LONP2_PICST
ID LONP2_PICST Reviewed; 1180 AA.
AC A3LUF7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
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 ORFNames=PICST_45980;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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 -!- 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; CP000498; ABN66580.2; -; Genomic_DNA.
DR RefSeq; XP_001384609.2; XM_001384572.1.
DR AlphaFoldDB; A3LUF7; -.
DR SMR; A3LUF7; -.
DR STRING; 4924.XP_001384609.2; -.
DR PRIDE; A3LUF7; -.
DR EnsemblFungi; ABN66580; ABN66580; PICST_45980.
DR GeneID; 4838390; -.
DR KEGG; pic:PICST_45980; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR InParanoid; A3LUF7; -.
DR OMA; NKSPIIM; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
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..1180
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395798"
FT DOMAIN 19..364
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 924..1163
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 416..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1032
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 1075
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 667..674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1180 AA; 132053 MW; 1A605C5111ACB917 CRC64;
MARYKNPKSP AKLKQQIVLP TCKLDSNLVL LPGIIYNVTF SRFKAAALLY RYKDLVSQVS
IINNLLNEYE FNPSKDSDSV EEDDMVTSPI TISKVAVEGI EQFFKYEAAF KNSQGLVSEK
DIAEVAPSNE FDWLTLAIKP NLEKIKEPSN AQIDPTEHNS VVTIARIVGI VDDTTNIKLT
LQAITRGLKI APKKKTRPNE QLLEVDWSSD IPELRRHFKS LKDSSLDLFK VIDKFIVDYR
QALSINSANG NKSNLQITKP GSRYKGANGS SQKPGDLLTL NPLANALYLQ LAGSKDFSKA
FLSLQKLYGQ FASDENLKVD TKSYLRLLDL TCGILPFPNH EKLKLLHKIS IDDRGNELIN
MINQLIKIFD TLDGNNSFVN HWFYNEATNI QKANVVANQL KSIRLLLEGM TNKTRPISNR
GNIKSFNNSE NGNNNKTNGS GITSRRPKSN EDGGEVYDEE DDDEEDDELR AITNFIKYKL
PNITTLSPDS KRLIIKDFKR IRASSQSPGG GGNSDFHVIR NYLEIVMDIP WDKYVTKFKS
NKDIDLNFAK KQLDDDHYGL EHVKKRLIQY LVVLKLLGIN AEKQISDFRK ENQVPSPSSS
GSNLATQNSL VPASSIVIAN NDETSFAHKQ AQNKVKTSIK ESNIENQTNQ SIQVTKYNKS
PIIMLAGPPG TGKTSLAKSI ASSLGRNFQR ISLGGVKDES EIRGHRRTYV GAMPGLIIQA
LRKSRSMNPV ILLDEIDKVI GGSSGVNKFN GDPSAALLEV LDPEQNTSFI DHYLGFPVDL
SQVIFICTAN EPHNLTRPLL DRLEMIEVSA YDYNEKLIIG RKYLLPRQVK RNGFPASDRI
EEFVNIDDAS MKKIIVDYTR EAGVRNLERK LGTICRFKAV EYCEGLSGKS FYNPNVEEAD
LPKYLGIPYS SGDFSSIETT ISNNSRVGIV NGLSYNSDGS GSVLVFETIG FDKRVGNPNS
SNTGCSLVMT GRLGEVLMES GKIGLTFIKS LIYKNLIQAK EQPDDKYLIE KFNNLELNLH
VPMGSISKDG PSAGITMATS FLSVILDKPV PADVAMTGEI TLRGLVLPIG GVKEKMMGAH
LNGNIRRMIV PRENRKDLIE EFSRSVEEAG DVVDSNLMNE LLKDNEEADF KMDKVEKFYL
KRYGIQIFYA REFYDVMKIL WGEDDLLTKP KSNRILEYHL
