DNAK_BUCAI
ID DNAK_BUCAI Reviewed; 637 AA.
AC O32464;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=BU153;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9276669; DOI=10.1093/oxfordjournals.jbchem.a021738;
RA Sato S., Ishikawa H.;
RT "Structure and expression of the dnaKJ operon of Buchnera, an intracellular
RT symbiotic bacteria of aphid.";
RL J. Biochem. 122:41-48(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; D88673; BAA21964.1; -; Genomic_DNA.
DR EMBL; BA000003; BAB12871.1; -; Genomic_DNA.
DR RefSeq; NP_239985.1; NC_002528.1.
DR RefSeq; WP_009874109.1; NC_002528.1.
DR AlphaFoldDB; O32464; -.
DR SMR; O32464; -.
DR STRING; 107806.10038836; -.
DR PRIDE; O32464; -.
DR EnsemblBacteria; BAB12871; BAB12871; BAB12871.
DR KEGG; buc:BU153; -.
DR PATRIC; fig|107806.10.peg.163; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001806; 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_0000078433"
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:0000250"
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