DNAK_PROA2
ID DNAK_PROA2 Reviewed; 640 AA.
AC B4S6P7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Paes_0755;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
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; CP001108; ACF45802.1; -; Genomic_DNA.
DR RefSeq; WP_012505339.1; NC_011059.1.
DR AlphaFoldDB; B4S6P7; -.
DR SMR; B4S6P7; -.
DR STRING; 290512.Paes_0755; -.
DR EnsemblBacteria; ACF45802; ACF45802; Paes_0755.
DR KEGG; paa:Paes_0755; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_10; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002725; 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..640
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119740"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
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 640 AA; 69265 MW; 00C06277072C2BF0 CRC64;
MGKIIGIDLG TTNSCVAVMQ GTQPTVIENS EGYRTTPSMV AFTKNGERLI GHAAKRQAIT
NAKNTVFSIK RFMGRKFDEV PNEKKIAPYK VVNINGEARV EIDDKNYSPQ EISAMILQKM
KQTAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGKIAGL EVKRIINEPT AAALAYGLDK
KKENEKVAVF DLGGGTFDIS ILELGDGVFE VKSTDGDTHL GGDDFDQTII DFLADEFKKQ
EGIDLRTDAI ALQRLKEAAE KAKIELSSRT DTEINLPFIT ATQEGPKHLV VNLTRAKFEA
LASTLFDNIM APCKRAIKNA KVNISEIDEV VLVGGSTRIP KVQELVKELF KREPNKSVNP
DEVVAVGAAI QGGVLTGEVS DVLLLDVTPL SLGIETLGGV MTKLIEANTT IPTKKQEVFS
TAADNQTSVE VHVLQGERPM ASDNKTLGRF HLGDIPPAPR GMPQVEVAFD IDANGILHVS
AKDKATGKEQ SIRIEAGGKL NDAEIEKMKN DAKAHAEEDA KRKEEVETKN AADSLIFSTE
KQLQELGDKI PADKKAPLES ALDRLKEAHK SGSADAIKPA MDEVNTIWND IASQLYQAAD
APGSGTPNPE AESGKQESSG KTDGQVDAEY EVIDGNDKDK