ID   DNAK_METNO              Reviewed;         637 AA.
AC   B8IHL3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Mnod_6931;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) 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; CP001349; ACL61676.1; -; Genomic_DNA.
DR   RefSeq; WP_015933240.1; NC_011894.1.
DR   AlphaFoldDB; B8IHL3; -.
DR   SMR; B8IHL3; -.
DR   STRING; 460265.Mnod_6931; -.
DR   PRIDE; B8IHL3; -.
DR   EnsemblBacteria; ACL61676; ACL61676; Mnod_6931.
DR   KEGG; mno:Mnod_6931; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008207; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133153"
FT   REGION          600..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..637
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   637 AA;  68509 MW;  2A1B9DD18EA20A1F CRC64;
     MGKVIGIDLG TTNSCVAVME GTQPKVIENA EGARTTPSIV AFTDDGERLV GQPAKRQAVT
     NPSRTFFAIK RLIGRTYDDP MTQKDKGLVP YAITRAGNGD AWVAADGKQF SPSQISAFTL
     QKMKETAESY LGQPVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKRKSGVIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDNR IVEYLAAEFK
     REQGIDLTKD KLALQRLKEA AEKAKIELSS ATQTEINLPY ITADASGPKH LALKLSRAKF
     ESLVDDLIQR TIEPCRKALK DAGVSANEID EVVLVGGMTR MPKIQDVVKT FFGKEPHKGV
     NPDEVVAIGA AVQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVN
     VTAKDKATGK EHQIRIQASG GLSETEIQRM VQEAEANAAE DKKRRELVEV KNQGESLIHA
     TEKSVKEYGD KVSEADKAGI TTAIDALRQA LAGEDVETIK ARTTDLMQAS MKLGEAMYAA
     SQGAGPEAGA DQAQAKKDDV IDADFQEVDD KDQKKRA