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   03-AUG-2022, entry version 92.
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}.
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DR   EMBL; D78172; BAA21650.1; -; mRNA.
DR   PIR; T09132; T09132.
DR   AlphaFoldDB; O24361; -.
DR   SMR; O24361; -.
DR   MEROPS; T01.A10; -.
DR   OrthoDB; 929961at2759; -.
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   Gene3D; 3.60.20.10; -; 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   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Threonine protease;
KW   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"
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