ID PSB5_SPIOL Reviewed; 272 AA. AC O24361; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Proteasome subunit beta type-5; DE EC=3.4.25.1; DE AltName: Full=20S proteasome subunit E; DE AltName: Full=Proteasome epsilon chain; DE Flags: Precursor; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9207846; DOI=10.1023/a:1005839501822; RA Ito N., Tomizawa K., Tanaka K., Matsui M., Kendrick R.E., Sato T., RA Nakagawa H.; RT "Characterization of 26S proteasome alpha- and beta-type and ATPase RT subunits from spinach and their expression during early stages of seedling RT development."; RL Plant Mol. Biol. 34:307-316(1997). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr, CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic CC pH. The proteasome has an ATP-dependent proteolytic activity. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of peptide bonds with very broad specificity.; CC EC=3.4.25.1; CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits. The 20S proteasome core is composed of 28 CC subunits that are arranged in four stacked rings, resulting in a CC barrel-shaped structure. The two end rings are each formed by seven CC alpha subunits, and the two central rings are each formed by seven beta CC subunits. The catalytic chamber with the active sites is on the inside CC of the barrel. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. CC Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. 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; D78172; BAA21650.1; -; mRNA. DR PIR; T09132; T09132. DR PDB; 7QVE; EM; 3.30 A; e/s=1-272. DR PDBsum; 7QVE; -. DR AlphaFoldDB; O24361; -. DR EMDB; EMD-14175; -. DR SMR; O24361; -. DR MEROPS; T01.A10; -. DR OrthoDB; 4492251at2759; -. DR Proteomes; UP001155700; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro. DR CDD; cd03761; proteasome_beta_type_5; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. 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; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; KW Reference proteome; Threonine protease; Zymogen. FT PROPEP 1..55 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000026607" FT CHAIN 56..272 FT /note="Proteasome subunit beta type-5" FT /id="PRO_0000026608" FT ACT_SITE 56 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 104..125 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 131..144 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 153..160 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 163..170 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 204..221 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 227..234 FT /evidence="ECO:0007829|PDB:7QVE" FT STRAND 239..246 FT /evidence="ECO:0007829|PDB:7QVE" FT HELIX 247..254 FT /evidence="ECO:0007829|PDB:7QVE" SQ SEQUENCE 272 AA; 29620 MW; 4D800127F7CEFC3A CRC64; MKLDTSGLES TAPIFRRSDF VFDGLQMTPS FDLPNPTDFD GFQKEAVQMV KPAKGTTTLA FIFKHGVMVA ADSRASMGGY ISSQSVKKII EINPYMLGTM AGGAADCQFW HRNLGIKCRL HELANKRRIS VTGASKLLAN ILYNYRGMGL SVGTMIAGWD ETGPGLYYVD SEGGRLKGMR FSVGSGSPYA YGVLDNGYKY DMTVEEASEL ARRAIYHATY RDGASGGVVS VYHVGPDGWK KVTGDDVGDL HFQYYPVVPA TVEQEMVEVV GA //