ID B0L7G5_9ACTO Unreviewed; 278 AA. AC B0L7G5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 09-JAN-2013, entry version 24. DE RecName: Full=Proteasome subunit beta; DE EC=3.4.25.1; DE AltName: Full=20S proteasome beta subunit; DE AltName: Full=Proteasome core protein PrcB; GN Name=salI; Synonyms=prcB; OS Salinispora tropica. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=168695; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNB-476; RX PubMed=19590008; DOI=10.1073/pnas.0901237106; RA Eustaquio A.S., McGlinchey R.P., Liu Y., Hazzard C., Beer L.L., RA Florova G., Alhamadsheh M.M., Lechner A., Kale A.J., Kobayashi Y., RA Reynolds K.A., 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 CC complex with broad specificity involved in protein degradation (By CC similarity). CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. CC -!- ENZYME REGULATION: The formation of the proteasomal ATPase ARC-20S CC proteasome complex, likely via the docking of the C-termini of ARC CC into the intersubunit pockets in the alpha-rings, may trigger CC opening of the gate for substrate entry. Interconversion between CC the open-gate and close-gate conformations leads to a dynamic CC regulation of the 20S proteasome proteolysis activity (By CC similarity). CC -!- PATHWAY: Protein degradation; proteasomal pup-dependent pathway. 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 by the proteasome- CC associated ATPase, ARC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the peptidase T1B family. 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 ProteinModelPortal; B0L7G5; -. DR SMR; B0L7G5; 45-266. 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:HAMAP. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:HAMAP. DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:HAMAP. DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:HAMAP. DR HAMAP; MF_02113_B; Proteasome_B_B; 1; -. DR InterPro; IPR022483; Pept_T1A_Psome_suB_actinobac. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR11599:SF2; PTHR11599:SF2; 1. DR Pfam; PF00227; Proteasome; 1. DR TIGRFAMs; TIGR03690; 20S_bact_beta; 1. DR PROSITE; PS51476; PROTEASOME_B_2; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Proteasome; KW Threonine protease; Zymogen. FT PROPEP 1 44 Removed in mature form; by autocatalysis FT (By similarity). FT ACT_SITE 45 45 Nucleophile (By similarity). 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 //