DNAK_METS4
ID DNAK_METS4 Reviewed; 639 AA.
AC B0UR84;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=M446_6270;
OS Methylobacterium sp. (strain 4-46).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4-46;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL Submitted (FEB-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}.
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DR EMBL; CP000943; ACA20536.1; -; Genomic_DNA.
DR RefSeq; WP_012335914.1; NC_010511.1.
DR AlphaFoldDB; B0UR84; -.
DR SMR; B0UR84; -.
DR STRING; 426117.M446_6270; -.
DR PRIDE; B0UR84; -.
DR EnsemblBacteria; ACA20536; ACA20536; M446_6270.
DR KEGG; met:M446_6270; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
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..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119731"
FT REGION 601..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..639
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 639 AA; 68742 MW; EECBBCB2B76A9819 CRC64;
MGKVIGIDLG TTNSCVAVME GTQPKVIENA EGARTTPSIV AFTDEGERLV GQPAKRQAVT
NPSRTFFAIK RLIGRTYDDP MTQKDKGLVP YHIVRAGNGD AWVEADGKQF SPSQISAFTL
QKMKETAESY LGQPVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKKKSGVIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDNR IVEYLAAEFK
REQGIDLTRD KLALQRLKEA AEKAKIELSS ATQTEINLPY ITADASGPKH LALKLSRAKF
ESLVDDLIQR TIEPCRKALK DAGVAASEID EVVLVGGMTR MPKIQDVVKT FFGKEPHKGV
NPDEVVAIGA AVQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
FSTAEDNQNA VTIRVFQGER EMAADNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVN
VTAKDKATGK EHQIRIQASG GLSDTEIQRM VQEAEANAAE DKKRRELVEV KNQGESLVHA
TEKSVKEYGD KVSESDRAGI STAIDALRQA LAGEDVETIK ARTTDLMQAS MKLGEAMYAA
QAGGGEAASA GAEDPQAKKD DVIDADFQEV DDKDHKKRA