ID PSB2_SULTO Reviewed; 207 AA. AC Q975D1; DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Proteasome subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_02113}; DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113}; DE AltName: Full=20S proteasome beta subunit 2 {ECO:0000255|HAMAP-Rule:MF_02113}; DE AltName: Full=Proteasome core protein PsmB 2 {ECO:0000255|HAMAP-Rule:MF_02113}; DE Flags: Precursor; GN Name=psmB2 {ECO:0000255|HAMAP-Rule:MF_02113}; GN OrderedLocusNames=STK_04770; OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) OS (Sulfolobus tokodaii). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfurisphaera. OX NCBI_TaxID=273063; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7; RX PubMed=11572479; DOI=10.1093/dnares/8.4.123; RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T., RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.; RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, RT Sulfolobus tokodaii strain7."; RL DNA Res. 8:123-140(2001). CC -!- FUNCTION: Component of the proteasome core, a large protease complex CC with broad specificity involved in protein degradation. CC {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|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; BA000023; BAB65470.1; -; Genomic_DNA. DR RefSeq; WP_010978453.1; NC_003106.2. DR AlphaFoldDB; Q975D1; -. DR SMR; Q975D1; -. DR STRING; 273063.STK_04770; -. DR MEROPS; T01.002; -. DR GeneID; 1458419; -. DR KEGG; sto:STK_04770; -. DR PATRIC; fig|273063.9.peg.551; -. DR eggNOG; arCOG00970; Archaea. DR OrthoDB; 6330at2157; -. DR Proteomes; UP000001015; 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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 NCBIfam; TIGR03634; arc_protsome_B; 1. DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Proteasome; KW Reference proteome; Threonine protease; Zymogen. FT PROPEP 1..13 FT /note="Removed in mature form; by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113" FT /id="PRO_0000397460" FT CHAIN 14..207 FT /note="Proteasome subunit beta 2" FT /id="PRO_0000397461" FT ACT_SITE 14 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113" SQ SEQUENCE 207 AA; 23041 MW; 44137E4A7D05A2D1 CRC64; METNNKLKIL KTGTTTVGIK VKDGVVLAAD RRASAGMYVA HKYVRKVLYV APNIGITTAG SVADLQFIYD LLKNIYHYNL ITGMRPITIK ALATYLANML SFSKYLPYIV QILIGGVDEQ PRLYNLDYVG DITEEDYTAT GSGSVEAIGV IEDEYRPDMT LDEAADLARR AIFSSIKRDP YTGTGVIVSK ITKNGHEEKE YYPQRKI //