ID LONM_MAIZE Reviewed; 964 AA.
AC P93648;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
GN Name=LON2;
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).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND SUBUNIT.
RA Mertova J., Almasiova M., Perecko D., Bilka F., Benesova M., Bezakova L.,
RA Psenak M., Kutejova E.;
RT "ATP-dependent Lon protease from maize mitochondria - comparison with the
RT other Lon proteases.";
RL Biologia 57:739-745(1998).
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:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homoheptamer. Organized in a ring with a central cavity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|Ref.2}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U85495; AAC50021.1; -; mRNA.
DR PIR; T04325; T04325.
DR RefSeq; NP_001105895.1; NM_001112425.1.
DR AlphaFoldDB; P93648; -.
DR SMR; P93648; -.
DR STRING; 4577.P93648; -.
DR PaxDb; 4577-GRMZM2G113056_P01; -.
DR GeneID; 732810; -.
DR KEGG; zma:732810; -.
DR MaizeGDB; 136450; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_3_1; -.
DR InParanoid; P93648; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P93648; baseline and differential.
DR Genevisible; P93648; ZM.
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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease.
FT CHAIN 1..964
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000026740"
FT DOMAIN 89..300
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 773..957
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 663..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 863
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 906
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 964 AA; 105659 MW; D78A6C6B0F8A6D9E CRC64;
MLRAAVAAAE ELRSPLLRVI GTLRDGRGSV LLGRRVRFCS NSSASDTEAA VAEAEAKAED
ASAAEGEADS KASSAIVPTS TNIDDCLSVI ALPLPHRPLF PGFYMPINVK DQKLLQALIE
NRKRSAPYAG AFLVKDEEGT DPNIVTGSDS AKSIDDLKGK DLLKRLHEVG TLAQITSIQG
DHVVLLGHRR LRITEMVEED PLTVKVDHLK EKPYNKDDDV MKATSFEVIS TLREVLRTSS
LWKDHVQTYT QHIGDFNYQR LADFGAAISG ANKLLCQEVL EELDVYKRLK LTLELVKKEM
EISKLQQSIA KAIEEKISGD QRRYLLNEQL KAIKKELGLE TDDKTALSAK FRERIESKKD
KCPPHVLQVI EEELTKLQLL EASSSEFSVT RNYLDWLTVL PWGNYSDENF DVHHAQKILD
EDHYGLSDVK ERILEFIAVG KLRGTSQGKI ICLSGPPGVG KTSIGRSIAR ALNRQFYRFS
VGGLADVAEI KGHRRTYVGA MPGKMVQCLK SVGTANPLVL IDEIDKLGKG HSGDPASALL
ELLDPEQNVN FLDHYLDVPI DLSKVLFVCT ANVIEMIPNP LLDRMEIIAI AGYITDEKMH
IARDYLEKNT RQACGIKPEQ VEVTDTALLA LIENYCREAG VRNLQKQIEK IYRKIALQLV
RQGVSNEPDH ESVSASVTEE SGNGDNTTTK DEILKDPAVE DASVTNNVTN PASEEANEEN
LTSEAAKEDS TSKGNKGTDG AADKAIEKVV VDSSNLGDFV GKPVFQAERI YEHTPVGVVM
GLAWTAMGGS TLYIETKKVE EREGKGALVL TGQLGDVMKE SAQIAHTVGR AVLLEKEPDN
HFFANSKVHL HVPAGSTPKD GPSAGCTMIT SMLSLAMGKP VKKDLAMTGE VTLTGRILPI
GGVKEKTIAA RRSAIKTLIF PAANKRDFDE LASNVKEGLE VHFVDTYSEI YDLAFQSDAG
TETS
//
