ID D7M5E0_ARALL Unreviewed; 991 AA.
AC D7M5E0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_03120};
GN ORFNames=ARALYDRAFT_489519 {ECO:0000313|EMBL:EFH48501.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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:0000256|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03120, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; GL348718; EFH48501.1; -; Genomic_DNA.
DR RefSeq; XP_002872242.1; XM_002872196.1.
DR AlphaFoldDB; D7M5E0; -.
DR STRING; 81972.D7M5E0; -.
DR MEROPS; S16.011; -.
DR EnsemblPlants; fgenesh2_kg.6__2653__AT5G26860.1; fgenesh2_kg.6__2653__AT5G26860.1; fgenesh2_kg.6__2653__AT5G26860.1.
DR Gramene; fgenesh2_kg.6__2653__AT5G26860.1; fgenesh2_kg.6__2653__AT5G26860.1; fgenesh2_kg.6__2653__AT5G26860.1.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03120}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120,
KW ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 145..358
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 802..986
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 109..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 892
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 935
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 991 AA; 109637 MW; B28A8920684EC15B CRC64;
MKGFDTNLRL QASSRELSNG FLHKRQNFIN LNLRNCYYPR SSFSPTMLKL FTSSASRVQH
LTPAIRVGSS PVESPLFKAL SQITGWNRRS GSLGHRAFFC SEPTDGEAAA EAEAKAVESD
SEGSDSKSSS AIVSTNPRPE DCLTVLALPV PHRPLFPGFY MPIYVKDPKV LAALQESRRR
QAPYAGAFLL KDGPSADSSS STDAEKNINE LKGKELLNRL HEVGTLAQIS SIQGDQVILV
GHRRLRITEM VSEEPLTVKV DHLKDNPFDM DDDVIKATSF EVISTLRDVL KTSSLWRDHV
QTYTQACLRV QHIGDFTYPR LADFGAAICG ANRHQAQEVL EELDVHKRLR LTLELMKKEM
EISKIQESIA KAIEEKISGE QRRYLLNEQL KAIKKELGVE TDDKSALSAK FKERIEPNKE
KIPAHVLQVI EEELTKLQLL EASSSEFNVT RNYLDWLTIL PWGNYSDENF DVVGAQKILD
EDHYGLSDVK ERILEFIAVG RLRGTSQGKI ICLSGPPGVG KTSIGRSIAR ALNRKFFRFS
VGGLGDVAEI KGHRRTYVGA MPGKMVQCLK SVGTANPLVL IDEIDKLGRG HAGDPASALL
ELLDPEQNAN FLDHYLDVTI DLSKVLFVCT ANVIDMIPNP LLDRMEVISI AGYITDEKVH
IARDYLEKTA RGDCGVKPEQ VEVSDAALLS LIENYCREAG VRNLQKQIEK IYRKIALKLV
REGAVAEEPA VAIDPEEAEI VADVGESPEN HTVEENPVSS AEEPKEAAQT EKIAIEKVMI
DESNLADYVG KPVFHEEKLY EQTPVGVVMG LAWTSMGGST LYIETTVVEE GEGKGGLNIT
GQLGDVMKES AQIAHTVARK IMLEKEPENQ FFANSKLHLH VPAGATPKDG PSAGCTMITS
LLSLATKKPV RKDLAMTGEV TLTGRILPIG GVKEKTIAAR RSQIKTIIFP EANRRDFDEL
AENVKEGLDV HFVDDYGKIF ELAFGYDKQE D
//
