DNAK_CHLL2
ID DNAK_CHLL2 Reviewed; 639 AA.
AC B3EHR1;
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=Clim_0761;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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; CP001097; ACD89841.1; -; Genomic_DNA.
DR RefSeq; WP_012465721.1; NC_010803.1.
DR AlphaFoldDB; B3EHR1; -.
DR SMR; B3EHR1; -.
DR STRING; 290315.Clim_0761; -.
DR PRIDE; B3EHR1; -.
DR EnsemblBacteria; ACD89841; ACD89841; Clim_0761.
DR KEGG; cli:Clim_0761; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008841; 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..639
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119684"
FT REGION 592..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..639
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 639 AA; 69167 MW; 656ADED7E2621F52 CRC64;
MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGNRTTPSMV AVTKTGDRLV GQAAKRQAIT
NPKNTVFSIK RFMGRKYDEV PNEKKLASYD VINEGGEARV KINDKIYSPQ EVSAMILQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGRIAGL DVKRIINEPT AAALAYGLDK
KMSSEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQKII DYLADEFKKQ
EGIDLRNDAI ALQRLKEAAE KAKVELSSRT DTEINLPFIT ATQEGPKHLV INLTRAKFEA
MCADLFEKIL EPCHRAVKNS KLDMKEIDEV VLVGGSTRIP KVQTLVKEFF GKEPNRSVNP
DEVVAIGAAI QGGVLKGDVT DVLLLDVSPL SLGIETLGGV MTRLIEANTT IPTRKQEVFS
TAADSQTSVE VHVLQGERPM ASDNKTLGRF HLGDIPPAPR GVPQIEVTFD IDSNGILSVS
AKDKATGKEQ TIRIEASGKL NDAEIEKMKQ DAKEHAAEDQ KKKEEIDIRN SADSLIFSTE
KQLTELGDKI PADKKPRLEG SLEKLKEAYK NGTAESIKSA MDDLNKEWSD IASSLYQTPD
AGAPGASGPS AGGEPETGKK GGDGEVQNAE YEVIDGNDK