviewed; 653 AA.
AC A2SIR4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Mpe_A2498;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95453.1; -; Genomic_DNA.
DR RefSeq; WP_011830086.1; NC_008825.1.
DR AlphaFoldDB; A2SIR4; -.
DR SMR; A2SIR4; -.
DR STRING; 420662.Mpe_A2498; -.
DR PRIDE; A2SIR4; -.
DR EnsemblBacteria; ABM95453; ABM95453; Mpe_A2498.
DR KEGG; mpt:Mpe_A2498; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000366; 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..653
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059602"
FT REGION 613..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 653 AA; 69995 MW; BB5241CCDCB7C0ED CRC64;
MAKIIGIDLG TTNSCVAIME GNTTKVIENS EGARTTPSII AYQEDGEVLV GASAKRQAVT
NPRNTLYAVK RLIGRKFTEK EVQKDIDLMP YTIAAAENGD AWVEVRGNKL APPQVSAEVL
RKMKKTAEDY LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKHNDGKGG DRKIAVYDLG GGTFDISIIE IADVDGEMQF EVLSTNGDTF LGGEDFDQRV
IDYIIAEFKK EQGVDLSKDV LALQRLKEAA EKAKIELSNS TQTDINLPYV TADASGPKHL
NIKLTRAKLE ALVEELIERT IAPCRTAIKD AGVSTSQIND VILVGGMTRM PKVQEKVKEF
FGQEPRKDVN PDEAVAVGAA IQGQVLAGDR KDVLLLDVTP LSLGIETLGG VMTKMITKNT
TIPTKFAQTF STADDNQPAV TIKVFQGERE LASGNKMLGE FNLEGIAPAP RGMPQIEVSF
DIDANGILHV GAKDKGTGKE NKITIKANSG LSEEEIQKMV KDAELNAAED KKKLELVQAR
NQADAMVHSV KKSLAEHGDK LDAGEKEKIE SALKDAETAL KGEDKAEIEA KTEALMSASQ
KLGEKVYADM QAAQAAAGAA AGGGEAPAAE ATASKPADDN VVDAEFKEVK DQK