PSB_SACVD
ID PSB_SACVD Reviewed; 289 AA.
AC C7MWV7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=Svir_22030;
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharomonospora.
OX NCBI_TaxID=471857;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101;
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU97211.1; -; Genomic_DNA.
DR RefSeq; WP_015786524.1; NC_013159.1.
DR AlphaFoldDB; C7MWV7; -.
DR SMR; C7MWV7; -.
DR STRING; 471857.Svir_22030; -.
DR EnsemblBacteria; ACU97211; ACU97211; Svir_22030.
DR KEGG; svi:Svir_22030; -.
DR eggNOG; COG0638; Bacteria.
DR HOGENOM; CLU_035750_2_0_11; -.
DR OMA; NLGMAMQ; -.
DR OrthoDB; 1129370at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000000841; 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 Reference proteome; 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_0000397570"
FT CHAIN 60..289
FT /note="Proteasome subunit beta"
FT /id="PRO_0000397571"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 289 AA; 30377 MW; 7FBB4759A24BE9E1 CRC64;
MEHTPRNAGF ALPAAYMSTM TSSFIDFLKA EAPDLLPRAR VENMPAVPGG GSAFEPPHGT
TIVASTFNGG VLIAGDRRAT TGNTIASRDL EKVYVTDAYS AVGIAGTAGI ALELVRLYTV
ELAHYEKIEG VSLSLDGKAN KLANMVKGNL DGALAGLAVL PLFVGYDIDA DDPKRAGRIV
SFDVTGGRYE ENAGYHAIGS GAVYAKSSLK KLYDPEADAD TAVRTAIEAL YDAADDDTAT
GGPDLVRRIY PTVVTITAEH GAVMLPQEET ASIAESVVRE RSERPGQLG
