ID   DNAK_AZOPC              Reviewed;         641 AA.
AC   B6YRF7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, 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=CFPG_516;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(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; AP010656; BAG83779.1; -; Genomic_DNA.
DR   RefSeq; WP_012573540.1; NC_011565.1.
DR   AlphaFoldDB; B6YRF7; -.
DR   SMR; B6YRF7; -.
DR   STRING; 511995.CFPG_516; -.
DR   EnsemblBacteria; BAG83779; BAG83779; CFPG_516.
DR   KEGG; aps:CFPG_516; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000723; 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..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119664"
FT   REGION          604..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69158 MW;  3C5E215C16AD7722 CRC64;
     MGKIIGIDLG TTNSCVAVME GGKPVVIPNS EGKMTTPSIV AFVGSERKIG DPAKRQAITN
     PTKTIFSIKR FMGESYDKVQ NEINRIPYKV TRGGNDTSRV DIDGRLYSPQ EISAMILQKM
     KKTAEDYLGQ EVTEAVITVP AYFGDSQRQA TIEAGEIAGL KVKRIINEPT AAALAYGLEK
     ADKDMKIAVF DLGGGTFDIS ILELGSGVFE VLSTNGDTHL GGDDFDHVII DFLADEFQRN
     EGLDLRKDAM AMQRLKEAAE KAKIELSSST STEINLPYIM PVDGMPKHLI VTLTRSKFEQ
     LSDKLIRSTV DPCEKALKGA GLTAKDINEI ILVGGSTRIP IIQTEVEKIF GKVPSKGVNP
     DEVVAVGAAI QGAILSGDSN LGEMVLLDVT PLSLGIETMG SVMTKLIEAN STIPIKKSET
     FTTAADNQPS VEIHVLQGER PLAKDNKTIG KFHLDGIMPA PRGIPQIEVT FDIDANGVVS
     VSAKDKATGK EQSIRIEASS GLSEAEIKRM KEEATANAEA DTKAKERVDK LNHADSVIFQ
     TEKQLKDFGD KIPADKKASI EATLTKLKEA HKAQDLSSID TIIAEINNTF QAMSQELYNA
     KAQTNNSAGN NNSAGNNTQN NNNASDNNNN NVTDVDFEEV K