DNAK_LEPIN
ID DNAK_LEPIN Reviewed; 646 AA.
AC P61443; O51869; P71442;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=LA_3705;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-645.
RC STRAIN=Serogroup Pomona;
RA Gul B., Yelton D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AE010300; AAN50903.1; -; Genomic_DNA.
DR EMBL; U72647; AAB17395.1; -; Genomic_DNA.
DR RefSeq; NP_713885.1; NC_004342.2.
DR RefSeq; WP_000031822.1; NC_004342.2.
DR AlphaFoldDB; P61443; -.
DR SMR; P61443; -.
DR STRING; 189518.LA_3705; -.
DR EnsemblBacteria; AAN50903; AAN50903; LA_3705.
DR KEGG; lil:LA_3705; -.
DR PATRIC; fig|189518.3.peg.3680; -.
DR HOGENOM; CLU_005965_2_1_12; -.
DR InParanoid; P61443; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001408; Chromosome I.
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 Reference proteome; Stress response.
FT CHAIN 1..646
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078481"
FT REGION 598..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 285..288
FT /note="DASG -> EPSR (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..294
FT /note="DM -> EL (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="Q -> QD (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 318..319
FT /note="NA -> KH (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="SI -> GL (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="G -> E (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> T (in Ref. 2; AAB17395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 69129 MW; 8C63B784AA27EAC3 CRC64;
MSKEKIIGID LGTTNSVVSV MEGGDPVVIQ NSEGARTTPS IVAFTAKGET LIGQFAKNQA
ITNAVNTIRS AKRFIGRRLN ECESEMKHVS YKVIRSGNEG VKFETSAGEF TPQEISARVL
MKMKQTAEDY LGQKVTKAVI TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
FDKKNVNSKI AVYDLGGGTF DISILELADG VFEVKSTNGD THLGGDDFDM AIMEWMISEF
KNQTGIDISA DKNTVQRLKE AAEKAKIELS GTMSTQINLP FITADASGPK HLDMTLTRAK
FDQLTKSLVD RTRIPCENAL RDAGLKASDI NEVILVGGSI RIPAVQELVK QVFGKEPNKS
VNPDEVVAIG AAIQGGVLAG EVSDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTKKSQ
VFSTAADNQS AVSIHVLQGE REMASANRTL GRFDLIGIPP APRGVPQIEV TFDIDANGIV
HVSAKDLGTG KEQKIRIESS SGLSEDEIQK MVKDAEAHAA ADKAQREVIE AKNELDTLTY
SLEKTVNEAG DKIGANEKQL ATDEIKRARE AIESNDKARI ESAKASISKI ATDIASKVYS
QSAPGAEQAA AGGPNGSAGS NDQGNSTNNG EKVVDADYTV VDDEKK