DNAK_LACE2
ID DNAK_LACE2 Reviewed; 628 AA.
AC C4Z1J4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
GN OrderedLocusNames=EUBELI_01360;
OS Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS (Eubacterium eligens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospira.
OX NCBI_TaxID=515620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001104; ACR72355.1; -; Genomic_DNA.
DR RefSeq; WP_012739590.1; NC_012778.1.
DR AlphaFoldDB; C4Z1J4; -.
DR SMR; C4Z1J4; -.
DR STRING; 515620.EUBELI_01360; -.
DR EnsemblBacteria; ACR72355; ACR72355; EUBELI_01360.
DR GeneID; 41356068; -.
DR KEGG; eel:EUBELI_01360; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001476; 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; 2.
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..628
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205187"
FT REGION 589..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 628 AA; 66574 MW; B915FA7F9EDB34E4 CRC64;
MGKIIGIDLG TTNSCVAVME GGKPVVIANA EGLRTTPSVV AFSKTGERLV GDPAKRQAVT
NADKTISSIK RHMGTDYKVE IDGKKYTPQE ISAMILQKLK SDAENYLGEK VTEAVITVPA
YFNDAQRQAT KDAGKIAGLD VKRIINEPTA AALAYGLDNE HEQKIMVYDL GGGTFDVSII
EIGDGVIEVL ATAGNNKLGG DDFDNAVTQY MLNDFKAKEG VDLSKDTMAL QRLKEAAEKA
KKELSSTTQT EINLPYITAT AEGPKHFEMT LTRAKFDELT HDLVEKTAEP VKNALSDAGL
TASELSKVLL VGGSTRIPAV QDKVKSLTGH EPSKTLNPDE CVAIGASIQG GKLAGDAGAG
DILLLDVTPL SLSIETMGGI ATRLIERNTT IPTKKSQIFS TAADNQTAVD INVVQGERQF
ARDNKSLGQF RLDGIPPARR GVPQIEVTFD IDANGIVNVS AKDLGTGKEQ HITITAGSNM
SDEDIDKAVK EAAEFEAQDK KRKDAIDARN EADSMVFQTQ KAMDEAGDKL DASDKAAVET
DLNALKALVD GSDPENMTDA QVDEIKAAKE KLMESAQKLF AKLYESQQAA GGAGPDMGAG
AGPDMGAGAS NGSAPYGDDV VDGDYKEV