ID M5WHA3_PRUPE Unreviewed; 997 AA.
AC M5WHA3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_03120};
GN ORFNames=PRUPE_6G313300 {ECO:0000313|EMBL:ONI04281.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI04281.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI04281.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC in a site-specific manner. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03120, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM007656; ONI04281.1; -; Genomic_DNA.
DR RefSeq; XP_007204961.1; XM_007204899.1.
DR AlphaFoldDB; M5WHA3; -.
DR STRING; 3760.M5WHA3; -.
DR EnsemblPlants; ONI04281; ONI04281; PRUPE_6G313300.
DR GeneID; 18774588; -.
DR Gramene; ONI04281; ONI04281; PRUPE_6G313300.
DR KEGG; pper:18774588; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_2_0_1; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000006882; Chromosome g6.
DR GO; GO:0005759; C:mitochondrial 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; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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_03120; lonm_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; IPR027503; Lonm_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; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
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_03120}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120,
KW ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT ACT_SITE 897
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 940
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 997 AA; 109879 MW; 303A9A9E01902FF8 CRC64;
MLKLLSSSSS CLQARVHSLG PNLGLRPGPT ELASPFLRVL GSLTGLTRPN SSRRAFFCSD
ASDGSDQVVE VEAKKAGTEG EAESKSSSAI VPTNPRPEDY LTVLALPLPH RPLFPGFYMP
IYVKDPKLLA ALQESRKRQA PYAGAFLLKD EPGTDPSVVS GSETDKSISD LKGKELFNRL
HEVGTLAQIS SIQGDQVVLI GHRRLRITEM VDEDPLTVKV DHLKDKPYNK DDDVIKATSF
EVISTLRDVL KTSSLWRDHV QTYTQHIGDF NFPRLADFGA AISGANKLQC QQVLEELDVY
KRLKLTLELV KKEIEISKIQ ESIAKAIEEK ISGEQRRYLL NEQLKAIKKE LGLEADDKTT
LSAKFRERLE PNREKCPPHV LQVIEEELTK LQLLEASSSE FNVTRNYLDW LTSIPWGNYS
DENFDVLRAQ KILDEDHYGL SDVKERILEF IAVGKLRGIS QGKIICLSGP PGVGKTSIGR
SIARALNRKF YRFSVGGLSD VAEIKGHRRT YIGAMPGKMV QCLKNVGTAN PLVLIDEIDK
LGRGHAGDPA SALLELLDPE QNANFLDHYL DVPIDLSKVL FVCTANVVEM IPNPLLDRME
VISIAGYITD EKMHIARDFL EKTTREACGI KPEQVEVTNA ALLALIENYC REAGVRNLQK
HIEKIYRKIA LQLVRQGVSD EPEVAHQIES PTSQIDGPNE SAVVEAQVAE TDEAKVEDVD
KLDQNVVASE SQTASESLET DLPVEPAVGE VQVADTDEPM DSKDAKKTDK IQENETTKTV
DKVLVDESNV ADFVGKPVFH AERLYDQTPV GVVMGLAWTA MGGSTLYIET TQVEEGEGKG
SLNVTGQLGD VMKESTQIAH TVARAILLNK EPDNPFFANS KLHLHVPAGA TPKDGPSAGC
TMITSMLSLA MKKPVKKDLA MTGEVTLTGR ILPIGGVKEK TIAARRGEVR TIIFPAANRK
DFDELAPNVK EGLDVHFVDD YNQIFDLAFS DDQSKLK
//
