ID   DNAK_ACTSZ              Reviewed;         635 AA.
AC   A6VNB1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Asuc_1092;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74458.1; -; Genomic_DNA.
DR   RefSeq; WP_012072835.1; NC_009655.1.
DR   AlphaFoldDB; A6VNB1; -.
DR   SMR; A6VNB1; -.
DR   STRING; 339671.Asuc_1092; -.
DR   PRIDE; A6VNB1; -.
DR   EnsemblBacteria; ABR74458; ABR74458; Asuc_1092.
DR   KEGG; asu:Asuc_1092; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001114; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000072031"
FT   REGION          598..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..620
FT                   /note="Polar 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   635 AA;  68421 MW;  8A07A005BAF29307 CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGDRTTPSII AYTNDNETLV GQPAKRQAVT
     NPKNTLFAIK RLIGRRFEDN EVQRDVDIMP FKIIRADNGD AWVDVKGDKL APPQVSAEVL
     KKMKKTAEDF LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     LDKGKGNQTI AVYDLGGGTF DLSIIEIDEV GGEKTFEVLA TNGDTHLGGE DFDNRVINYL
     VDEFKKEQGV DLRNDPLAMQ RLKEAGEKAK IELSSAQQTD VNLPYITADA TGPKHLNIKL
     TRAKLEALVE DLVARSMEPV KVALKDAGLS VSEIDDVILV GGQTRMPLVQ QKVAEFFGKE
     PRKDVNPDEA VAVGAAVQGG VLSGNVTDVL LLDVTPLSLG IETMGGVMTT LIEKNTTIPT
     KKSQVFSTAE DNQSAVTIHV LQGERKQASA NKSLGQFNLE GINPAPRGMP QIEVTFDIDA
     DGIIHVSAKD KGTGKEQQIT IKASSGLSDE EIQQMVRDAE ANADADRKFE ELVQARNQAD
     ALVHATRKQL TEAGDKLSAD DKAPIEKAVS ELEDAVKGDD KDAIEAKSQA LIQVSEKLMQ
     AAQQQAQANT QGQQSQGGND DGVVDAEFEE VKDNK