ID A0A4P1RHH9_LUPAN Unreviewed; 877 AA.
AC A0A4P1RHH9;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=TanjilG_27811 {ECO:0000313|EMBL:OIW10865.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW10865.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW10865.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW10865.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM007366; OIW10865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P1RHH9; -.
DR STRING; 3871.A0A4P1RHH9; -.
DR Proteomes; UP000188354; Chromosome LG06.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 11..253
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 682..867
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 72..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 875..877
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT COMPBIAS 75..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 773
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 816
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 408..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 877 AA; 96861 MW; 23CA3F216875FDE6 CRC64;
MAESVELPSR LAILPFRNKV LLPGAIIRIR CTSPTSVKLV EQELWQREEK GLIGILPVHD
AAGIKPVGHS ISEGVGTDSL DQSSKTQGGS SDSHKLDTEN QNDVHWHSRG VAARALHLSR
GVEKPSGRVT YIVVLEGLCR FSVQELITRG TYHTARISSL EMMKTEMERV EQDPDFVMLS
RKFKATAMEL ISVLEQKQKT GGRTKVLLET VPVHKLADIF VASFEISFEE QLCMLDSVDL
KVRLSKATEM VDRHLQSIRV ADKITQKVEG QLSKSQKEFL LRQQMRAIKE ELGDNDDDED
DLAALERKMQ SAGMPQDIWK HAHRELRRLK KMQPQQPGYS SSRAYLDLLA DLPWQKASKE
RELDLRAAQE RLDNDHYGLV KVKQRIIEYL AVRKLKPDAK GPVLCFVGPP GVGKTSLASS
IAAALGRKFV RISLGGVKDE ADIRGHRRTY IGSMPGRLID GLKRVGVSDP VMLLDEIDKT
GSDVRGDPAS ALLEVLDPEQ NKTFNDQVIF VATANRAQPI PPPLLDRMEV IELPGYTSEE
KLKIAMRHLI PRVLDQHGLS SEFLHIPEGM VKLVIQRYTR EAGVRNLERN LAALARAAAV
SVAEQEQVVP LDKGMQELAT SLLENRLPND AEVEMEVIPM GVNNRDISNT FKFASPIVID
EAMLEKVLGP PKFDSKEAAE RVASPGVSVG LVWTTFGGEV QFVEATAMVG KGELHLTGQL
GDVIKESAQI ALTWVRARAA DLKLAAAEGN NLLEGRDVHI HFPAGAVPKD GPSAGVTLVT
ALVSLFSQKR VRSDTAMTGE MTLRGLVLPV GGIKDKILAA HRHGIKRVIL PERNSKDLVE
VPPSVLANLE IVLAKRMEDV LEQAFEGGCP WRQHSKL
//
