PSB_THEVO
ID PSB_THEVO Reviewed; 211 AA.
AC Q97AZ7; C5J9S1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
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 PsmB {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=psmB {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=TV0662;
GN ORFNames=TVG0656650;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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 PAN-20S
CC proteasome complex, via the docking of the C-termini of PAN into the
CC intersubunit pockets in the alpha-rings, triggers opening of the gate
CC for substrate entry. Interconversion between the open-gate and close-
CC gate conformations leads to a dynamic regulation of the 20S proteasome
CC proteolysis activity. {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 at one or both ends by the proteasome regulatory ATPase, PAN.
CC {ECO:0000255|HAMAP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000011; BAB59804.1; -; Genomic_DNA.
DR EMBL; FN397805; CAZ48528.1; -; Genomic_DNA.
DR RefSeq; WP_010916921.1; NC_002689.2.
DR AlphaFoldDB; Q97AZ7; -.
DR SMR; Q97AZ7; -.
DR STRING; 273116.14324878; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; BAB59804; BAB59804; BAB59804.
DR GeneID; 1441769; -.
DR KEGG; tvo:TVG0656650; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 89767at2157; -.
DR PhylomeDB; Q97AZ7; -.
DR Proteomes; UP000001017; 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:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03764; proteasome_beta_archeal; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_02113_A; Proteasome_B_A; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR019983; Pept_T1A_Psome_bsu_arc.
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 TIGRFAMs; TIGR03634; arc_protsome_B; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 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..8
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000397480"
FT CHAIN 9..211
FT /note="Proteasome subunit beta"
FT /id="PRO_0000397481"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 211 AA; 23087 MW; CA9487BE7B5776B4 CRC64;
MNQTLETGTT TVGITLTDAV IMATERRVTM ENFIMHKNGK KLFQIDTYTG MTIAGLVGDA
QVLVRYMKAE LELYRLQRRV NMPIEAVATL LSNMLNQVKY MPYMVQLLVG GIDTSPHVFS
IDAAGGSVED IYASTGSGSP FVYGVLESQY NEKLSIDEGV DLVIRAISAA KQRDSASGGM
IDVAVITKKD GYVQLPTEQI EARIKKLGLI L
