ID A0A1C8ZQM8_9CREN Unreviewed; 205 AA. AC A0A1C8ZQM8; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 25-APR-2018, entry version 9. 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. 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 RT comparative analyses of central carbon, nitrogen and sulfur metabolism RT in various Sulfolobus strains."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the proteasome core, a large protease CC complex with broad specificity involved in protein degradation. CC {ECO:0000256|HAMAP-Rule:MF_02113, ECO:0000256|SAAS:SAAS00636001}. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000256|HAMAP-Rule:MF_02113, CC ECO:0000256|SAAS:SAAS00636007}. CC -!- ENZYME REGULATION: The formation of the proteasomal ATPase PAN-20S CC proteasome complex, via the docking of the C-termini of PAN into CC the intersubunit pockets in the alpha-rings, triggers opening of CC the gate for substrate entry. Interconversion between the open- CC gate and close-gate conformations leads to a dynamic regulation of CC the 20S proteasome proteolysis activity. {ECO:0000256|HAMAP- CC Rule:MF_02113}. CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 CC beta subunits that assemble into four stacked heptameric rings, CC resulting in a barrel-shaped structure. The two inner rings, each CC composed of seven catalytic beta subunits, are sandwiched by two CC outer rings, each composed of seven alpha subunits. The catalytic CC chamber with the active sites is on the inside of the barrel. Has CC a gated structure, the ends of the cylinder being occluded by the CC N-termini of the alpha-subunits. Is capped at one or both ends by CC the proteasome regulatory ATPase, PAN. {ECO:0000256|HAMAP- CC Rule:MF_02113, ECO:0000256|SAAS:SAAS00635999}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113, CC ECO:0000256|SAAS:SAAS00636005}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000256|HAMAP-Rule:MF_02113, ECO:0000256|SAAS:SAAS00636006}. 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 EnsemblBacteria; AOL15729; AOL15729; BFU36_02165. DR GeneID; 28694626; -. DR KEGG; sula:BFU36_02165; -. DR KO; K03433; -. 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 PANTHER; PTHR11599:SF108; PTHR11599:SF108; 1. 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|HAMAP-Rule:MF_02113}; KW Complete proteome {ECO:0000313|Proteomes:UP000094286}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000256|SAAS:SAAS00636002}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000256|SAAS:SAAS00636003}; KW Protease {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000256|SAAS:SAAS00636010}; KW Proteasome {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000256|SAAS:SAAS00636004, ECO:0000313|EMBL:AOL15729.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000094286}; KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000256|SAAS:SAAS00636009}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_02113}. FT PROPEP 1 12 Removed in mature form; by autocatalysis. FT {ECO:0000256|HAMAP-Rule:MF_02113}. FT /FTId=PRO_5009005850. FT ACT_SITE 13 13 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_02113}. 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 //