DNAK_SODGM
ID DNAK_SODGM Reviewed; 636 AA.
AC Q2NVZ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SG0409;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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; AP008232; BAE73684.1; -; Genomic_DNA.
DR RefSeq; WP_011410272.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NVZ1; -.
DR SMR; Q2NVZ1; -.
DR STRING; 343509.SG0409; -.
DR PRIDE; Q2NVZ1; -.
DR EnsemblBacteria; BAE73684; BAE73684; SG0409.
DR KEGG; sgl:SG0409; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; SGLO343509:SGP1_RS03795-MON; -.
DR Proteomes; UP000001932; 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 Stress response.
FT CHAIN 1..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059672"
FT REGION 606..636
FT /note="Disordered"
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 636 AA; 68845 MW; 00836D25505ECDC5 CRC64;
MGKIIGIDLG TTNSCIAIIE GSKPRVLENS EGDRTTPSII AYTQDGEILV GQPAKRQSVT
NPQNTLFAIK RLIGRRYQDE EVQRDVSIMP YKIVAADNGD AWLEVKGQKM APPQISAEIL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDTQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
LDKETGNRTI AVYDLGGGTF DISIIEIDDV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
VDEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADG SGPKHMNLKV
TRAKLESLVE ELVNRTLEPL KVALKDAGLS VSDIKDVILV GGQTRMPLVQ KKVTDFFGKE
PRKDVNPDEA VAIGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTP LIAKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRSGD NKSLGQFNLD GISPAMRGTP QIEVTFDIDA
DGILHVSAKD KNSGREQKIT IKASSGLNEE EIQKMVQEAE ANAESDRKFE ALVQTRNQAD
HLLHSTRKQL EDAGDKLPAD DKTAIEDALK NLDTVLKGED KADIEAKMQA LIQVSGKLLE
VAQQQAQAAG DGGADGSAKA DDDVVDAEFE EVKDKK