ID A0A7G2D850_9EURY Unreviewed; 634 AA. AC A0A7G2D850; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 27-NOV-2024, entry version 16. DE RecName: Full=Archaeal Lon protease {ECO:0000256|ARBA:ARBA00022016}; GN Name=lon {ECO:0000313|EMBL:CAD5244066.1}; GN ORFNames=TIRI35C_0912 {ECO:0000313|EMBL:CAD5244066.1}; OS Thermococcus camini. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=2016373 {ECO:0000313|EMBL:CAD5244066.1, ECO:0000313|Proteomes:UP000516304}; RN [1] {ECO:0000313|EMBL:CAD5244066.1, ECO:0000313|Proteomes:UP000516304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IRI35c {ECO:0000313|EMBL:CAD5244066.1, RC ECO:0000313|Proteomes:UP000516304}; RA Courtine D.; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|ARBA:ARBA00026070}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB CC subfamily. {ECO:0000256|ARBA:ARBA00009579}. 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; LR881183; CAD5244066.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7G2D850; -. DR KEGG; tcq:TIRI35C_0912; -. DR Proteomes; UP000516304; Chromosome TIRI35C. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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:InterPro. 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. DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01122}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 130..148 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 144..334 FT /note="Sigma-54 factor interaction" FT /evidence="ECO:0000259|PROSITE:PS50045" FT DOMAIN 436..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 634 AA; 69941 MW; 1458CF3ED657BCCB CRC64; MGDKEKIEEA LAPREYGESL ELGVDFSTTE EIKVPEKLID QVIGQEHAVE VIRTAANQKR HVLLIGEPGT GKSMLGQAMA ELLPTENLED ILVFPNSEDE NMPRIKTVPA CQGRRIVEKY REKAKGQESI KSYILLFVMF TVMLALFIDF SATTLLMGLF VVILTIMALS NMRLRNTVLV PKLLVDNCGR TKAPFIDATG AHAGALLGDV RHDPFQSGGL GTPAHERVEP GMIHRAHKGV LFIDEIATLS LKMQQSLLTA MQEKRFPITG QSEMSSGAMV RTEPVPCDFV LVAAGNLDTV DKMHPALRSR IRGYGYEVYM RTTMPDTLEN RKKLVQFVAQ EVIRDGKIPH FTREAVEEIV REAQKRAGRK GHLTLRLRDL GGIVRAAGDI AIKKGRKYVE REDVIEAIRM AKPLEKQLAD WYIERKKEYQ VIKAEGKGIG RVNGLAVIGE QSGIVLPIEA VVAPAASKEE GKIIVTGKLG EIAKEAVQNV SAIIKRYKGE DISKYDIHVQ FLQTYEGVEG DSASISVATA VISALEEIPI RQDVAMTGSL SVLGEVLPIG GATPKIEAAI EAGIKTVIIP KANEKDVFLS RDKAEKIQIF PVETIDQVLE IALVDNEKKE ELLRRIREAL PLSL //