DNAK_CHLCH
ID DNAK_CHLCH Reviewed; 637 AA.
AC Q3APD2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Cag_1893;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
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 Chlorobium chlorochromatii CaD3.";
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; CP000108; ABB29143.1; -; Genomic_DNA.
DR RefSeq; WP_011362905.1; NC_007514.1.
DR AlphaFoldDB; Q3APD2; -.
DR SMR; Q3APD2; -.
DR STRING; 340177.Cag_1893; -.
DR PRIDE; Q3APD2; -.
DR EnsemblBacteria; ABB29143; ABB29143; Cag_1893.
DR KEGG; cch:Cag_1893; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225950"
FT REGION 503..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..623
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 637 AA; 69037 MW; 1A827FF15A294638 CRC64;
MGKIIGIDLG TTNSCVAVMQ GSQPTVIENS EGNRTTPSVV GFTKTGDRLV GQAAKRQAIT
NPKNTIFSIK RFMGRRFDEV GEEKKMAPYE LINDSGEARV KINDKVYSPQ EISAMVLQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGRIAGL EVKRIINEPT AAALAYGLDK
KNASEKVAVF DLGGGTFDIS ILELGEGVFE VKSTDGDTHL GGDDFDQKII DYIAEEFKKQ
EGIDLRKDAI TLQRLKEAAE KAKIELSSRS DTEINLPFIT ATQEGPKHLV INLTRAKFEA
ISADLFNKVL DPCRRAVKNA KIEMREIDEV VLVGGSTRIP KIQALVKEFF GKEPNKSVNP
DEVVAIGAAI QGGVLKGDVT DVLLLDVTPL SLGIETLGGV MTKLIEANTT IPTKKQEVFS
TASDNQTSVE VHVLQGERPM AADNKTLGRF HLGDIPPAPR GIPQVEVIFD IDANGILHVS
AKDKATGKEQ SIRIEASSKL SDAEINKMKD DAKQHADEDK KRKEEIDIKN SADALIFSTE
KQLTELGEKI PTDKKSALEG SLDKLRDAYK NGTTESIKSA MDDLNSQWNS IASDLYQSGA
GAAQAQPEAP QNSGSSQSSG GDGAVNAEYE VINDDKK