ID   DNAK_CHLPM              Reviewed;         635 AA.
AC   A4SFB1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Cvib_1158;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
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., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) 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; CP000607; ABP37170.1; -; Genomic_DNA.
DR   RefSeq; WP_011890393.1; NC_009337.1.
DR   AlphaFoldDB; A4SFB1; -.
DR   SMR; A4SFB1; -.
DR   STRING; 290318.Cvib_1158; -.
DR   EnsemblBacteria; ABP37170; ABP37170; Cvib_1158.
DR   KEGG; pvi:Cvib_1158; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079236"
FT   REGION          594..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..635
FT                   /note="Basic and acidic 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   635 AA;  68685 MW;  9AE885D82AA18CDB CRC64;
     MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGNRTTPSMV AFTKNGDRLV GQAAKRQAIT
     NPTNTIFSIK RFVGRKFDEV PNEKKIAPYA VVNEGGEARV KINDKTYSPQ EISAMILQKM
     KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGRIAGL EVKRIINEPT AAALAYGLDK
     KTSSEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQKII DFLADEFKKQ
     EGIDLRNDPI ALQRLKEAGE KAKIELSSRT DTEINLPFIT ATQEGPKHLV INLTRAKFEG
     ICADLFAKIL EPCQRAVKNS KVPMKEIDEI VLVGGSTRIP KVQALVKDFF GKEPNKSVNP
     DEVVAVGAAI QGGVLKGDVT DVLLLDVTPL SLGIETLGGV MTKLIDANTT IPTKKQEVFS
     TAGDNQTSVE VHVLQGERSM ATDNKTLGRF HLGDIPPAPR GLPQIEVAFD IDSNGILHVS
     AKDKATGKEQ SIKIEASSKL TDAEIEKMKE DAKAHAEEDK KLKEEIDIKN SADALIFSTE
     KQLEELGDKI PADKRPAIDG ALEKLKDAHK NGTTETIQSG MEELSKVWSE VAADLYKEEP
     QGNPEGGSAP EGEKKGDDGS VENAEYEVID GDDKK