DNAK_LEPBL
ID DNAK_LEPBL Reviewed; 645 AA.
AC Q04Y47;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=LBL_2644;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ79998.1; -; Genomic_DNA.
DR RefSeq; WP_011670944.1; NC_008508.1.
DR AlphaFoldDB; Q04Y47; -.
DR SMR; Q04Y47; -.
DR KEGG; lbl:LBL_2644; -.
DR HOGENOM; CLU_005965_2_4_12; -.
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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119722"
FT REGION 602..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 645 AA; 69002 MW; 7A56721377421BB0 CRC64;
MSKEKIIGID LGTTNSVVSV MEGGDPVVIQ NSEGARTTPS IVAFTAKGEN LVGQFAKNQA
ITNAVNTIRS AKRFIGRRIG ECESEMKHVS YKVIRSGNEG VKFETSAGEF TPQEISARVL
MKMKQTAEDY LGQKVTKAVI TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
FDKKNVNSKI AVYDLGGGTF DISILELADG VFEVKSTNGD THLGGDDFDM AIMEWMISEF
KNQTGIDISA DKNTVQRLKE AAEKAKIELS GTMSTQINLP FITADASGPK HLDMTLSRAK
FDQLTKSLVD RTRIPCENAL RDAGLKASDI NEVILVGGSI RIPAVQELVK QIFGKEPNKS
VNPDEVVAVG AAIQGGVLAG EVSDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTKKSQ
VFSTAADNQS AVSIHVLQGE REMASANRTL GRFDLIGIPP APRGVPQIEV TFDIDANGIV
HVSAKDLGTG KEQKIRIESS SGLSEDEIQK MVKDAEAHAA ADKAQREVIE AKNELDTLAY
SLEKTVNEAG DKIGASEKQL ATDEVKRARE AIESNDKARM ESAKASISKI ASDIATKVYS
QGAPGAEQAA GSTGPDQGQN DQGNSGNNGE KVVDADYTVV DDEKK