DNAK_CHLL3
ID DNAK_CHLL3 Reviewed; 637 AA.
AC Q3B577;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Plut_0621;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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; CP000096; ABB23504.1; -; Genomic_DNA.
DR RefSeq; WP_011357379.1; NC_007512.1.
DR AlphaFoldDB; Q3B577; -.
DR SMR; Q3B577; -.
DR STRING; 319225.Plut_0621; -.
DR EnsemblBacteria; ABB23504; ABB23504; Plut_0621.
DR KEGG; plt:Plut_0621; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002709; 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 Stress response.
FT CHAIN 1..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059625"
FT REGION 598..637
FT /note="Disordered"
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 637 AA; 68887 MW; 8BB973B85CB25D9B CRC64;
MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGNRTTPSMV AFTKTGDRLV GQAAKRQAIT
NPKNTIFSIK RFIGRKFDEV PNEKKIAPYE VVNEGGEARV KINDKTYSPQ EVSAMILQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGRIAGL EVKRIINEPT AAALAYGLDR
KQTSEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQKII DFLADEFKKQ
EGVDLRNDAI ALQRLKEAGE KAKVELSSRT DTEINLPFIT ATPEGPKHLV INLTRAKFEG
MCSDLFDKIL EPCRRAVKNS KVEMKDIDEI VLVGGSTRIP KVQALVKEFF GKEPNRSVNP
DEVVAIGAAI QGGVLKGDVT DVLLLDVTPL SLGIETLGGV MTKLIDANTT IPTRKQEVFS
TAGDNQTSVE VHVLQGERPL AVDNKTLGRF HLGDIPPAPR GMPQIEVTFD IDSNGILNVS
AKDKATGKEQ SIKIESSSKL TDAEVEKMKE DAKVHAEEDQ KRKEEIEVKN SADSLIFSTE
KQLSELGEKI PADKKPVIEG ALEKLKDAHK NGTIESIKGA MDELSKVWGE VASNLYQAEA
PGADAPEGQA PQDGGSKKGG EGAVENAEYE VIDGDGK