ID   DNAK_AMOA5              Reviewed;         632 AA.
AC   B3ERN8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Aasi_0481;
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2;
RX   PubMed=20023027; DOI=10.1128/jb.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(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; CP001102; ACE05890.1; -; Genomic_DNA.
DR   RefSeq; WP_012472654.1; NC_010830.1.
DR   AlphaFoldDB; B3ERN8; -.
DR   SMR; B3ERN8; -.
DR   STRING; 452471.Aasi_0481; -.
DR   PRIDE; B3ERN8; -.
DR   EnsemblBacteria; ACE05890; ACE05890; Aasi_0481.
DR   KEGG; aas:Aasi_0481; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001227; 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; 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_1000119662"
FT   REGION          597..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..622
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   632 AA;  68377 MW;  CE8BF7998B8B6EF8 CRC64;
     MGKIIGIDLG TTNSCVAVME GNEPVVIANS EGKRTTPSVV AFLNEGQGER KVGDAAKRQA
     IINPQNTISS IKRFMGKRYS DIAEESKLVP YQLEKGNNDT VRVRIGDRTY TPQEISAMIL
     QKMKTTAEDY LGTTVKEAVI TVPAYFNDAE RQATKEAGQI AGLEVKRIIN EPTAAALAYG
     LDKKNQDMKI AVFDLGGGTF DISILELGDG VFEVKSTNGD VHLGGDNFDQ KLIDWLAEEF
     KKEESVDLRK DPTALQRLKE AAEKAKIELS GSSTTEVNLP YITAIDGVPK HLVKKITRAQ
     FEQLVDGLVR RTLEPCKKAM QDAGLTVADI DEVILVGGST RIPKIQEEVE KFFNKKPSKG
     VNPDEVVAVG AAIQGGVLTG EVKDVLLLDV IPLSFGIETL GGVYTKLIEA NTTIPTKKSE
     VFSTAADSQS SVEIHVLQGE RAMARDNRTI GKFHLDGIPP APRGIPQIEV TFDIDANGIL
     NVSAKDKGTG KEQKIRIEAS SGLTDEEIKK MKQEAEANAE ADKQEREKVD KLNTADATIF
     QAQKQLQELG DKIPADTKKS AEDAIEELKK AHEAKDIAAI DTAMSKVNAA LQQLYAAAQQ
     AGQAEGQAAQ EPSQSTGNAQ AEATDAEYEE VK