ID   LONM_KLULA              Reviewed;        1111 AA.
AC   Q6CNR9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
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};
DE   Flags: Precursor;
GN   Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120};
GN   OrderedLocusNames=KLLA0E10407g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; CR382125; CAG99507.1; -; Genomic_DNA.
DR   RefSeq; XP_454420.1; XM_454420.1.
DR   AlphaFoldDB; Q6CNR9; -.
DR   SMR; Q6CNR9; -.
DR   STRING; 28985.XP_454420.1; -.
DR   MEROPS; S16.010; -.
DR   PRIDE; Q6CNR9; -.
DR   EnsemblFungi; CAG99507; CAG99507; KLLA0_E10407g.
DR   GeneID; 2894249; -.
DR   KEGG; kla:KLLA0_E10407g; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_1_0_1; -.
DR   InParanoid; Q6CNR9; -.
DR   OMA; YVGPPIY; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0000262; C:mitochondrial chromosome; IEA:EnsemblFungi.
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:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:1901858; P:regulation of mitochondrial DNA metabolic process; IEA:EnsemblFungi.
DR   Gene3D; 2.30.130.40; -; 1.
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; 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_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   SUPFAM; SSF88697; SSF88697; 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; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   CHAIN           22..1111
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000395780"
FT   DOMAIN          185..448
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          899..1085
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          85..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..835
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..851
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..866
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        991
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        1034
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         602..609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   1111 AA;  124188 MW;  EC35337C9F00F3B6 CRC64;
     MLRSSRSRLV TRNILLRQFK NGNNVRLMNA TRFQHNGIVG NEKLASDSQK FVDESYHWMQ
     YRKQMNDPVS RQRLEQLESQ WVKSIQLKQD DKGKDIDQPE SENRKKEEEQ VPTEEKDNDT
     AKESETSQQR DSVAETQGPA STSGGASGNG ESSGNGSGDD GNNGSGNGKP SKNAKQPFPE
     VYPQVMALPI SRRPLFPGFY KAVVISDERV MKAIKDMSDR QQPYIGAFLL KDSTVDTDVI
     HKADEVYNVG VFAQVTSAFP SKDEKTGAET MTALLYPHRR IKLDELIPPT SEQNLKDESD
     VSKSEGVENN EQEVVKASLQ KMENMKDVEE DDDENLTGFL KDYDVSLVNV SNLADKEFNP
     NSPVINALTS EILKVFKEIS QLNTMFREQI ATFSASIQSA TTNIFEEPAR LADFAAAVSA
     GEEEELQEIL ESLDIEQRLE KALTVLKKEL MNAELQNKIS KDVETKIQKR QREYYLMEQL
     KGIKRELGID DGRDKLIESF KDRVSKLQLP ETVQKVFDDE ITKLATLETS QSEFGVIRNY
     LDWITSLPWG IISKEQYSIP KAKKILDEDH YGMKDVKDRI LEFIAVGKLL GKVDGKIICF
     VGPPGVGKTS IGKSIARSLN RQFFRFSVGG MTDVAEIKGH RRTYIGALPG RVIQALKKCQ
     TQNPLILIDE IDKIGHGGIH GDPAAALLEL LDPEQNNSFL DNYMDIPIDL SKVLFVCTAN
     SLETIPRPLL DRMEVIELTG YVAEEKVKIA ENYLSPSAKK SAGLDNANVN ITENAIVSLM
     KHYCRESGVR SLKKHIEKIY RKAALNVVKQ LSIDDKPMEN EEVKDQKDIK VKQSENKSSA
     EASTVESTTE ENELIKTQKS HDNKGSLEVP ETVSVTVDEN NLKDYVGPPI FTTDRLYEST
     PPGVVMGLAW TSMGGCAMYV ESVLEQPLTH STQPTLERTG QLGDVMKESS RLAYSFSKMY
     LAKKFPENRF FEVAKIHLHC PEGATPKDGP SAGVTMASSF LSLALNKGLD PTVAMTGELT
     LTGKVLRIGG LREKAVAAKR SGAKTIIFPK DNLSDWAELP ENVKEGLEPL AADWYEDVFQ
     RLFGDVDTNK GNTVWSEDFK KIDEKRNKET K