LON_METBF
ID LON_METBF Reviewed; 802 AA.
AC Q469F5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Mbar_A2576;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(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}.
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; CP000099; AAZ71487.1; -; Genomic_DNA.
DR AlphaFoldDB; Q469F5; -.
DR SMR; Q469F5; -.
DR STRING; 269797.Mbar_A2576; -.
DR EnsemblBacteria; AAZ71487; AAZ71487; Mbar_A2576.
DR KEGG; mba:Mbar_A2576; -.
DR eggNOG; arCOG02161; Archaea.
DR HOGENOM; CLU_004109_4_3_2; -.
DR OMA; KKMNPVM; -.
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 Serine protease; Stress response.
FT CHAIN 1..802
FT /note="Lon protease"
FT /id="PRO_0000396618"
FT DOMAIN 17..209
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 600..780
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 686
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 729
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 363..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 802 AA; 88744 MW; 9237A7900E22CBC2 CRC64;
MRRLTMYPEQ PDENRESIVM PLFEVVVYPK SRAKFLADKV TGEILLNDMK NAESVSAIGL
TVKNGTKASD LSEESLYKIG NLLNITYVQP SDDGYLVVAK GIERVEAVSL YQKNGLFYAT
YRPVHDLPDF DEDAETEVMA NIKKTIHEIS ARFQGSEQFT KSIDKMDSID QIMGFVMPYI
PVKLAEKQRL LELASVRERY LLFLHILTKH KENINLQIEM AKKVTDKISK SNREAMLREQ
LKVIQEELNE GDDSASGDAA YREKIENSTM PDEVKKKAFS ELKKLETGGS HNPEAPGIRN
YLDLLLDLPW ITEEKKSIDI AEARRVLESN HNGLEKVKER IIQHLAVMKL KHEKQGSILL
LIGPPGTGKT SLGKSIADAL GRKYIRISLG GVKDEAEIRG HRRTYIGALP GRIIQGMRKA
GTKNPVFILD EVDKLSASYS GDPASALLEV LDPEQNSTFS DHYLEIPYDL SDVLFIATAN
SMANIPWPLL DRMETIEISG YTKNEKLAIA KDHLVPCILE DHGLDAEKLK IEDEALKVII
DKYTREAGVR GLKKQLAKTA RFVSEKIVSG KADLPYVVRA DMLKEILGKE IIRQEEARKE
NVPGVVTGLA WTPVGGDILF IEGTFMPGSG KLTLTGQLGD VMKESAKISL SLVRSRLANT
ANSFDFTSSD IHIHVPSGAT PKDGPSAGVT LFTALTSLII GKAVDPKLAM TGEITLSGAV
LPVGGIKEKV LAAHRAGIKK IILPKENERD LEDVPEDARN ELQFVPVETI EEVLREALDI
DLPRPVVPSS YPGSSYAPAH SV
