ID   DNAK_ACTP7              Reviewed;         632 AA.
AC   B3H2X7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=APP7_1995;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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; CP001091; ACE62647.1; -; Genomic_DNA.
DR   RefSeq; WP_005609378.1; NC_010939.1.
DR   AlphaFoldDB; B3H2X7; -.
DR   SMR; B3H2X7; -.
DR   EnsemblBacteria; ACE62647; ACE62647; APP7_1995.
DR   KEGG; apa:APP7_1995; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; APLE537457:APP7_RS10430-MON; -.
DR   Proteomes; UP000001226; 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..632
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119658"
FT   REGION          601..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;  EF45953A2101F117 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 IEKMVRDAEA NAEADKKFEE LVQARNQADG
     IAHATRKQIE EAGDALNADD KAKIEAAIAD LEKAAKGDDK AEIDAKTEAL IKASEPLMQA
     AQAKAQAGEQ PQQSAKDDGV VDAEFEEVKD NK