ID A0A378YXL6_9NOCA Unreviewed; 275 AA.
AC A0A378YXL6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=prcB2_1 {ECO:0000313|EMBL:SUA81181.1};
GN Synonyms=prcB {ECO:0000256|HAMAP-Rule:MF_02113};
GN ORFNames=NCTC1934_04648 {ECO:0000313|EMBL:SUA81181.1};
OS Nocardia otitidiscaviarum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1823 {ECO:0000313|EMBL:SUA81181.1, ECO:0000313|Proteomes:UP000255467};
RN [1] {ECO:0000313|EMBL:SUA81181.1, ECO:0000313|Proteomes:UP000255467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC1934 {ECO:0000313|EMBL:SUA81181.1,
RC ECO:0000313|Proteomes:UP000255467};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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: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}.
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DR EMBL; UGRY01000002; SUA81181.1; -; Genomic_DNA.
DR RefSeq; WP_039814845.1; NZ_UGRY01000002.1.
DR AlphaFoldDB; A0A378YXL6; -.
DR STRING; 1406858.GCA_000710895_06719; -.
DR OrthoDB; 5174038at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000255467; 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; 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 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02113};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113};
KW Proteasome {ECO:0000256|HAMAP-Rule:MF_02113, ECO:0000313|EMBL:SUA81181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255467};
KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113};
KW Zymogen {ECO:0000256|HAMAP-Rule:MF_02113}.
FT PROPEP 1..48
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5017095554"
FT CHAIN 49..275
FT /note="Proteasome subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5023557634"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
SQ SEQUENCE 275 AA; 29098 MW; 140C15FC67205853 CRC64;
MTAADSLPLD TGYNRSSFSD YLRRHAPELL PGNGFGGEPL GREIAVHGTT IVAVSFHGGV
LIAGDRRGTM GNLLATRDME KVFITDTYSA AGFAGTVGVA LEMIRLFAVE LEHYEKIEGV
ALTFDGKATK LSKMVRDNLP AALQDLAVVP VLVGYDPSIV DPDRAGRIVS YDVAGGRSEE
RFGYAAVGSG SVFAKSSLKK TYSAGLDEER ALRIAVEALF DAADDDTATG GPDVVRGIYP
TSVVVDAEGA REIPDDRLMG IARDLVDERV VANGG
//
