ID A0A2K6UGB2_SAIBB Unreviewed; 959 AA.
AC A0A2K6UGB2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
DE AltName: Full=Lon protease-like protein {ECO:0000256|HAMAP-Rule:MF_03120};
DE Short=LONP {ECO:0000256|HAMAP-Rule:MF_03120};
DE AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000256|HAMAP-Rule:MF_03120};
DE AltName: Full=Serine protease 15 {ECO:0000256|HAMAP-Rule:MF_03120};
GN Name=LONP1 {ECO:0000256|HAMAP-Rule:MF_03120,
GN ECO:0000313|Ensembl:ENSSBOP00000030935.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000030935.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000030935.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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
CC promoters and RNA in a single-stranded, site-specific, and strand-
CC specific manner. May regulate mitochondrial DNA replication and/or gene
CC expression using site-specific, single-stranded DNA binding to target
CC the degradation of regulatory proteins binding to adjacent sites in
CC mitochondrial promoters. {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. Organized in a ring with a central cavity. The
CC ATP-binding and proteolytic domains (AP-domain) form a hexameric
CC chamber, while the N-terminal domain is arranged as a trimer of dimers.
CC DNA and RNA binding is stimulated by substrate and inhibited by ATP
CC binding. Interacts with TWNK and mitochondrial DNA polymerase subunit
CC POLG. {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}.
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DR AlphaFoldDB; A0A2K6UGB2; -.
DR Ensembl; ENSSBOT00000047823.1; ENSSBOP00000030935.1; ENSSBOG00000031618.1.
DR GeneTree; ENSGT00530000063553; -.
DR Proteomes; UP000233220; Unplaced.
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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03120}; 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:UP000233220};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}; Transit peptide {ECO:0000256|HAMAP-Rule:MF_03120}.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT CHAIN 68..959
FT /note="Lon protease homolog, mitochondrial"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT /id="PRO_5023303194"
FT DOMAIN 124..368
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 759..949
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 76..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 855
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 898
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 523..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 959 AA; 106579 MW; 8A84C1AF03FD2E58 CRC64;
MAAGTGYVRL WGAARCWALR RPMLAAAGGR VPTAAGAWLL RGRRACDASP PWTLWGRGPA
IGGQWRGLWE ANSRGGGAFS GEDDASEGGA EEGAGGTGGS AGGGEGPVIT ALTPMTIPDV
FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDNNESDVVE
NLDEIYHTGT FAQIHEMQDL GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK
RGRKEAEDEL GTRHPAELAM EPATELPGEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNIPKRLY
KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK
FRERLKELVV PKHVMDVVDE ELSKLGLLDN HSSEFNVTRN YLDWLTSIPW GKYSDENLDL
ARAQAVLEED HYGMEDVKKR VLEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL
NREYFRFSVG GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLVLID EVDKIGRGYQ
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG
YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI KQYCRESGVR NLQKQVEKVL
RKSAYKIVSG EAESVEVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV
ETSLRRPRDK DGKGEKDGSL EVTGQLGEVM KESARIAYTF ARAFLMQHAP DNEYLVTSHI
HLHVPEGATP KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKVL PVGGIKEKTI
AAKRAGVTCI VLPAENKKDF YDLAGFITEG LEVHFVEHYH QIFDIAFPEE QAEAVAVER
//
