ID B0L7G5_9ACTN Unreviewed; 278 AA. AC B0L7G5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 13-SEP-2023, entry version 59. 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 PrcB {ECO:0000256|HAMAP-Rule:MF_02113}; GN Name=salI {ECO:0000313|EMBL:ABP73653.1}; GN Synonyms=prcB {ECO:0000256|HAMAP-Rule:MF_02113}; OS Salinispora tropica. OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Salinispora. OX NCBI_TaxID=168695 {ECO:0000313|EMBL:ABP73653.1}; RN [1] {ECO:0000313|EMBL:ABP73653.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNB-476 {ECO:0000313|EMBL:ABP73653.1}; RX PubMed=19590008; DOI=10.1073/pnas.0901237106; RA Eustaquio A.S., McGlinchey R.P., Liu Y., Hazzard C., Beer L.L., Florova G., RA Alhamadsheh M.M., Lechner A., Kale A.J., Kobayashi Y., Reynolds K.A., RA Moore B.S.; RT "Biosynthesis of the salinosporamide A polyketide synthase substrate RT chloroethylmalonyl-coenzyme A from S-adenosyl-L-methionine."; RL Proc. Natl. Acad. Sci. U.S.A. 106:12295-12300(2009). 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 ARC-20S CC proteasome complex, likely via the docking of the C-termini of ARC into CC the intersubunit pockets in the alpha-rings, may trigger opening of the CC gate for substrate entry. Interconversion between the open-gate and CC close-gate conformations leads to a dynamic regulation of the 20S CC proteasome proteolysis activity. {ECO:0000256|HAMAP-Rule:MF_02113}. CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. CC {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 by the proteasome-associated ATPase, ARC. {ECO:0000256|HAMAP- CC Rule:MF_02113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113}. 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; EF397502; ABP73653.1; -; Genomic_DNA. DR AlphaFoldDB; B0L7G5; -. DR SMR; B0L7G5; -. DR MEROPS; T01.005; -. DR UniPathway; UPA00997; -. 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:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01906; proteasome_protease_HslV; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR HAMAP; MF_02113_B; Proteasome_B_B; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR InterPro; IPR022483; PSB_actinobac. DR NCBIfam; TIGR03690; 20S_bact_beta; 1. DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR Pfam; PF00227; Proteasome; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_02113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02113}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113}; KW Proteasome {ECO:0000256|HAMAP-Rule:MF_02113}; KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_02113}. FT PROPEP 1..44 FT /note="Removed in mature form; by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5005033303" FT CHAIN 45..278 FT /note="Proteasome subunit beta" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5023458959" FT ACT_SITE 45 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" SQ SEQUENCE 278 AA; 29432 MW; 6ABF307076BF563F CRC64; MNRGLPSTFL TFHSSSFVEL LKEYDPTLLP AKRAAETFGE APHGTTIVAA TFAGGVLLAG DRRTTMGNLI AGRDVDKLTI TDDYSAVGFA GTVGISIDMT RLFVVELEHY EKIEGVPLSL EGKSNRLAAI VKGNLPMANA GMVSIPLFIG YDLEASDPAR AGRIVSFDAI GARYEEKSGY QSIGSGSPFA KSSLKKLHDP GSDDAATLSA LIEALYDAAD DDSATGGPDM VRRIFPTAIR ITAEGAYRYT EEELAAVADA VVARRSADEP GVRSFTAS //