PSB2_SACS9
ID PSB2_SACS9 Reviewed; 211 AA.
AC D0KTH0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 52.
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}; OrderedLocusNames=Ssol_1825;
OS Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=555311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98/2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Mead D.;
RT "Complete sequence of Sulfolobus solfataricus 98/2.";
RL Submitted (OCT-2009) 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: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 -!- SEQUENCE CAUTION:
CC Sequence=ACX92039.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001800; ACX92039.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_029552577.1; NZ_ACUK01000205.1.
DR AlphaFoldDB; D0KTH0; -.
DR SMR; D0KTH0; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; ACX92039; ACX92039; Ssol_1825.
DR GeneID; 44129771; -.
DR KEGG; sol:Ssol_1825; -.
DR HOGENOM; CLU_035750_7_2_2; -.
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..17
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000397458"
FT CHAIN 18..211
FT /note="Proteasome subunit beta 2"
FT /id="PRO_0000397459"
FT ACT_SITE 18
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 211 AA; 23271 MW; 2CD506CE3E096B10 CRC64;
MVIMGNELQL ENKILKGTTT VGIRVNDGVI LAADRRASAG FFVANKMVRK VLYITDKIGI
TTAGSVADLQ FIYDVLKNIY HYNSITKYGP ISIKGIATRL ANVLSATKYF PYIVQILIGG
YDDQPRLFNL DYLGDITEEN YVATGSGSPV AMGVLEDEYN PKMTLDEAAD LAKRAVFSAI
KRDSFTGTGV IVAKIHSKGH EELEFYLNKK M