LONP2_CAEBR
ID LONP2_CAEBR Reviewed; 773 AA.
AC A8Y3E2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=lonp-2 {ECO:0000312|WormBase:CBG23035};
GN ORFNames=CBG23035 {ECO:0000312|WormBase:CBG23035};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600964; CAP39411.2; -; Genomic_DNA.
DR AlphaFoldDB; A8Y3E2; -.
DR SMR; A8Y3E2; -.
DR STRING; 6238.CBG23035; -.
DR PRIDE; A8Y3E2; -.
DR WormBase; CBG23035; CBP45854; WBGene00041464; Cbr-lonp-2.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_3_1; -.
DR InParanoid; A8Y3E2; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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: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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..773
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395784"
FT DOMAIN 9..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 587..766
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT MOTIF 771..773
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 672
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 715
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 336..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 773 AA; 86062 MW; 4B836E84AB24900E CRC64;
MKFEESMELP VIVVDSGVLL PGASLKIPIR SKLNTRTIEQ HLTRGGSNYV VIAYKLSTDK
IYNVATIAYI EKLFGWTFNS TTNYSLDVIG LHRANIDKLS FPKCRVSKLE DSSERAEFNH
STIENVISGA KILAQNSESL KFSQEIHNSI DDHDYGKLAD LCVSQIKNLE FSQFLDFLGT
KNVEKRLEMC EKWMQMQRET KALQLKMAVP GNSEIPKKIN KQRIPNSKNQ VEQLEEKLSA
IEFSEEVSDR VFSELHRLKN MNPQQSEYTV LMNWLELVSN LPWNTSTVDD IEINKARKIL
EDSHESMDDV KQRVLEHLAV CKINNSVKGM ILCFTGPPGI GKTSIAKAIA ESMGRKFQRV
SLGGIRDESD IRGHRRTYVA AMPGRIIEAL KHCKSNNPVF LLDEVDKLYS GNQGSPSAAL
LELLDPEQNS TFHDHYLNIP FDVSKIMFIA TANDVERLEP ALKDRLEIIE MSGYSMKEKV
KICENHLVNR QLSKHCISPD YVNLDRHAIM AMIEEFTMEA GVRQLERNVG AVCRHVALRL
AEALNSDPSA DVLPDMDLPI QIGEPDIHKI LKAKHMKRVK IVEKMRPLPP GVCFGLSVTT
NGGRVMPIEA SKCKGTGKIV TTGHLGKVLE ESILVAKGWL GANAEKLGLK TLEENDIHVH
LPAGAVNKDG PSAGTGLACA LVSLAMGVPL RSDAAVTGEI SLTGHVLAIG GVKEKVLAAQ
REGLRRVVLP KSNEEEYLKI DEDIRNEMDV VLADTVEDVI EAMMEKEPVL AKL
