ID   LONP2_KLULA             Reviewed;        1003 AA.
AC   Q6CWS4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
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   OrderedLocusNames=KLLA0B01892g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR382122; CAH02008.1; -; Genomic_DNA.
DR   RefSeq; XP_451615.1; XM_451615.1.
DR   AlphaFoldDB; Q6CWS4; -.
DR   SMR; Q6CWS4; -.
DR   STRING; 28985.XP_451615.1; -.
DR   EnsemblFungi; CAH02008; CAH02008; KLLA0_B01892g.
DR   GeneID; 2897516; -.
DR   KEGG; kla:KLLA0_B01892g; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q6CWS4; -.
DR   OMA; NKSPIIM; -.
DR   Proteomes; UP000000598; Chromosome B.
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; IPR003111; Lon_prtase_N.
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   Pfam; PF02190; LON_substr_bdg; 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   Reference proteome; Serine protease.
FT   CHAIN           1..1003
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395795"
FT   DOMAIN          14..303
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          773..969
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          367..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        874
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        917
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         520..527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   1003 AA;  112645 MW;  9578E061519BCCE6 CRC64;
     MGLFFDSPGS NLYLPCFTLV DAPKLVPLPG VSYKVSFERD SIIHVLSEFK RNNSFKNNHL
     LDKINTAIAQ NEIVVDNSVV NSCKQFHKKY GSDNSNNDAE VQMYIVLLPF EAVNNSVGAA
     SRITAIQVED DTITITFKSV ARVENKQPLL NMQHSLWKSS ILEIDDRSEL RTWDHKSINK
     SILSFVKIFY DTDKIIKDFK SKYSLASKRS GDIDSRVLYL SPLANTLFMQ LNGSHFNKSW
     KLLKAYLEQL TVLERNYDTC FELVSMMDLV MSILPMSLKQ RLDFLTAKKL KSRAILFSTC
     VQDFQQIFKK LDDSVDYVNN HFSNSSNNDK SKLIANQLRA LRFYIDDIKR NNSSVILKAN
     SEKERTDVTS PNKFLKTSSS HDEDSDSNDE MEQIKSFIDS LEEKNVHPDG IKLLQKDFKR
     FMKMTPQNAD YQVLRNYFDI VMDIPFGKTV NISTIDLAKS RAKLNEDHYG LQSVKRRLVE
     YLSVLKISEI STNDPNLNTD LHPKKDRASI NKPPILLLVG PPGVGKTSIA KSVADVLGRK
     FQRISLGGIH NEAEIRGHRR TYVGSMCGLI IGALRKAGTM NPLILLDEVD KVLSGGVGGF
     GNRVNGDPGA ALLEVLDPEQ NSTFSDHYVG FPVDLSQVLF FCTANDLEGI SEPLLNRMEL
     IELPGYTPDE KIMIGSKFLL PKQIKANGLD AIKELPKIYL TDEAWNCVVL EYTREPGVRG
     LERRIGAIVR GKVVEYVENK MIQGEVDKEH LYKYLGLAHH PISEEILAPT EHSEKFGVVN
     GLSYNSDGSG SVLLFEVIKI HTDESGATNG PYIKTTGNLG NILEESIKIA TSFVKHILFR
     GLIPGVNEKD INEFLTSEYH LHVPMGAVSK DGPSAGAAIS LAILSCALKR PVSPKLCMTG
     EITLRGKILP IGGIKEKLLG AQFYHMNHVL VPSANLSDVV QAVSTDNQEQ YEIYMDRSRQ
     PELQKLKDKT QLQLHYCSDF FDVVKYTWPE LLNKEVSHSR PSL