ID A0A3R7MUL9_9STRA Unreviewed; 1332 AA.
AC A0A3R7MUL9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BBI17_009242 {ECO:0000313|EMBL:RLN38412.1}, BBO99_00008234
GN {ECO:0000313|EMBL:RLN75563.1}, JM16_008121
GN {ECO:0000313|EMBL:KAG2512340.1}, JM18_009112
GN {ECO:0000313|EMBL:KAG2508746.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN38412.1, ECO:0000313|Proteomes:UP000285883};
RN [1] {ECO:0000313|EMBL:KAG2508746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2512340.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2508746.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN38412.1}, and Chile4
RC {ECO:0000313|EMBL:RLN75563.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2508746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2512340.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2508746.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN38412.1}.
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DR EMBL; JPWU03000676; KAG2508746.1; -; Genomic_DNA.
DR EMBL; JPWV03000412; KAG2512340.1; -; Genomic_DNA.
DR EMBL; MAYM02000429; RLN38412.1; -; Genomic_DNA.
DR EMBL; MBDN02000406; RLN75563.1; -; Genomic_DNA.
DR STRING; 325452.A0A3R7MUL9; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR Proteomes; UP000792063; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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: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 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; IPR001810; F-box_dom.
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; PS50181; FBOX; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000285624};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 199..243
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 516..721
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 1147..1331
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 164..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..77
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 113..150
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 258..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 328..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 473..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1237
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1280
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 879..886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1332 AA; 149771 MW; 9BE405712FD8136F CRC64;
MLQRTSDLVR RTIEQEEAQC TQNRHIFTEV QSILDDIVYD VENCEHECEL VQLRRQLATA
ESSLSEYQER ETELIQERQQ AYEYAVKVEQ DGRSIMSKLN EHLAVVVAEL TKKEVMEREL
QQTKEHLKLT SQLSKELASA QREIRELRRA NDIQHLLKSS TVPVKPASDM RIPSRGNNVP
KQVKSAGNES SLIANSEEAN VFSQLPAKVM LKLFSYLDED SMVAISVTDR VLLSKVDAIV
KSLKPDQIKF FHDMSTRVKT LEAHLAQVQT EKEDVAARLY SAENVRDFLM EKLKDLEDTL
ANNMTMTAKK DEQAGLDREI IGFLDAKTQE YETALKEYAK QNDGLRMEIV HLREDYASKT
TIIQDMVELL TDEKKELEAQ SQRKILILHV TQSSTHQIVS AFRIVLPPAF MATAALRRFA
LTRPHVPANT TNTLRFHRPL VASQRVRSNP FGLEFRSPQL FTALYSTSSG DGDDGKTPKD
TDKSKEEDED PSVEVVIDND LATVGEGDKA PTYPHVLAMP AHRRPFFPGV VLPMTITNPE
VTRALMALKE SGQKYVGVFL KKSSGDPLKT GGQEDLVKNL SEIHHVGSFA RIDNMLPFDA
NSVQVLMVSQ RRIAIDDVRD EGPPLRVNIS NLDNPSYDPK SKLIRAYSNE IVATLREIVK
MNPLFKDHMQ YFSQRIDIHN PYKLADFAAS VTSADGEELQ QVMEEMSCEA RLKKALELIT
KELELSKVQQ TIKEQVEEKV SKNQRNYLLM EQLKAIKKEL GMEKDDKDAM ITKYRERLAQ
LEPGSIPESV NEVVEDELNK MSMLEKNSSE FNVTRNYLDW LTQLPWGKAT EENFDLAKAK
QILDEDHYGL KDIKERILEF IAVSKLKGDV QGKIICFVGP PGVGKTSIGK SIARSLNREF
YRFSVGGLSD VAEIKGHRRT YVGAMPGKII QCLKSTQSSN PLILIDEIDK LGRGYQGDPA
SALLELLDPS QNSGFVDHYM DVPVDLSRVL FICTANVTDT IPGPLLDRME VLRLSGYDSP
EKLAIAKEYL VPKALERTGL QKSETTPESL GLTDEAILTL VKQYCRESGV RNLEKHVEKV
FRKVALEVVE DIESANGAQI QDAGESTTAT KDMEEVSSDE DRFLITPDKL AKYVGKPIFT
SDRMFEKQFP GVVMGLAWTA MGGASLYIET TKVETKADRS GLITTGQMGS VMEESTKIAH
TYARSKMHQI DPESKFFEEN EVHLHVPEGA TPKDGPSAGC TMVTALLSLA MNKTVKPDLA
MTGELSLVGK VLPVGGIKEK TIAAKRSGVK TLILPLGNQR DFEELEEYLR KDLDVHFADY
YDDVYKVAFE QE
//
