ID   PSB2_THEGJ              Reviewed;         200 AA.
AC   C5A2D5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Proteasome subunit beta 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_02113};
DE   AltName: Full=Proteasome core protein PsmB 2 {ECO:0000255|HAMAP-Rule:MF_02113};
DE   Flags: Precursor;
GN   Name=psmB2 {ECO:0000255|HAMAP-Rule:MF_02113}; Synonyms=psmB-2;
GN   OrderedLocusNames=TGAM_2052;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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}.
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DR   EMBL; CP001398; ACS34554.1; -; Genomic_DNA.
DR   RefSeq; WP_015859657.1; NC_012804.1.
DR   AlphaFoldDB; C5A2D5; -.
DR   SMR; C5A2D5; -.
DR   STRING; 593117.TGAM_2052; -.
DR   MEROPS; T01.002; -.
DR   PaxDb; C5A2D5; -.
DR   EnsemblBacteria; ACS34554; ACS34554; TGAM_2052.
DR   GeneID; 7988618; -.
DR   KEGG; tga:TGAM_2052; -.
DR   PATRIC; fig|593117.10.peg.2063; -.
DR   eggNOG; arCOG00970; Archaea.
DR   HOGENOM; CLU_035750_7_2_2; -.
DR   OMA; NLGMAMQ; -.
DR   OrthoDB; 89767at2157; -.
DR   Proteomes; UP000001488; 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..7
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT                   /id="PRO_0000397464"
FT   CHAIN           8..200
FT                   /note="Proteasome subunit beta 2"
FT                   /id="PRO_0000397465"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   200 AA;  22020 MW;  A76808E0F6C7513B CRC64;
     MEEKKTGTTT VGIKVKEGVV LAADTQASLG NMVETLNIRK ILPITDRIAI TTAGSVGDVQ
     ALARMLEAQA RYYQFTWGRP MTTRAMANLL SNILNENKWF PYMVQIIIGG YVDKPELASV
     DALGGLVFEK YTATGSGSPF AIAIIEDGYR EDMSIEEAKE LAVRAVKTAG KRDVYTGERK
     VQVVVITKDG MKEEFVEFKE