LON_DICNV
ID LON_DICNV Reviewed; 805 AA.
AC A5EWF3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=DNO_0227;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; CP000513; ABQ14320.1; -; Genomic_DNA.
DR RefSeq; WP_011927973.1; NC_009446.1.
DR AlphaFoldDB; A5EWF3; -.
DR SMR; A5EWF3; -.
DR STRING; 246195.DNO_0227; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABQ14320; ABQ14320; DNO_0227.
DR KEGG; dno:DNO_0227; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000248; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..805
FT /note="Lon protease"
FT /id="PRO_0000396560"
FT DOMAIN 6..198
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 596..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 725
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 361..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 805 AA; 90289 MW; 42CC398B3D280148 CRC64;
MTDKIYPILP LRDVVVFPHV IVPLFIGREK SIAALDAAMN GSQELLLVPQ RDPAVVEPTL
ADLHEIGSLG RIVQMAKLSD GTVKALVEGL YRVHLEALND DEKMFSAKKR NMLEKNSTKS
EEHDSIVEIL IEEFAKYLRN QERSADELLE TLRGINDIGR ISDTIAAHMD FRIEERVHLL
AMEDAYERSQ RLMILLAQES EKNELNKKIK NRVKQQMERN QREYYLNEKI KAIQKELGEM
DEAQNDIELL EAQIKKAKMP VDVEKKALSE LNKLKQMSAM SSEANVIRNY LEWLIDYPWA
IEKPARYDLE EAARILDRDH YGLEDVKERI LEYLAVQKRI NEHNQKEAGT IGKGPIICLI
GPPGVGKTSL GKSIAEATGR DFDRIALGGL HDEAEIRGHR RTYIGALPGK IVQKLCKLGS
NNPVILLDEI DKIGHDHHGD PAAALLEVLD PAQNHTFNDH YLETDIDLSN VLFIATANTL
NISEPLLDRM EVIRLPGYTT QEKIQIAKRY IVPRQRKENV LKASEFKIKN GVLNDVIEDY
TREAGVRNLE REIGKLARKS VRRLQEGKQK SILITPNNLK DFLGVAKYHR NDEDLQAKIG
SVTGLAWTSV GGELLQIEGV AFSGKGRLTH TGQLGDVMQE SIRTALSVVR SYLDDLDDNF
RFDEYDIHLH LPEGATPKDG PSAGIAMATA LLSALSKQAV RGDLAMTGEI TLHGKVLAIG
GLKEKLLAAQ RGRLKMVLIP EDNLKDLDEI PEEVKAALEI VPVSHIHEVF DHAFVADHAP
FKARIEQKSL PTVSAVMHET PAGRC
