ID   LONP2_ORYSI             Reviewed;         884 AA.
AC   B8BDV1; Q8GV57;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
GN   Name=LON1; ORFNames=OsI_32159;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16786279; DOI=10.1007/s10529-006-9022-x;
RA   Su W., Lin C., Wu J., Li K., He G., Qian X., Wei C., Yang J.;
RT   "Molecular cloning and expression of a cDNA encoding Lon protease from rice
RT   (Oryza sativa).";
RL   Biotechnol. Lett. 28:923-927(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded and unassembled polypeptides in the
CC       peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC       (PTS2)-containing protein processing and facilitates peroxisome matrix
CC       protein import. {ECO:0000255|HAMAP-Rule:MF_03121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and panicles.
CC       {ECO:0000269|PubMed:16786279}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
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DR   EMBL; AY129070; AAM95459.1; -; mRNA.
DR   EMBL; CM000134; EEC84943.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BDV1; -.
DR   SMR; B8BDV1; -.
DR   STRING; 39946.B8BDV1; -.
DR   MEROPS; S16.003; -.
DR   EnsemblPlants; BGIOSGA029377-TA; BGIOSGA029377-PA; BGIOSGA029377.
DR   Gramene; BGIOSGA029377-TA; BGIOSGA029377-PA; BGIOSGA029377.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   OMA; GAWQVVD; -.
DR   Proteomes; UP000007015; Chromosome 9.
DR   GO; GO:0005782; C:peroxisomal 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048527; P:lateral root development; IEA:EnsemblPlants.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:EnsemblPlants.
DR   GO; GO:0016485; P:protein processing; 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_03121; lonp2_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; IPR027501; Lonp2_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; 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   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW   Reference proteome; Serine protease.
FT   CHAIN           1..884
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395786"
FT   DOMAIN          12..253
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          689..874
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          67..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           882..884
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        780
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        823
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         408..415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   CONFLICT        426
FT                   /note="N -> D (in Ref. 1; AAM95459)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   884 AA;  97336 MW;  6F9D960F5FA5EFB7 CRC64;
     MADAAVELPG RLAILPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQREE KGLIGVLPVH
     DSEAAGSLLS PGVGSDSGEG GSKAPGGSAG ESTKQDTKNG KETIHWHSRG VAARALHLSR
     GVEKPSGRVT YIVVLEGLCR FSVQELSARG SYHVARVSRL DMTKTELEHA EQDPDLIALS
     RQFKATAMEL ISVLEQKQKT VGRTKVLLET VPVYRLADIF VASFEISFEE QLSMLDSVDL
     KVRLSKATEL VDRHLQSILV AEKITQKVEG QLSKSQKEFL LRQQMRAIKE ELGDNDDDED
     DVAALERKMQ NAGMPANIWK HAQRELRRLR KMQPQQPGYS SSRTYLELLA ELPWQKVSEE
     RELDLRAAKE SLDRDHYGLT KVKQRIIEYL AVRKLKPDAR GPVLCFVGPP GVGKTSLASS
     IAKALNRKFI RISLGGVKDE ADIRGHRRTY IGSMPGRLID GLKRVSVSNP VMLLDEIDKT
     GSDVRGDPAS ALLEVLDPEQ NKTFNDHYLN VPFDLSKVIF VATANRMQPI PPPLLDRMEV
     IELPGYTPEE KLKIAMKHLI PRVLEQHGLS STYLQIPEAM VRLIIERYTR EAGVRNLERN
     LAALARAAAV KVAEQDSVLR LGKEIQPITT TLLDSRLADG GEVEMEVIPM GQDISNTYEN
     PSPMIVDEAM LEKVLGPPRF DDSEAADRVA SPGVSVGLVW TSFGGEVQFV EATAMVGKGD
     LHLTGQLGDV IKESAQLALT WVRARAADLN LSPTSDINLL ESRDIHIHFP AGAVPKDGPS
     AGVTLVTSLV SLFSHRKVRA DTAMTGEMTL RGLVLPVGGV KDKVLAAHRY GIKRVILPER
     NMKDLAEVPA PILSGLEILL VKRIEEVLDH AFEGGCPLRP HSKL