LONM_OSTTA
ID LONM_OSTTA Reviewed; 920 AA.
AC Q00WL5; A0A096P7R8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN OrderedLocusNames=Ot13g03040 {ECO:0000312|EMBL:CEG00235.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC in a site-specific manner. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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; CAID01000013; CEG00235.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00WL5; -.
DR SMR; Q00WL5; -.
DR STRING; 70448.A0A096P7R8; -.
DR PRIDE; Q00WL5; -.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; Q00WL5; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000009170; Chromosome 13.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03120; lonm_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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; IPR027503; Lonm_euk.
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; PTHR43718; PTHR43718; 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; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..58
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 59..920
FT /note="Lon protease homolog, mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT /id="PRO_0000395769"
FT DOMAIN 102..336
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 734..918
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 65..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 920 AA; 99963 MW; D3AD89FDC71A139B CRC64;
MLARALIRRR QAVTTLAAPS RARSTRSRAL LDELGAGAVA AEGVGRARGS SKNAFVRATT
ANGNETLASA GDGGSTSSAS SSSTTSGGIM VSAAHPSSHP QVLAVPLPRR PLMPGIIMPV
KVTDEKLIAE LEDMRNRGQA YVGAFLMRSE GSSSSSAAGK EEDAFDALTK RTVASVGLDG
EEEEGADPSD HMHDIGTFAQ VHNIVRLPAD SPNGEESATL LLLGHRRLRK LGTMKRDPLV
VQVEHLKDEK FDANDDIIKA TTNEVVATIK DLLKTNPLHK ETLQYFAQNF NDFQDPPKLA
DLGASMCSAD DAQLQRVLEL LSVKDRLDAT LELLKKEVEI GKLQADIGKK VEDKISGDQR
RYFLMEQLKS IKKELGMERD DKTALIEKFT KRFEPKRKSV PEETVKVIDE ELQKLSGLEP
SSSEFNVTRN YLEWLTSLPW GVCGDEKLDI AHAQEVLDAD HYGLEDVKDR ILEFIAVGQL
LGTTQGKIIT MVGPPGVGKT SIGQSIAKAL GRKFYRFSVG GMSDVAEIKG HRRTYVGAMP
GKLIQCLKST GVCNPVVLID EIDKLGRGYQ GDPASALLEL LDPEQNGTFL DHYLDVPVDL
SKVLFVCTAN VLDTIPGPLL DRMEVVRLSG YITDEKVQIA RTYLEKAAKG KSGLSDFDAT
ITDEAMSKLI GDYCREAGVR NLQKHLEKVY RKVALKVARA KSTDTTLDPI VIDVDDLVDY
VGQPPFQTDR IYDETPPGVV TGLAWTAMGG STLYIECTSV ESGEGKGSLK TTGQLGDVMK
ESSAIAHTFT RGFLQSKDPG NDFLQKTSLH VHVPAGATPK DGPSAGVTIT TSLLSLAMDK
PVKPNLAMTG ELTLTGRVLP VGGIKEKTIA ARRSGVKTII FPQGNKKDYD ELSEDIREGL
EACFVSTYDE VYRHALDWDR
