ID   LONP2_SPIOL             Reviewed;         887 AA.
AC   O04979;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 113.
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};
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Inagaki N., Watanabe A., Satoh K.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20482.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D85610; BAA20482.1; ALT_FRAME; mRNA.
DR   PIR; T09142; T09142.
DR   AlphaFoldDB; O04979; -.
DR   SMR; O04979; -.
DR   MEROPS; S16.003; -.
DR   PRIDE; O04979; -.
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:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
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   Serine protease.
FT   CHAIN           1..887
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000026738"
FT   DOMAIN          11..254
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          693..878
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          72..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           885..887
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   COMPBIAS        80..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        784
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        827
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         409..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   887 AA;  98272 MW;  D4842C77778D0E36 CRC64;
     MAEAVELPSR LGILAFRNKV LLPGAIIRIR CTSPSSVKLV EQELWQREEK GLIGIVPVRD
     ASESASVAPV LYPGGGTDSG ERNVKSQPGL SDSRKADGKS QQEAVHWHTR GVAARALHLS
     RGVEKPSGRV TYTVVLEGLC RFRVMELNSR GNYYTARISP LDITKADMEQ AQQDPDFVSL
     ARQFKVTAVE LISVLEQKQK TGGRTKVLLE TVPVHKLADI FVASFEISFE EQLCMLDSID
     LKVRLSKATE LVDRHLQSIR VAEKITQKVE GQLSKSQREF LLRQQMRAIK EELGDNDDDE
     DDVAVLERKM QSAGMPANIW KHAQRELRRL KKMQPQQPGY SSSRVYLELL ADLPWQNATE
     EQKLDLRAAK ERLDSDHYGL VKVKQRIIEY LAVRKLKPDA RGPILCFVGP PGVGKTSLAA
     SISAALGRKF IRISLGGVKD EADIRGHRRT YIGSMPGRLI DGIKRVGVSN PVMLLDEIDK
     TGSDVRGDPA SALLEVLDPE QNKTFNDHYL NVPYDLSKVI FVATANKVQP IPPPLLDRME
     VIELPGYTPE EKARIAMQYL IPRVMDQHGL SSEFLQISED MVKLIIQRYT REAGVRNLER
     NLSALARAAA VKVAEQDNAT AVSKDFHQFT SPVEESRLAE GAEVEMEVIP MGVDNREISN
     ALQVMSPLIV DETMLENVLG PPRYDDRETA ERVSNPGVSV GLVWTAFGGE VQFVEASVMA
     GKGELRLTGQ LGDVIKESAQ IALTWVRARA MELNLVATGE INLMEGRDIH IHFPAGAVPK
     DGPSAGVTLV TALVSLLSQK RMRADTAMTG EMTLRGLVLP VGGVKDKVLA AHRYGIKRVI
     LPERNLKDLV EVPSAVLSNL EIIYAKRMEV LEQAFEGGCP WRQRARL