LONM4_ARATH
ID LONM4_ARATH Reviewed; 942 AA.
AC Q9M9L7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Lon protease homolog 4, chloroplastic/mitochondrial;
DE Short=AtLon4;
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
GN Name=LON4; OrderedLocusNames=At3g05790; ORFNames=F10A16.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=17478548; DOI=10.1093/pcp/pcm052;
RA Ostersetzer O., Kato Y., Adam Z., Sakamoto W.;
RT "Multiple intracellular locations of Lon protease in Arabidopsis: evidence
RT for the localization of AtLon4 to chloroplasts.";
RL Plant Cell Physiol. 48:881-885(2007).
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, ECO:0000269|PubMed:17478548}. Plastid, chloroplast
CC thylakoid membrane {ECO:0000269|PubMed:17478548}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17478548}; Stromal side
CC {ECO:0000269|PubMed:17478548}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC012393; AAF26081.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74297.1; -; Genomic_DNA.
DR RefSeq; NP_566259.1; NM_111453.1.
DR AlphaFoldDB; Q9M9L7; -.
DR SMR; Q9M9L7; -.
DR STRING; 3702.AT3G05790.1; -.
DR MEROPS; S16.A02; -.
DR PaxDb; Q9M9L7; -.
DR PRIDE; Q9M9L7; -.
DR ProteomicsDB; 238473; -.
DR EnsemblPlants; AT3G05790.1; AT3G05790.1; AT3G05790.
DR GeneID; 819748; -.
DR Gramene; AT3G05790.1; AT3G05790.1; AT3G05790.
DR KEGG; ath:AT3G05790; -.
DR Araport; AT3G05790; -.
DR TAIR; locus:2074469; AT3G05790.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q9M9L7; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q9M9L7; -.
DR PRO; PR:Q9M9L7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9L7; baseline and differential.
DR Genevisible; Q9M9L7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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 PIRSF; PIRSF001174; Lon_proteas; 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; Chloroplast; DNA-binding; Hydrolase; Membrane; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Plastid; Protease; Reference proteome;
KW Serine protease; Thylakoid.
FT CHAIN 1..942
FT /note="Lon protease homolog 4, chloroplastic/mitochondrial"
FT /id="PRO_0000045425"
FT DOMAIN 79..299
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 756..940
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 673..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 846
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 889
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 456..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P93655"
SQ SEQUENCE 942 AA; 104925 MW; 90F3238714F4C52E CRC64;
MLKFLTPTAY ASHHVTPATR FRSTPVKNLL FKQLTLLTGW NRSSYELGRR SFSSDLDSDT
KSSTTTVSAK PHLDDCLTVI ALPLPHKPLI PGFYMPIYVK DPKVLAALQE SRRQQAPYAG
AFLLKDDASS DSSSSSETEN ILEKLKGKEL INRIHEVGTL AQISSIQGEQ VILIGHRQLR
ITEMVSESED PLTVKVDHLK DKPYDKDDDV IKATYFQVMS TLRDVLKTTS LWRDHVRTYT
QACSLHIWHC LRHIGEFNYP KLADFGAGIS GANKHQNQGV LEELDVHKRL ELTLELVKKE
VEINKIQESI AKAVEEKFSG DRRRIILKEQ INAIKKELGG ETDSKSALSE KFRGRIDPIK
DKIPGHVLKV IEEELKKLQL LETSSSEFDV TCNYLDWLTV LPWGNFSDEN FNVLRAEKIL
DEDHYGLSDV KERILEFIAV GGLRGTSQGK IICLSGPTGV GKTSIGRSIA RALDRKFFRF
SVGGLSDVAE IKGHRRTYIG AMPGKMVQCL KNVGTENPLV LIDEIDKLGV RGHHGDPASA
MLELLDPEQN ANFLDHYLDV PIDLSKVLFV CTANVTDTIP GPLLDRMEVI TLSGYITDEK
MHIARDYLEK TARRDCGIKP EQVDVSDAAF LSLIEHYCRE AGVRNLQKQI EKIFRKIALK
LVRKAASTEV PRISDDVTTD TEETKSLAKT DLESPETSAE GSTVLTDELA TGDPTESTTE
QSGEVAETVE KYMIDESNLS DYVGKPVFQE EKIYEQTPVG VVMGLAWTSM GGSTLYIETT
FVEEGEGKGG LHITGRLGDV MKESAEIAHT VARRIMLEKE PENKLFANSK LHLHVPAGAT
PKDGPSAGCT MITSLLSLAL KKPVRKDLAM TGEVTLTGRI LAIGGVKEKT IAARRSQVKV
IIFPEANRRD FDELARNVKE GLEVHFVDEY EQIFELAFGY DH
