ID   LONP2_PICAN             Reviewed;         935 AA.
AC   Q2V573;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PLN;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL
RC   Y-1798 / VKM Y-1397;
RX   PubMed=17172804; DOI=10.4161/auto.3534;
RA   Aksam E.B., Koek A., Kiel J.A., Jourdan S., Veenhuis M., van der Klei I.J.;
RT   "A peroxisomal lon protease and peroxisome degradation by autophagy play
RT   key roles in vitality of Hansenula polymorpha cells.";
RL   Autophagy 3:96-105(2007).
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       ECO:0000269|PubMed:17172804}.
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}.
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DR   EMBL; DQ297145; ABB88892.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2V573; -.
DR   SMR; Q2V573; -.
DR   PhylomeDB; Q2V573; -.
DR   BRENDA; 3.6.4.7; 2587.
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; 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; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027501; Lonp2_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 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; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW   Serine protease.
FT   CHAIN           1..935
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395797"
FT   DOMAIN          11..227
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   DOMAIN          692..922
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   MOTIF           933..935
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        789
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        832
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         452..459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   935 AA;  104880 MW;  8C35E3D905A5069F CRC64;
     MSSKSSAWQV ELPVHRLERN LIFLPGITYR VVFDKQKALD LASRWSAKER SERVAAIASR
     FGLSSKHLVA CVPGYPDSDT CTVCVVNGFY EMSETTVVSF KGVTRGYIVQ SDEDTATVEI
     QEETSVPHPD TKDMIRLFDN IDQFLTYYKD EGTLDSEDKE ERSRHILLRL TPLATLLNAQ
     LSASDVSAGL KRLRQAYGRK SGDFAHYNDV LVALFPFPIE LKISYLRSKG AERIEVFNKC
     VAFANKVFEE HLDTSYLAEI WSSLDHHSSK AQSNVSRSQF ISNHLRNLRR LVEEMGLMRV
     TGRGSRTAED NDENKSIQDF VDSLDKYLIN EDGKRLIAKD FERLKQMQSS SSDYQVLRAY
     LEIIMDLPWQ RLDSFVESVN VDLARAREQL DADHYGMESA KERILEYLAV LNLHNQKQPR
     HEPEFVYGTG DEPTTKERPA STLKAPILLL TGPPGVGKTS LARSIATTLG RKFQRISVGG
     LNDFADLKGH RRTYVGAIPG LIVQALRRSQ SMNPVILLDE VDKIGSNSRK GDPEAALLEI
     LDPEQNTNFH DHYIGFPIDL SQILFVCTSN DLWQLSDPLR DRMEVIELAG YNYMEKVEIS
     KKYLIPRQLE RAGLSSDAVA MDDETILKMA THYTSEPGIR NLERLIAAIC RGKAVERQMG
     EATKTVTVHD LAKYIGSPSH LRATAAGETK FQKGYGVVNG LSYNSDGSGS LLRFEMIGLP
     GSQKMNCTGR LGEVLLESSQ IANTLVGYLL HNNLVAGTQE FRDELLKRYE NTSVHLHVPE
     GAISKDGPSA GITMTLCLMS LVLRKKVPET LAMTGEITLT GKVLPIGGVR EKLLGAHLAG
     KVNKVLLPRQ NRKDVIEDFI YNLRNRELAK ELFAKFLDEE EQLLKEGRTH AGEPEKWVYQ
     TLGLEIVYVD DFSDVLASVW EGEVLLTGGI REARI