LONM_CAEBR
ID LONM_CAEBR Reviewed; 960 AA.
AC A8XFM8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 5.
DT 03-AUG-2022, entry version 89.
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=lonp-1 {ECO:0000312|WormBase:CBG12802};
GN ORFNames=CBG12802 {ECO:0000312|WormBase:CBG12802};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP31724.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HE600940; CAP31724.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002640277.1; XM_002640231.1.
DR AlphaFoldDB; A8XFM8; -.
DR SMR; A8XFM8; -.
DR STRING; 6238.CBG12802; -.
DR GeneID; 8582273; -.
DR CTD; 8582273; -.
DR WormBase; CBG12802; CBP42408; WBGene00033694; Cbr-lonp-1.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; A8XFM8; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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; 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..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 57..960
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395763"
FT DOMAIN 92..350
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 773..960
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 195..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 867
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 910
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 960 AA; 106955 MW; 658262FAF61BA8F3 CRC64;
MYRAGALVLR SATLRRTRFL AAHQNFATIS SQRSSVLLAK SLESSIGGAG NQKKFYSSKD
HDDPIAVDDS LELYKDLGGM SPIQVPADMP NVPILAINRY PLFPGFIKKV DIVKDDNLKA
LIRRQLSLKQ PYAGVFVKKD DENKEETIVS LSEVYPTGSF VQIIEVRDQG SVLELVLSAH
RRIRVIEPIE DVVAPKTDTP LNGRRARGKR AGLPPTPPPT PPLSTPTSAP EASATSPEEK
EEKKDPERKG IVMVRTENVV ADPVPKNNET KATMMAIVQT IRDVVQFNQL FGQQINLLLH
PSQNVIDNPV YLCDLVATLV QSAETKDLQE MMDETDVSKR LKIALLLIQK EKAVAKLKHD
INKDVEKKVQ DHHRKYLLNE QLKVIKKELG IEKDEKTTII EKIDERMKTL AVPEYALKVI
NEEKTKLQFL DPHSSEFSVT RNYLEWLTSV PWGLTSPENR RLSHAKKALD EGHYGMKDVK
ERIMEFIAVN LLRKSVGGKI LCFHGPPGVG KTSIAKSIAN ALNREYFRFS VGGMTDVAEI
KGHRRTYVGA MPGKMIQCMK KVKTENPLVL IDEVDKIGGA GFHGDPASAL LELLDPEQNA
NFNDHFLDVP VDLSRVLFIC TANEISKIPG PLRDRMEMID VSGYLAEEKV AIAHQHLIPQ
LRKETSLSAD QLNIEDSALE ELIKHYCRES GVRNLQQHIE RIFRKAALQI AEQQPEDEQP
AATTAISENS DAEPVSTPSD PPTFTPEKIN ISTENLQKFV GRPKFTSDRM YEVTPPGVIM
GLAWTAMGGS ALYIETVLKR PVDVTSDKDG SIETTGNLGD VMKESVRTAL TVSKGILARE
QPDNKFFDKS HIHIHVPEGA TPKDGPSAGV TLVSSLLSLA LNRPVVQDMA MTGEISLTGK
VLPVGGIREK IIAARRVGAK RVFLPAENRR DFDDLPEFMK SELDIRFVSH YDELYEHLFQ
