DNAK_LAWIP
ID DNAK_LAWIP Reviewed; 633 AA.
AC Q1MPW1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=LI0912;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54966.1; -; Genomic_DNA.
DR RefSeq; WP_011526995.1; NC_008011.1.
DR AlphaFoldDB; Q1MPW1; -.
DR SMR; Q1MPW1; -.
DR STRING; 363253.LI0912; -.
DR PRIDE; Q1MPW1; -.
DR KEGG; lip:LI0912; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002430; 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..633
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059592"
FT REGION 592..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 633 AA; 67998 MW; 6A2D492708C2D9CA CRC64;
MGKIIGIDLG TTNSCVYVME GKEPKCITNP NGGRTTPSVV AFTDKDRLVG DAAKRQAITN
SARTIFAVKR LMGRRADSPE VVHWKEHAPY KIVAASNGDA AVEIDGREYS PQEISAIILS
KLKADAEAYL GESVSEAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAASLAYGF
DKKANEKIAV FDLGGGTFDV SILEVGDSVV EVLATNGDTF LGGEDFDQRI INYLVEEFKK
EQGIDLSKDN MALQRLKDSA ENAKKELSTA METEINLPFI TADQSGPKHL LIKLTRAKLE
QLVMDLVGRT IEPCSKALED AGLQTSNIDE VILVGGMTRM PLVQKKVAEF FGKEPNRSVN
PDEVVAMGAA IQGGILAGDV KDVLLLDVTP LSLGIETMGG VFTKLIDRNT TIPTRKSQTF
TTAADNQPSV SIHVLQGERP MASDNMTLAR FDLTGIPPAP RGVPQIEVAF NIDANGIVNV
SAKDLGTGKE QSIQITASSG LSEADIEKLI REAESHASED KKKQEIIEVR NHADGLIYST
EKSIKDLEGK IDAELQADIT SKIEALKKVM EGEDSAAIKK ATDELASASH KLAEQLYKQT
QETSGASGDP TDTSASSSKS GDDVVDADFT EVK