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Database: UniProt
Entry: I7J752_METBM
LinkDB: I7J752_METBM
Original site: I7J752_METBM 
ID   I7J752_METBM            Unreviewed;       646 AA.
AC   I7J752;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Archaeal Lon protease {ECO:0000256|ARBA:ARBA00022016, ECO:0000256|RuleBase:RU369001};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU369001};
DE   AltName: Full=ATP-dependent protease La homolog {ECO:0000256|RuleBase:RU369001};
GN   Name=lon3 {ECO:0000313|EMBL:CCJ35078.1};
GN   OrderedLocusNames=BN140_0155 {ECO:0000313|EMBL:CCJ35078.1};
OS   Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS   (Methanogenium bourgense).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ35078.1, ECO:0000313|Proteomes:UP000009007};
RN   [1] {ECO:0000313|Proteomes:UP000009007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC   {ECO:0000313|Proteomes:UP000009007};
RX   PubMed=22965103; DOI=10.1128/JB.01292-12;
RA   Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA   Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT   "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT   Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT   digester.";
RL   J. Bacteriol. 194:5487-5488(2012).
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. Degrades polypeptides processively.
CC       {ECO:0000256|RuleBase:RU369001}.
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000256|ARBA:ARBA00026070, ECO:0000256|RuleBase:RU369001}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|RuleBase:RU369001}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU369001}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009579,
CC       ECO:0000256|RuleBase:RU369001}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369001}.
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DR   EMBL; HE964772; CCJ35078.1; -; Genomic_DNA.
DR   RefSeq; WP_014866055.1; NC_018227.2.
DR   AlphaFoldDB; I7J752; -.
DR   STRING; 1201294.BN140_0155; -.
DR   MEROPS; S16.A11; -.
DR   GeneID; 13355243; -.
DR   KEGG; mbg:BN140_0155; -.
DR   PATRIC; fig|1201294.9.peg.171; -.
DR   HOGENOM; CLU_392630_0_0_2; -.
DR   OMA; GLYFWNL; -.
DR   BioCyc; MBOU1201294:BN140_RS00775-MONOMER; -.
DR   Proteomes; UP000009007; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004663; Lon_arc.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR002078; Sigma_54_int.
DR   NCBIfam; TIGR00764; lon_rel; 1.
DR   PANTHER; PTHR10046:SF66; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU369001};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU369001};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01122};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369001};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU369001};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000009007};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01122};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369001};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369001}.
FT   TRANSMEM        138..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369001"
FT   DOMAIN          437..615
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        522
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   646 AA;  70558 MW;  3ECC42393EDD77B1 CRC64;
     MDSTTSKEIP NIELTNDELA EIDDFAGLEL SASSDIDVPP NLIDQVIGQE HAVEVIRKAA
     VQRRHVMMIG SPGTGKSMLA KAMAELLPKE ELQDILVYPN SEDNNNPIIR TVPAGRGKQI
     VSAHKMEARK KIQMRSTLIM LLIVGIVVYA ILASQWLMGI IAAAFVFMAL KYSTPREETM
     VPKLLVSHDP NTPAPFVDAT GSHAGALLGD VRHDPFQSGG LETPSHDRVE SGAIHRAHGG
     VLFIDEINTL TPHSQQNLLT ALQEGNFPIT GQSERSSGAM VRTEPVPCRF VMIAAGNLDA
     IQGMHPALRS RIRGYGYEVY MRETMEDTQE NRRKFIRFIA QEVKNDGKIP HFDRDAMLEI
     LREARRRSNR KGHLTLKLRD MGGLIRVAGD LARQEGADFT TAKHVIAAKK TARSIEDQIS
     DEYIRRSRDY DITVVEGTRV GRVNGLAVMG NDSGSVLPVM AEVTPSQGAN GTVIATGMLK
     DIAKESITNV SALIKKFTGK DIRNIDIHIQ FIGTYGGVEG DSASVTVATA VISAIEDIPV
     RQDVAMTGSL SVRGDVLPIG GVTYKIEAAA KAGIKKVIIP RSNLDDVLIE DRYRAMVEVV
     PVDHIEEVLQ NALVPENREG FFAKLRKMAV NPTTGMFDST VGRSVI
//
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