ID   DNAK_CHLPD              Reviewed;         640 AA.
AC   A1BET8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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};
GN   OrderedLocusNames=Cpha266_0864;
OS   Chlorobium phaeobacteroides (strain DSM 266).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) 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; CP000492; ABL64915.1; -; Genomic_DNA.
DR   RefSeq; WP_011744743.1; NC_008639.1.
DR   AlphaFoldDB; A1BET8; -.
DR   SMR; A1BET8; -.
DR   STRING; 290317.Cpha266_0864; -.
DR   PRIDE; A1BET8; -.
DR   EnsemblBacteria; ABL64915; ABL64915; Cpha266_0864.
DR   KEGG; cph:Cpha266_0864; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008701; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059535"
FT   REGION          547..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..618
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   640 AA;  69142 MW;  62291CB13E968FEA CRC64;
     MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGNRTTPSMV AFTKSGDRLV GQAAKRQAIT
     NPKNTIYSIK RFVGRKFDEV PNEKKLAPYD IVNEGGEARV KINDKAYSPQ EISAMILQKM
     KQTAEDFLGE KVSEAVITVP AYFNDAQRQA TKDAGRIAGL DVKRIINEPT AAALAYGLDK
     KQSSEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQKII NFLADEFKKQ
     EGIDLRNDAI ALQRLKEAAE KAKVELSSRT DTEINLPFIT ATQEGPKHLV INLTRAKFEA
     MCSDLFDKIL EPCHRAVKNS SVEIKDIDEV VLVGGSTRIP KVQALVKEFF GREPNKSVNP
     DEVVAVGAAI QGGVLKGDVT DVLLLDVSPL SLGIETLGGV MTRLIEANTT IPTRKQEVFS
     TAGDNQTSVE VHVLQGERPM ASDNKTLGRF HLGDIPPAPR GLPQIEVTFD IDSNGILSVS
     AKDKATGKEQ SIKIEASGKL SDAEIEKMKR DAKEHAAEDM KKKEEIDSKN AADGLIFSTE
     KQLAELGDKI PSDKRPALEG ALEKLKDATK NGTTESIKNA MDELSKVWND VSSNLYQAPG
     AETNASEPTQ NTDGSGHTKK SGNDGEVENA EFEVIDGNGK