LON_METST
ID LON_METST Reviewed; 825 AA.
AC Q2NEP8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Msp_1328;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; CP000102; ABC57705.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NEP8; -.
DR SMR; Q2NEP8; -.
DR STRING; 339860.Msp_1328; -.
DR PRIDE; Q2NEP8; -.
DR EnsemblBacteria; ABC57705; ABC57705; Msp_1328.
DR KEGG; mst:Msp_1328; -.
DR eggNOG; arCOG02161; Archaea.
DR HOGENOM; CLU_004109_4_3_2; -.
DR OMA; KKMNPVM; -.
DR Proteomes; UP000001931; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
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; 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; PTHR10046; PTHR10046; 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; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..825
FT /note="Lon protease"
FT /id="PRO_0000396619"
FT DOMAIN 41..235
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 625..805
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 711
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 754
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 825 AA; 92970 MW; 19D9BC4FE88B491B CRC64;
MTQEMENENL SFTQQLRKDG FIKDIDTNPT CFDDTDSQNQ LPIIFIPNTI LLPHTDITLN
LDKQHTDNLL HTVDDNNHGI ILTPKKLEEG NGNVEFYDVG VILEIKSLTE DKENELLPEE
YVLELKVKDK VYVNKILKKD GFFHAQYKIL PEENTLTEDE ITELNKNIDE TVLEIAKFLP
NTDKYTRKIL GKLDTQDKLA EVFPFLKVPI NKKQELLELD SVKIRALKVI QLLLEQKDAI
GIQMELAKKL NKKMNETHKN TLLREQMKLI QEELNMTDDT PAHKTYRERI KDAQLPKEVE
EAALEEVTKL ERQGQNNAEE NIIRNYLDTI LQLPWHKEEN PTIDIVKAKK QLNDDHYGLK
KVKTRIIQHL TVLKMKKDKQ GSILLFVGPP GTGKTSLGKS IAAALERPYV RVSLGGVNDE
SEIRGHRRTY LGALPGRIIN GMKKAGKTNP VFVLDEIDKM TESLNGNPTS ALLEVLDPEQ
NDSFSDNYLE VPYDLSDVFF IGTANSLQDI PGPLRDRLEI IELDSYTNTE KHHIADEHLI
KEVLLEHGLT EDDLKITYDA IDCLIEKYTR ESGVRGLKRE IAAIARYVTE KIVVDNVERP
YVVDENMLYD ILGHEKSHYD KVPDSNPPGV VTGLAWTPIG GDILFIEAVL LPGEEKLKLT
GQLGDVMKES AQIAQSLIKS RLATVLKDSD IEKRDIHIHV PAGSIPKDGP SAGVTLLTTI
ASLVTNTPVD STLAMTGEIS LRGKVLPVGG IKEKVIAAHR SGIKTVLLPE ENMKDLDDVP
CEVKDDMTFK PMKTVDEVLY EALGLKLPEN KPLNISIDEI NKVTP
