PSB_RHOE4
ID PSB_RHOE4 Reviewed; 292 AA.
AC C0ZZU7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Proteasome subunit beta {ECO:0000255|HAMAP-Rule:MF_02113};
DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=20S proteasome beta subunit {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PrcB {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=prcB {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=RER_31740;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation.
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02113}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_02113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC Rule:MF_02113}.
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DR EMBL; AP008957; BAH33882.1; -; Genomic_DNA.
DR RefSeq; WP_019748515.1; NC_012490.1.
DR AlphaFoldDB; C0ZZU7; -.
DR SMR; C0ZZU7; -.
DR STRING; 234621.RER_31740; -.
DR MEROPS; T01.005; -.
DR EnsemblBacteria; BAH33882; BAH33882; RER_31740.
DR GeneID; 57486888; -.
DR KEGG; rer:RER_31740; -.
DR eggNOG; COG0638; Bacteria.
DR HOGENOM; CLU_035750_2_0_11; -.
DR OMA; NLGMAMQ; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000002204; Chromosome.
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 Gene3D; 3.60.20.10; -; 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 Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03690; 20S_bact_beta; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Proteasome;
KW Threonine protease; Zymogen.
FT PROPEP 1..59
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000397564"
FT CHAIN 60..292
FT /note="Proteasome subunit beta"
FT /id="PRO_0000397565"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 292 AA; 30398 MW; 759E364233C73FBE CRC64;
MTVDRAPRIT DGDTRLSFGS NLSSFSEYLR VHAPEHLPQN RFADTGGVVM GGGDVAPHGT
TIVAISYAGG VLLAGDRRAT MGNLIASRDV QKVYVTDDYS AAGIAGTAGI AIELVRLFAV
ELEHYEKIEG VPLTFDGKAN RLSSMVRGNL GAAMQGLAVV PLLVGYDLDA VDPSRAGRIV
SYDVVGGRYE ERAGYHAVGS GSLFAKSALK KLYSPGIDED TALRFAVEAL YDAADDDSAT
GGPDLTRGIY PTAVTITSAG AVELSTAKAA EIAREIVAAR TATASPEGES AL