DNAK_CAUSK
ID DNAK_CAUSK Reviewed; 631 AA.
AC B0T138;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Caul_0004;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000927; ABZ69142.1; -; Genomic_DNA.
DR RefSeq; WP_012284100.1; NC_010338.1.
DR AlphaFoldDB; B0T138; -.
DR SMR; B0T138; -.
DR STRING; 366602.Caul_0004; -.
DR EnsemblBacteria; ABZ69142; ABZ69142; Caul_0004.
DR KEGG; cak:Caul_0004; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
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..631
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079217"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 631 AA; 67652 MW; 0C7C6412A8C2FE3F CRC64;
MSKIIGIDLG TTNSCVAIMD GKTPKVIENA EGARTTPSVV AFLEDGERLV GQPAKRQAVT
NPTNTLFAIK RLIGRNFADP VVAKDKAMVP YEIVKGPTGD AWVKAHGKDY SPQEVSAFIL
QKMKEAAESH LGEPVTKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LEMNEGKKIA VYDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDLR IVDYLADEFK
KEQGVDLRKD KLALQRLREE AEKAKKELSS TAQYEVNLPF ISMNASGPLH LNIKLSRSKL
EALVEDLITR TIGPCEQALK DAGLKKSDID EVILVGGMSR MPKVQQAVQD FFGREPHKGV
NPDEVVALGA AVQAGVLQGD VKDVLLLDVT PLTLGIETLG GVFTPLIERN TTIPTKRSQT
FSTADDNQSA VTIRAFQGER PMAVDNKFLG QFDLQGIPPA PRGVPQIEVT FDIDANGIVN
VHAKDKATNK EHSIRIQANG GLSDADIERM VKEAEANKAS DEKKKALVEA KNQGEAIVHS
TEKAFAEHGD KIGGAEKTAI ETGLTDLKAA LEGEDVEAIQ AKTQALIQAS MKLGEAMYGA
QQGADGGEEA AHDDGVVDAE FEEVDDSKPS A