ID H8I956_METCZ Unreviewed; 636 AA.
AC H8I956;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:AFC99059.1};
GN OrderedLocusNames=Mtc_0288 {ECO:0000313|EMBL:AFC99059.1};
OS Methanocella conradii (strain DSM 24694 / JCM 17849 / CGMCC 1.5162 /
OS HZ254).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=1041930 {ECO:0000313|EMBL:AFC99059.1, ECO:0000313|Proteomes:UP000005233};
RN [1] {ECO:0000313|EMBL:AFC99059.1, ECO:0000313|Proteomes:UP000005233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24694 / JCM 17849 / CGMCC 1.5162 / HZ254
RC {ECO:0000313|Proteomes:UP000005233};
RX PubMed=22493204; DOI=10.1128/JB.00207-12;
RA Lu Z., Lu Y.;
RT "Complete genome sequence of a thermophilic methanogen, Methanocella
RT conradii HZ254, isolated from Chinese rice field soil.";
RL J. Bacteriol. 194:2398-2399(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}.
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DR EMBL; CP003243; AFC99059.1; -; Genomic_DNA.
DR AlphaFoldDB; H8I956; -.
DR STRING; 1041930.Mtc_0288; -.
DR MEROPS; S16.005; -.
DR KEGG; mez:Mtc_0288; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000005233; 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; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000005233};
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; 69637 MW; 1A761A78E332C5DC CRC64;
MSEEVKMEKQ DDLCGGLEFS STSEIEVPTK LIDQVIGQEH AVEVIKKAAN QRRHVMMIGT
PGTGKSMLAK AMAELLPKEE LQDVLIYHNP EDPNNPKVRV VPAGKGKQIV NAHKAEAQKN
SQLRNLIIVC SMLGILVFAF VYMNSQFMWA VIAVLLLLLL LRYVTPKETV ITPKLLVSNQ
GRTTAPFIDA TGAHAGALLG DVRHDPFQSG GLETPAHERV EAGAIHKAHK GVLFIDEINT
LRMESQQHLL TALQEKKFHI TGQSERSSGA MVKTDPVPCD FIMVLAGNLD AKEGMHPALR
SRIKGYGYEL YMQDTMEDTP ENRRKLVRFV AQEVLRDGKI PHFDRSAVEE IIREARRRAG
RKGHLTLKLR DLGGLVRVSG DIARAEGAQL TTAEHVLKAK KISRSVEQQL ADTYLDRRKD
YRLFKVTGEE VGRVNGLAVI GGDSGIVLPI VAEVTPAISK SEGHVYATGK LKSIAKESVQ
NVSAIIKKYT GYDIASMDVH IQFVGAYEGV EGDSASVSIA TAVISALSQI PVDQSVAMTG
SLSVRGEVLP IGGVTYKIEA AALAGIQTVL IPKSNMGDVL IEEYYKDKVR IVPVSNISEV
LEYALVGKMK ESFLDKIRNF SVDKMGIGIF DKALPH
//
