ID   DNAK_ACTP2              Reviewed;         632 AA.
AC   A3N3K0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=APL_1906;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74986.1; -; Genomic_DNA.
DR   RefSeq; WP_005599634.1; NC_009053.1.
DR   AlphaFoldDB; A3N3K0; -.
DR   SMR; A3N3K0; -.
DR   STRING; 416269.APL_1906; -.
DR   EnsemblBacteria; ABN74986; ABN74986; APL_1906.
DR   GeneID; 66258701; -.
DR   KEGG; apl:APL_1906; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001432; 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..632
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059500"
FT   REGION          599..632
FT                   /note="Disordered"
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   632 AA;  67941 MW;  5F5F953A211BF11C CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKARVIENA EGARTTPSII AYTDNETLVG QPAKRQAITN
     PKNTLFAIKR LIGRRFESEE VQRDIKIMPF EITRADNGDA WVNVKGDKLA PPQISAEVLK
     KMKKTAEDFL GEAVTEAVIT VPAYFNDAQR QATIDAGRIA GLDVKRIINE PTAAALAFGL
     GSTKENQVIA VYDLGGGTFD ISIIEIDNFD GEQTFEVLAT GGNTHLGGED FDNRVIDYII
     DEFKKEQGVD LRNDPMALQR VKEAAEKAKI ELSSAQSTEV NLPYITADAT GPKHLAINVT
     RAKLEALVED LVASSIESLK TVLKDAGKSV NEINDIILVG GQTRMPLVQQ KVAEFFGKEA
     RKDVNPDEAV AIGAAVQGGV LKGDVKDVLL LDVTPLSLGI ETMGGVMTVL IEKNTTIPTK
     KSQVFSTAED NQSAVTIHVL QGERKQASAN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN
     GVINVSAKDK NTGKEQQIRI QASSGLSDEE IEQMVRDAEA NAEADKKFEE LVQARNQADG
     IAHATRKQIE EAGDALNADD KAKIEAAIAD LEKAAKGDDK AEIDAKTEAL IKASEPLMQA
     AQAKAQAGEQ PQQSAKDDGV VDAEFEEVKD NK