DNAK_CHLP8
ID DNAK_CHLP8 Reviewed; 638 AA.
AC B3QMB2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Cpar_0645;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
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., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-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; CP001099; ACF11065.1; -; Genomic_DNA.
DR RefSeq; WP_012501898.1; NC_011027.1.
DR AlphaFoldDB; B3QMB2; -.
DR SMR; B3QMB2; -.
DR STRING; 517417.Cpar_0645; -.
DR EnsemblBacteria; ACF11065; ACF11065; Cpar_0645.
DR KEGG; cpc:Cpar_0645; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008811; 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..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119685"
FT REGION 592..638
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 638 AA; 69083 MW; 24FD933EDB56C749 CRC64;
MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGYRTTPSMV AFTKTGERLI GQAAKRQAVT
NPKNTIFSIK RFMGRKYDEV PNEKKFASYD VVNEGGDARV KIGEKSYSPQ EISAMILQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGKIAGL EVKRIINEPT AAALAYGLDK
KKENEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQVII DYLADEFKKQ
EGIDLRKDAI ALQRLKEAAE KAKIELSSRT DTEINLPFIT ATQEGPKHLV INLTRAKFEA
MSATLFDKVL EPCRRALKNS KLDMKEIDEV VLVGGSSRIP KVQALVKEFF GKEPNKSVNP
DEVVAIGAAI QGGVLQGDVT DVLLLDVTPL SLGIETLGGV MTKLIEANST IPTRKQETFS
TAADNQTSVE VHVLQGERPM ASDNKTLGRF HLGDIPPAPR GIPQIEVTFD IDANGILNVS
AKDKATGKEQ SIKIEASGKL TEAEIEKMKE DAKAHADEDQ KRKEEIDLKN SADSLIFSTE
KQLSELGDKL PADKKAEIES ALEKLKEAHK AGSADAIKPA MDELSKVWSE AASNLYQQPG
AEAGAAPQPE TNGQQESKGG DGAVNAEYEV IDGDDDKK