ID   LONM2_DICDI             Reviewed;         836 AA.
AC   Q550C8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Lon protease homolog, mitochondrial 2 {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
GN   ORFNames=DDB_0217928, DDB_G0277307;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
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}.
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DR   EMBL; AAFI02000019; EAL68840.1; -; Genomic_DNA.
DR   RefSeq; XP_642688.1; XM_637596.1.
DR   AlphaFoldDB; Q550C8; -.
DR   SMR; Q550C8; -.
DR   STRING; 44689.DDB0304635; -.
DR   MEROPS; S16.A13; -.
DR   PaxDb; Q550C8; -.
DR   EnsemblProtists; EAL68840; EAL68840; DDB_G0277307.
DR   GeneID; 8620877; -.
DR   KEGG; ddi:DDB_G0277307; -.
DR   dictyBase; DDB_G0277307; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_2_0_1; -.
DR   InParanoid; Q550C8; -.
DR   OMA; NSIHIHA; -.
DR   PhylomeDB; Q550C8; -.
DR   PRO; PR:Q550C8; -.
DR   Proteomes; UP000002195; Chromosome 2.
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; 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   SMART; SM00382; AAA; 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.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease.
FT   CHAIN           1..836
FT                   /note="Lon protease homolog, mitochondrial 2"
FT                   /id="PRO_0000395765"
FT   DOMAIN          1..235
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          627..805
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          24..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        711
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        754
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         391..398
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   836 AA;  93649 MW;  808A904DD5A27DF2 CRC64;
     MGSPTHFGLF LISDAEREVH MEELKSQEAS KSKPPSKPKS NFTTFSHGTP DLSKIHKVGM
     LATVCRTQGY FVLGGGPIIE ITGVSNDHDN NNSNLVEITE SKNDTSDSTT TTTTTPSTSI
     TPITTPVVPQ IPTSKYLKVS IEPHEYSELG DSLTVRALRL QLVKCIYSAI NRYQDSSFAQ
     HLKQICMLPI FKMDDSSLLN SIGPLCISSP SEYQKLLECK SLEEKLNMVL SMLVKKCEVF
     DFNFSIEKQL EEKTMAQQKK YFLTEQMKLI RKELGIDLDE KETIKNKFNS RWKEIAVMDK
     QILQVFKEEM DKLSSCESNS SEYNTSRNYL DWMTLLPWNV YTNDNFDISK VKEILDRDHY
     GLKDIKEMIQ TFIAVGKLRG SIGGKVILLV GPPGTGKTSV GKSIANALGR QFHRISVGGL
     SDVSEIKGHR RTYVASMPGK IIQALKTVKT SNPVILIDEI DKISRSSQGD PNSALLEVLD
     PQQNKNFVDY YLDVPYDLSR VLFICTANDA DSIPAPLLDR MEVMTLNGYI QSEQMEIAKR
     YLLPLVRKET GISEEQLQFT PEAIKKLCEL YCREAGVRNL KKFIDKIFRK MAYKLSMGME
     QSVIITPDNL EQYVGPIKYP SSRLFQKQKP GIVMGLGGSL IHIESALDRF TNGPTVTTTG
     SLGLVMRESI DISYSYVKDF LLKVDASNDY FLKNSIHIHA PDGSTQKDIS SAGITIVSSL
     LSLATGKLVK PDLAMVGEVS LTGKVIGVSG IVEKIVLAKR ESIKTIIIPK ENKKQLEEIP
     DFIKEGIEIY LVDYYSDVYS IAFTNDSTIK PLIFNDNKEN QNENENQSEV KSTIIQ