ID A0A1Q9TUU5_9ACTN Unreviewed; 280 AA.
AC A0A1Q9TUU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=BJF83_12610 {ECO:0000313|EMBL:OLT29265.1};
OS Nocardiopsis sp. CNR-923.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1904965 {ECO:0000313|EMBL:OLT29265.1, ECO:0000313|Proteomes:UP000185703};
RN [1] {ECO:0000313|EMBL:OLT29265.1, ECO:0000313|Proteomes:UP000185703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNR-923 {ECO:0000313|EMBL:OLT29265.1,
RC ECO:0000313|Proteomes:UP000185703};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT29265.1}.
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DR EMBL; MKKC01000064; OLT29265.1; -; Genomic_DNA.
DR RefSeq; WP_075925514.1; NZ_MKKC01000064.1.
DR AlphaFoldDB; A0A1Q9TUU5; -.
DR STRING; 1904965.BJF83_12610; -.
DR OrthoDB; 5174038at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000185703; 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|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:OLT29265.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185703};
KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}.
FT PROPEP 1..52
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5010391574"
FT CHAIN 53..280
FT /note="Proteasome subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5023506361"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113,
FT ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 280 AA; 30014 MW; 9A3D695B0606FAFB CRC64;
MFEGFEGGRL PAAFMSAGTS SFTEFVRSVS PELLPGHHLP SGEGAEHLTP DATTIVALTF
PGGVVMAGDR RATQGNVIAN RDMEKLFRTD EFSAVAFAGS AGIGIELARL FQVELEHYEK
MEGRVLSLEG KANKLAQMVR GNLGMAMQGF VVVPLLVGYD ETADVGRVFS YDAVGGRYEE
HRYHSIGSGS VYARGSVKKL YRDDLDETGA VRVALESLYD AADDDSATGG PDLHRKIFPL
VDVITEAGHR RVPTDDVARL ATEVVQGRAA HPDGPTATLS
//
