LONP2_MAIZE
ID LONP2_MAIZE Reviewed; 885 AA.
AC P93647;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
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;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RX PubMed=9620272; DOI=10.1023/a:1005912831051;
RA Barakat S., Pearce D.A., Sherman F., Rapp W.D.;
RT "Maize contains a Lon protease gene that can partially complement a yeast
RT pim1-deletion mutant.";
RL Plant Mol. Biol. 37:141-154(1998).
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; U85494; AAC50011.1; -; mRNA.
DR PIR; T04321; T04321.
DR RefSeq; NP_001105903.1; NM_001112433.1.
DR AlphaFoldDB; P93647; -.
DR SMR; P93647; -.
DR STRING; 4577.GRMZM2G109560_P01; -.
DR MEROPS; S16.003; -.
DR PaxDb; P93647; -.
DR PRIDE; P93647; -.
DR EnsemblPlants; Zm00001eb319680_T001; Zm00001eb319680_P001; Zm00001eb319680.
DR GeneID; 732820; -.
DR Gramene; Zm00001eb319680_T001; Zm00001eb319680_P001; Zm00001eb319680.
DR KEGG; zma:732820; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OrthoDB; 528132at2759; -.
DR BRENDA; 3.6.4.7; 6752.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; P93647; baseline and differential.
DR Genevisible; P93647; ZM.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
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:0032042; P:mitochondrial DNA metabolic process; IDA:AgBase.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
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..885
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000026737"
FT DOMAIN 12..254
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 690..875
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 70..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 883..885
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 781
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 824
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 885 AA; 97733 MW; 331A321B56C75407 CRC64;
MSDSPVELPS RLAVLPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQKEE KGLIGVLPVR
DSEATAVGSL LSPGVGSDSG EGGSKVGGSA VESSKQDTKN GKEPIHWHSK GVAARALHLS
RGVEKPSGRV TYIVVLEGLC RFSVQELSAR GPYHVARVSR LDMTKTELEQ AEQDPDLIAL
SRQFKATAME LISVLEQKQK TVGRTKVLLD TVPVYRLADI FVASFEISFE EQLSMLDSVH
LKVRLSKATE LVDRHLQSIL VAEKITQKVE GQLSKSQKEF LLRQQMRAIK EELGDNDDDE
DDVAALERKM QNAGMPANIW KHAQREMRRL RKMQPQQPGY SSSRAYLELL ADLPWQKVSE
ERELDLRVAK ESLDQDHYGL TKVKQRIIEY LAVRKLKPDA RGPVLCFVGP PGVGKTSLAS
SIAKALNRKF IRISLGGVKD EADIRGHRRT YIGSMPGRLI DGLKRVSVSN PVMLLDEIDK
TGSDVRGDPA SALLEVLDPE QNKAFNDHYL NVPFDLSKVI FVATANRMQP IPPPLLDRME
IIELPGYTPE EKLKIAMKHL IPRVLEQHGL STTNLQIPEA MVKLVIERYT REAGVRNLER
NLAALARAAA VKVAEQVKTL RLGKEIQPIT TTLLDSRLAD GGEVEMEVIP MEHDISNTYE
NPSPMIVDEA MLEKVLGPPR FDDREAADRV ASPGVSVGLV WTSVGGEVQF VEATAMVGKG
DLHLTGQLGD VIKESAQLAL TWVRARAADL NLSPTSDINL LESRDIHIHF PAGAVPKDGP
SAGVTLVTAL VSLFSNRKVR ADTAMTGEMT LRGLVLPVGG VKDKVLAAHR YGIKRVILPE
RNLKDLSEVP LPILSDMEIL LVKRIEEVLD HAFEGRCPLR SRSKL
