DNAK_BUCAT
ID DNAK_BUCAT Reviewed; 637 AA.
AC B8D758;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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};
GN OrderedLocusNames=BUAPTUC7_152;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=561501;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuc7;
RX PubMed=19150844; DOI=10.1126/science.1167140;
RA Moran N.A., McLaughlin H.J., Sorek R.;
RT "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT bacteria.";
RL Science 323:379-382(2009).
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; CP001158; ACL29973.1; -; Genomic_DNA.
DR RefSeq; WP_009874109.1; NC_011834.1.
DR AlphaFoldDB; B8D758; -.
DR SMR; B8D758; -.
DR KEGG; bau:BUAPTUC7_152; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133136"
FT REGION 599..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..637
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 637 AA; 70042 MW; 838C8C215A648BDE CRC64;
MGKIIGIDLG TTNSCVAIMD GNKPRVLENA EGDRTTPSII AYTQEGEVLV GQPAKRQAIT
NPKNTLFAIK RLIGRKFKDD EVQRDIKIMP YNIVNSDNGD AWIDVKKQKM APPQISAEVL
KKMKKTAEDY LGETIKEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKGKGNRTI AVYDLGGGTF DISIIEIDEV DKEKTFEVLA TNGDTHLGGE DFDSRLINYL
VTEFKKEQGI DLRNDPLSMQ RLKESAEKAK IELSSAQQTD VNLPYITADS NGPKHLNIKV
TRAKLESLVE DLILRSIEPL KVALKDAGLS VTDINDVILV GGQTRMPMVQ SKVADFFGKE
PRKDVNPDEA VAVGAAVQGG VLSGDVKDVL LLDVTPLSLG IETMGGIMTS LINKNTTIPT
KHSQIFSTAE DNQSAVTIHV LQGERKRSSD NKSLGQFNLD GINPAPRGTA QIEVTFDIDS
DGILHVSAKD KKTGKEQKIT IKASSGLNEE EIKKMVNDAE ANSEADQKFE ELIQTRNQGD
QLVHSIKKQL NENKNSIEEE SKKDIQLALN KLENALKGED KSDIEKNIQN LLKISSKLTE
INQKKSEKDQ KDNNMSANKK DENVVDAEFE EIKDPKK