ID D1Z2L6_METPS Unreviewed; 636 AA.
AC D1Z2L6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=lon {ECO:0000313|EMBL:BAI62938.1};
GN OrderedLocusNames=MCP_2866 {ECO:0000313|EMBL:BAI62938.1};
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI62938.1, ECO:0000313|Proteomes:UP000001882};
RN [1] {ECO:0000313|Proteomes:UP000001882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC {ECO:0000313|Proteomes:UP000001882};
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT paludicola, the first cultivated representative of the order
RT Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
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}.
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DR EMBL; AP011532; BAI62938.1; -; Genomic_DNA.
DR AlphaFoldDB; D1Z2L6; -.
DR STRING; 304371.MCP_2866; -.
DR MEROPS; S16.005; -.
DR KEGG; mpd:MCP_2866; -.
DR PATRIC; fig|304371.9.peg.2935; -.
DR eggNOG; arCOG02160; Archaea.
DR InParanoid; D1Z2L6; -.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000001882; 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 CDD; cd00009; AAA; 1.
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; 2.
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:SF46; 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};
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 123..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT TRANSMEM 147..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 428..607
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 636 AA; 69515 MW; 9025A8920D9DFD08 CRC64;
MSEEVKIEKQ DDLCGGLEFN STSDIEVPTK LIDQVIGQEH AVEVIKKAAN QRRHVMMIGT
PGTGKSMLAK AMAELLPKEE LQDVLIYHNP EDGNNPKVRV VPAGKGKQIV NAHKMEAQKS
SQMRNLIIVF AMLGILVFAF VYLREQFMWA IIAVLLLLLL LRYVTPKETV ITPKLLVTNQ
GKTTAPFIDA TGAHAGALLG DVRHDPFQSG GLETPAHDRV EAGAIHKAHK GVLFIDEINT
LRMESQQHLL TALQEKKFHI TGQSERSSGA MVKTDPVPCD FIMVLAGNLD AKEGMHPALR
SRIKGYGYEL YMTDSMEDNP ENRRKLVRFV AQEVMRDGKI PHFDHSAVDE IIREARRRAG
RKGHLTLKLR DLGGLVRVSG DIARSEGAAL TTADHVLKAK KISRSVEQQL ADTYLDQRRD
YRLFKAAGEE VGRVNGLAVI GGDSGIVLPI VAEVTPALSK AEGHVYATGK LKSIAKESVQ
NVSAIIKKFT GYDISSMDVH IQFVGAYEGV EGDSASVSIA TAVISALSQI PIDQTVAMTG
SLSVRGEVLP IGGVTYKIEA AALAGIKTVL IPKSNVGDVL IEEVYKDKVK IIPVTNISEV
LEYALVGKMK ESFLDKIRNF SMDKMGIGIF DKALPH
//
