ID   LONM1_DICDI             Reviewed;         956 AA.
AC   Q54YV4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 3.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Lon protease homolog, mitochondrial 1 {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
GN   ORFNames=DDB_G0278063;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- 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   -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC       central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAL68204.2; Type=Miscellaneous discrepancy; Note=The initiator methionine is coded by a AGG arginine codon. EST data suggests that the genomic sequence of the start codon is incorrect.; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000023; EAL68204.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_642098.2; XM_637006.2.
DR   AlphaFoldDB; Q54YV4; -.
DR   SMR; Q54YV4; -.
DR   STRING; 44689.DDB0235386; -.
DR   PaxDb; Q54YV4; -.
DR   EnsemblProtists; EAL68204; EAL68204; DDB_G0278063.
DR   GeneID; 8621309; -.
DR   KEGG; ddi:DDB_G0278063; -.
DR   dictyBase; DDB_G0278063; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   InParanoid; Q54YV4; -.
DR   PhylomeDB; Q54YV4; -.
DR   PRO; PR:Q54YV4; -.
DR   Proteomes; UP000002195; Chromosome 3.
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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR027503; Lonm_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43718; PTHR43718; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 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   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease.
FT   CHAIN           1..956
FT                   /note="Lon protease homolog, mitochondrial 1"
FT                   /id="PRO_0000395764"
FT   DOMAIN          159..355
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          747..945
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        851
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        894
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         511..518
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   956 AA;  108047 MW;  EA2509BAA8EDCEB6 CRC64;
     MLSINNKLKN LKLSTVKNLY NKSSSISIIL VNNNNNNNNN NNNNNNNNNN NNNNNNNFIS
     LSTTNLFNQK LCIESYKKVN YCKKKGGGNK NNDDNDNEKN EKNEKKVKNE KKEKNEKNDG
     NEKVEIVEDN DLIVPLSKEL LQFDKPSNKR KDWPLNSEVV IYPSNSVNFI GTTGPINLGF
     QFITRLVPNA SGKTFLGFFL CKDAYRNNNN QIGRTIDSIH NVGVLAQVTL SPSGIYHFET
     IKRIRIKEVQ NGQFPFIASI EPLSNDEREL KDPRIAELMT KINVLSLEYR KLYPDVYTIN
     SVDFENQIEV IDNPDYYLAA VINYYGLNYP DECQKILETQ SVVKRLEMLY HMILNEQPLL
     ALQQKIAKDL DDKTTAYKNK LLLTEQLKKL KALLGNETDE KEKTIEKYQN KLSELTLISE
     SSKKVIQDEI YKISTIDPSS SEYSALKNYL EWLTNLPWGI YSADYFDLKH SKMVLDSDHY
     GLEDIKQRIL EFISVGHIKG TVQGKILCFI GPPGTGKTSI AKSIAKALKK EFFRFSVGGL
     FDESEIKGHR RTYVGSMPGK IIQALKITQT SNPVILIDEI DKIGKRNHGD PSSALLEVLD
     PEQNVSFVDH YLDTPYDLSK VLFICTANSG QDIPAALSDR MEIIRLPGYV EEEQIEIVKN
     FIIPKTFIDC GIKLDQLSIS DDVIKQIVKF YSREVGIREL EKLIEKIMRK TALKLVNGTA
     ERVDLTLDNL EQYLGIPSYT SDRYYDVTPI GVVNGLAYTK KGGATLYIES TSEEIQKPLS
     SLPPSQQQQN QLEPSIKTTG NLGDVMSESS TIAYTFAKNF LYELDPNNTF FSNHNIHLHS
     PQGNIPKDGP SAGVTMVTSL LSLALNEPVQ NNLGMTGEVT ITGKVITIGG VKEKTIAAKR
     SGLTSVIFPI NNRINFEELP TYIKNDIDVT YANDYKDVFE VAFPNKKYLL NNLKTF