ID A0A1C8ZQM8_9CREN Unreviewed; 205 AA. AC A0A1C8ZQM8; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 19-JAN-2022, entry version 23. DE RecName: Full=Proteasome subunit beta {ECO:0000256|HAMAP-Rule:MF_02113}; DE EC=3.4.25.1 {ECO:0000256|HAMAP-Rule:MF_02113}; DE AltName: Full=20S proteasome beta subunit {ECO:0000256|HAMAP-Rule:MF_02113}; DE AltName: Full=Proteasome core protein PsmB {ECO:0000256|HAMAP-Rule:MF_02113}; GN Name=psmB {ECO:0000256|HAMAP-Rule:MF_02113}; GN ORFNames=BFU36_02165 {ECO:0000313|EMBL:AOL15729.1}; OS Sulfolobus sp. A20. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus; unclassified Sulfolobus. OX NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL15729.1, ECO:0000313|Proteomes:UP000094286}; RN [1] {ECO:0000313|Proteomes:UP000094286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A20 {ECO:0000313|Proteomes:UP000094286}; RA Dai X.; RT "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative RT analyses of central carbon, nitrogen and sulfur metabolism in various RT Sulfolobus strains."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the proteasome core, a large protease complex CC with broad specificity involved in protein degradation. CC {ECO:0000256|HAMAP-Rule:MF_02113}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of peptide bonds with very broad specificity.; CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198, CC ECO:0000256|HAMAP-Rule:MF_02113}; CC -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S CC proteasome complex, via the docking of the C-termini of PAN into the CC intersubunit pockets in the alpha-rings, triggers opening of the gate CC for substrate entry. Interconversion between the open-gate and close- CC gate conformations leads to a dynamic regulation of the 20S proteasome CC proteolysis activity. {ECO:0000256|HAMAP-Rule:MF_02113}. CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta CC subunits that assemble into four stacked heptameric rings, resulting in CC a barrel-shaped structure. The two inner rings, each composed of seven CC catalytic beta subunits, are sandwiched by two outer rings, each CC composed of seven alpha subunits. The catalytic chamber with the active CC sites is on the inside of the barrel. Has a gated structure, the ends CC of the cylinder being occluded by the N-termini of the alpha-subunits. CC Is capped at one or both ends by the proteasome regulatory ATPase, PAN. CC {ECO:0000256|HAMAP-Rule:MF_02113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000256|HAMAP- CC Rule:MF_02113}. 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; CP017006; AOL15729.1; -; Genomic_DNA. DR RefSeq; WP_069281892.1; NZ_CP017006.1. DR STRING; 1891280.BFU36_02165; -. DR EnsemblBacteria; AOL15729; AOL15729; BFU36_02165. DR GeneID; 28694626; -. DR KEGG; sula:BFU36_02165; -. DR OrthoDB; 89767at2157; -. DR Proteomes; UP000094286; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:UniProtKB-UniRule. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_02113_A; Proteasome_B_A; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR019983; Pept_T1A_Psome_bsu_arc. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03634; arc_protsome_B; 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_02113}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02113}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02113}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113}; KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP- KW Rule:MF_02113}; Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}. FT PROPEP 1..12 FT /note="Removed in mature form; by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5009005850" FT CHAIN 13..205 FT /note="Proteasome subunit beta" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5023273787" FT ACT_SITE 13 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113, FT ECO:0000256|PIRSR:PIRSR600243-1" SQ SEQUENCE 205 AA; 22719 MW; EFAB03763009CDC1 CRC64; MFLEIKNKIL KGTTTVGIRV KDGVVLAADR RASAGFFVAN KMVRKVLYIT DKIGITTAGS VADLQFIYDV LKNIYHYNSI TRYGPVSVKG IATRLANILS ATKYFPYLVQ ILIGGYDDQP RLYNLDYLGD ITEEQYVATG SGSPVAMGVL EDEYDESMSL DKAVDLAKRA VFSAIKRDSF TGTGVIVTKI NSVGHEEYEF YLKKI //