ID A0A927BNU2_STRGL Unreviewed; 281 AA. AC A0A927BNU2; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 24-JAN-2024, entry version 5. 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=prcB {ECO:0000256|HAMAP-Rule:MF_02113, GN ECO:0000313|EMBL:MBD2830051.1}; GN ORFNames=ID875_22960 {ECO:0000313|EMBL:MBD2830051.1}; OS Streptomyces globisporus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1908 {ECO:0000313|EMBL:MBD2830051.1, ECO:0000313|Proteomes:UP000616788}; RN [1] {ECO:0000313|EMBL:MBD2830051.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=QF2 {ECO:0000313|EMBL:MBD2830051.1}; RA Montano E.T., Nideffer J.F., Brumage L., Erb M., Derman A.I., Davis J.P., RA Estrada E., Fu S., Le D., Vuppala A., Tran C., Luterstein E., Lakkaraju S., RA Panchagnula S., Ren C., Doan J., Tran S., Soriano J., Fujita Y., Gutala P., RA Fujii Q., Lee M., Bui A., Villarreal C., Shing S.R., Kim S., Freeman D., RA Racha V., Ho A., Kumar P., Falah K., Dawson T., Enustun E., Prichard A., RA Gomez A., Khanna K., Trigg S., Fernandez L., Pogliano K., Pogliano J.; RT "Isolation and characterization of Streptomyces bacteriophages and RT Streptomyces strains encoding biosynthetic arsenals: Streptomyces strains RT and phages for antibiotic discovery."; RL PLoS ONE 0:0-0(2020). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBD2830051.1}. 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; JACWUS010000007; MBD2830051.1; -; Genomic_DNA. DR Proteomes; UP000616788; Unassembled WGS sequence. 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; IPR000243; Pept_T1A_subB. 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 PRINTS; PR00141; PROTEASOME. 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|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|HAMAP-Rule:MF_02113, ECO:0000313|EMBL:MBD2830051.1}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113}; KW Proteasome {ECO:0000256|HAMAP-Rule:MF_02113, KW ECO:0000313|EMBL:MBD2830051.1}; KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}. FT PROPEP 1..53 FT /note="Removed in mature form; by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5038196042" FT CHAIN 54..281 FT /note="Proteasome subunit beta" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113" FT /id="PRO_5038196041" FT ACT_SITE 54 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113, FT ECO:0000256|PIRSR:PIRSR600243-1" SQ SEQUENCE 281 AA; 30174 MW; BA6463C8407C28D7 CRC64; MEANTRSTGR LPAAFLTPGS SSFMDFLSDH SPEMLPGKRS LPPLQGAVEA PHGTTIVAAS FPGGVVLAGD RRATMGNMIA QRDIEKVFPA DEYSAVGIAG TAGLAVEMVK LFQLELEHFE KVEGAQLSLE GKANRLSTMI RSNLAMAMQG LAVVPLFAGY DVDRDKGRIF SYDVTGGRSE ENGYAATGSG SIFARGSMKK LYREDLTEQQ ALTLVVQALY DAADDDSATG GPDVARRIYP IVTVITDEGF RRLTDQESSE IARAVLERRL EEPDGPRAAL L //