DNAK_METFK
ID DNAK_METFK Reviewed; 640 AA.
AC Q1H3B8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Mfla_0751;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
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 Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-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; CP000284; ABE49019.1; -; Genomic_DNA.
DR RefSeq; WP_011479116.1; NC_007947.1.
DR AlphaFoldDB; Q1H3B8; -.
DR SMR; Q1H3B8; -.
DR STRING; 265072.Mfla_0751; -.
DR PRIDE; Q1H3B8; -.
DR EnsemblBacteria; ABE49019; ABE49019; Mfla_0751.
DR KEGG; mfa:Mfla_0751; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002440; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059601"
FT REGION 603..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 69317 MW; 634F1F95953FA155 CRC64;
MGKIIGIDLG TTNSCVAVME GGKPRVIENA EGARTTPSVI AYQEDGEILV GAPAKRQAVT
NPKNTLFAVK RLIGRRFDEK EVQKDIGLMP YTITKADNGD AWVEVRGQKL APPQISAEVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
LDKQEGDRKI AVYDLGGGTF DISIIEISEI DGEHQFEVLS TNGDTFLGGE DFDNRLIDFL
ADEFKKENGI DLRNDLLAKQ RLKEAAEKAK IELSSSTQTE VNLPYITADA SGPKHLVVKI
TRAKFESLVE DLIERSIKPC EVALKDAGVK VSDIQDVILV GGQTRMPKVQ EKVKEFFGKE
PRKDVNPDEA VAVGAAIQGG VLQGDVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTIPT
KASQVFSTAE DNQSAVTIHV LQGEREMASG NKSLGQFNLT DIPPAPRGMP QIEVTFDIDA
NGILHVSAKD KATGKENKIT IKANSGLSDE EIKRMEEEAA KYADEDKKLR ELVDARNSAD
SAIHSVKKSL AEHGDKLDAA EKGAIEKAVQ ELEDVIKGDD KAAIESKTNA LIEASQKLGE
KVYAAGETES SAAEPGEPQE KTVDAEVVDA EFEEVKDDKK