LONM_OSTLU
ID LONM_OSTLU Reviewed; 936 AA.
AC A4S6Y4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 ORFNames=OSTLU_41620, OSTLU_52138;
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus; unclassified Ostreococcus.
OX NCBI_TaxID=436017;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901;
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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}.
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DR EMBL; CP000593; ABO99468.1; -; Genomic_DNA.
DR EMBL; CP000601; ABP01139.1; -; Genomic_DNA.
DR RefSeq; XP_001421175.1; XM_001421138.1.
DR RefSeq; XP_001422780.1; XM_001422743.1.
DR AlphaFoldDB; A4S6Y4; -.
DR SMR; A4S6Y4; -.
DR STRING; 436017.A4S6Y4; -.
DR EnsemblPlants; ABO99468; ABO99468; OSTLU_41620.
DR EnsemblPlants; ABP01139; ABP01139; OSTLU_52138.
DR GeneID; 5005054; -.
DR GeneID; 5006932; -.
DR Gramene; ABO99468; ABO99468; OSTLU_41620.
DR Gramene; ABP01139; ABP01139; OSTLU_52138.
DR KEGG; olu:OSTLU_41620; -.
DR KEGG; olu:OSTLU_52138; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000001568; Chromosome 13.
DR Proteomes; UP000001568; Chromosome 21.
DR GO; GO:0005759; C:mitochondrial matrix; 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:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
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; 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_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..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 41..936
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395768"
FT DOMAIN 112..350
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 748..932
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 65..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 838
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 881
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 507..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 936 AA; 101688 MW; 7BCF7680ABE28B8E CRC64;
MYATRAIARR LERHAARCKG AHVARAVRGA RARTTSAPRA LLDALGAGRG DADAFGTRTR
RTRNAFVSSV DGDGSTGSTG SSSSSSSSAF GDSASSGGIM VSASHPSSHP QVLAVPLPRR
PLMPGIIMPV KVTDEKLIAE LEDMRNRGQA YVGAFLQRTD AASSASKGEG EDVFDALSAM
KRTTTSVGLD GEEMVDEDEV DPADHMHDIG TFAQVHNIVR LPTDSTTGEE SATLLLLGHR
RLRKLGTMKR DPMVVKVEHL KDEKFDANDD IIKATTNEVV ATIKDLLKTN PLHKETLQYF
AQNFNDFQDP PKLADLGASM CSADDAQLQH VLELLSVKER LDATLELLKK EVEIGKLQAD
IGKKVEEKIS GDQRRYFLME QLKSIKKELG MERDDKTALI EKFTKRFEPK RASVPEDTAK
VIDEELQKLG GLEPSSSEFN VTRNYLEWLT SLPWGVCGDE KLDISHAQEV LDSDHYGLED
VKDRILEFIA VGQLLGTTQG KIITMVGPPG VGKTSIGQSI AKALGRKFYR FSVGGMSDVA
EIKGHRRTYV GAMPGKLIQC LKSTGVCNPV VLIDEIDKLG RGYQGDPASA LLELLDPEQN
GTFLDHYLDV PVDLSKVLFV CTANVLDTIP GPLLDRMEVV RLSGYITDEK VQIARTYLEK
AAREKSGLSD VDASITDAAM GKLIGDYCRE AGVRNLQKHL EKVYRKIALK VARAKSADEK
LDSIVVDVDD LVDYVGQPPF ATDRIYDVTP PGVVTGLAWT AMGGSTLYIE CTAIDSGDGK
GALKTTGQLG DVMKESSTIA HTFTRGFLEL KDPGNKYLAD TSLHVHVPAG ATPKDGPSAG
ITITTSLLSL AMNKPVKPNL AMTGELTLTG RVLPIGGVKE KTIAARRSGV KTIIFPEGNK
KDYDELSEDI REGLDAHFVS TYDEVYRQAL DWEASS
