PSB_THEAC
ID PSB_THEAC Reviewed; 211 AA.
AC P28061;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 150.
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=Ta0612;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1734972; DOI=10.1021/bi00119a004;
RA Zwickl P., Grziwa A., Puehler G., Dahlmann B., Lottspeich F.,
RA Baumeister W.;
RT "Primary structure of the Thermoplasma proteasome and its implications for
RT the structure, function, and evolution of the multicatalytic proteinase.";
RL Biochemistry 31:964-972(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, AND KINETIC
RP PARAMETERS.
RX PubMed=8999862; DOI=10.1074/jbc.272.3.1791;
RA Akopian T.N., Kisselev A.F., Goldberg A.L.;
RT "Processive degradation of proteins and other catalytic properties of the
RT proteasome from Thermoplasma acidophilum.";
RL J. Biol. Chem. 272:1791-1798(1997).
RN [4]
RP SUBUNIT.
RX PubMed=1373380; DOI=10.1002/j.1460-2075.1992.tb05206.x;
RA Puehler G., Weinkauf S., Bachmann L., Mueller S., Engel E., Hegerl R.,
RA Baumeister W.;
RT "Subunit stoichiometry and three-dimensional arrangement in proteasomes
RT from Thermoplasma acidophilum.";
RL EMBO J. 11:1607-1616(1992).
RN [5]
RP ACTIVE SITE, CATALYTIC MECHANISM, AND MUTAGENESIS OF THR-9.
RX PubMed=7725107; DOI=10.1126/science.7725107;
RA Seemuller E., Lupas A., Stock D., Lowe J., Huber R., Baumeister W.;
RT "Proteasome from Thermoplasma acidophilum: a threonine protease.";
RL Science 268:579-582(1995).
RN [6]
RP AUTOCATALYTIC PROCESSING.
RX PubMed=8684489; DOI=10.1038/382468a0;
RA Seemuller E., Lupas A., Baumeister W.;
RT "Autocatalytic processing of the 20S proteasome.";
RL Nature 382:468-471(1996).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9442034; DOI=10.1074/jbc.273.4.1982;
RA Kisselev A.F., Akopian T.N., Goldberg A.L.;
RT "Range of sizes of peptide products generated during degradation of
RT different proteins by archaeal proteasomes.";
RL J. Biol. Chem. 273:1982-1989(1998).
RN [8]
RP INTERACTION WITH PAN, SUBUNIT, AND GATED STRUCTURE.
RX PubMed=16337593; DOI=10.1016/j.molcel.2005.10.019;
RA Smith D.M., Kafri G., Cheng Y., Ng D., Walz T., Goldberg A.L.;
RT "ATP binding to PAN or the 26S ATPases causes association with the 20S
RT proteasome, gate opening, and translocation of unfolded proteins.";
RL Mol. Cell 20:687-698(2005).
RN [9]
RP GATE OPENING MECHANISM, AND ACTIVITY REGULATION.
RX PubMed=17803938; DOI=10.1016/j.molcel.2007.06.033;
RA Smith D.M., Chang S.C., Park S., Finley D., Cheng Y., Goldberg A.L.;
RT "Docking of the proteasomal ATPases' carboxyl termini in the 20S
RT proteasome's alpha ring opens the gate for substrate entry.";
RL Mol. Cell 27:731-744(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT, AND
RP SUBUNIT.
RX PubMed=7725097; DOI=10.1126/science.7725097;
RA Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R.;
RT "Crystal structure of the 20S proteasome from the archaeon T. acidophilum
RT at 3.4-A resolution.";
RL Science 268:533-539(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND
RP T.BRUCEI PA26.
RX PubMed=15916965; DOI=10.1016/j.molcel.2005.04.016;
RA Forster A., Masters E.I., Whitby F.G., Robinson H., Hill C.P.;
RT "The 1.9 A structure of a proteasome-11S activator complex and implications
RT for proteasome-PAN/PA700 interactions.";
RL Mol. Cell 18:589-599(2005).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.8 ANGSTROMS) OF THE OPEN-GATE AND
RP CLOSED-GATE CONFORMATIONS, AND GATE OPENING MECHANISM.
RX PubMed=18471981; DOI=10.1016/j.molcel.2008.03.004;
RA Rabl J., Smith D.M., Yu Y., Chang S.C., Goldberg A.L., Cheng Y.;
RT "Mechanism of gate opening in the 20S proteasome by the proteasomal
RT ATPases.";
RL Mol. Cell 30:360-368(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH THE ALPHA SUBUNIT AND
RP THE C-TERMINUS OF PAN FROM M.JANNASCHII.
RX PubMed=20019667; DOI=10.1038/emboj.2009.382;
RA Yu Y., Smith D.M., Kim H.M., Rodriguez V., Goldberg A.L., Cheng Y.;
RT "Interactions of PAN's C-termini with archaeal 20S proteasome and
RT implications for the eukaryotic proteasome-ATPase interactions.";
RL EMBO J. 29:692-702(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND
RP CHIMERIC PA26 CONSTRUCTS.
RX PubMed=19889631; DOI=10.1074/jbc.c109.070425;
RA Stadtmueller B.M., Ferrell K., Whitby F.G., Heroux A., Robinson H.,
RA Myszka D.G., Hill C.P.;
RT "Structural models for interactions between the 20S proteasome and its
RT PAN/19S activators.";
RL J. Biol. Chem. 285:13-17(2010).
RN [15]
RP ACTIVITY REGULATION.
RX PubMed=20360109; DOI=10.1126/science.1184991;
RA Religa T.L., Sprangers R., Kay L.E.;
RT "Dynamic regulation of archaeal proteasome gate opening as studied by TROSY
RT NMR.";
RL Science 328:98-102(2010).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The
CC T.acidophilum proteasome is able to cleave oligopeptides after Tyr,
CC Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays
CC chymotrypsin-like activity and low level of caspase-like and trypsin-
CC like activities. {ECO:0000255|HAMAP-Rule:MF_02113,
CC ECO:0000269|PubMed:8999862}.
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 ECO:0000269|PubMed:8999862};
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 ECO:0000269|PubMed:17803938, ECO:0000269|PubMed:20360109}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for Suc-LLVY-Amc (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:8999862};
CC Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55
CC degrees Celsius) {ECO:0000269|PubMed:8999862};
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, ECO:0000269|PubMed:1373380,
CC ECO:0000269|PubMed:15916965, ECO:0000269|PubMed:16337593,
CC ECO:0000269|PubMed:19889631, ECO:0000269|PubMed:20019667,
CC ECO:0000269|PubMed:7725097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC -!- MISCELLANEOUS: The configuration of the closed gate contains an opening
CC large enough to allow rapid entry of tetrapeptides but able to impede
CC the entry of proteins and longer peptides.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC Rule:MF_02113}.
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DR EMBL; M83674; AAA72102.1; -; Genomic_DNA.
DR EMBL; AL445064; CAC11751.1; -; Genomic_DNA.
DR PIR; A42068; A42068.
DR RefSeq; WP_010901036.1; NC_002578.1.
DR PDB; 1PMA; X-ray; 3.40 A; 1/2/B/P/Q/R/S/T/U/V/W/X/Y/Z=1-211.
DR PDB; 1YA7; X-ray; 2.30 A; H/I/J/K/L/M/N=1-211.
DR PDB; 1YAR; X-ray; 1.90 A; H/I/J/K/L/M/N=1-211.
DR PDB; 1YAU; X-ray; 2.40 A; H/I/J/K/L/M/N=1-211.
DR PDB; 3C91; EM; 6.80 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDB; 3C92; EM; 6.80 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDB; 3IPM; X-ray; 4.00 A; H/I/J/K/L/M/N=1-211.
DR PDB; 3J9I; EM; 3.30 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDB; 3JRM; X-ray; 2.90 A; H/I/J/K/L/M/N=9-211.
DR PDB; 3JSE; X-ray; 2.90 A; H/I/J/K/L/M/N=9-211.
DR PDB; 3JTL; X-ray; 3.20 A; H/I/J/K/L/M/N=9-211.
DR PDB; 5VY3; EM; 3.10 A; 1/B/D/F/H/J/L/N/P/R/T/V/X/Z=9-211.
DR PDB; 5VY4; EM; 3.30 A; 1/B/D/F/H/J/L/N/P/R/T/V/X/Z=9-211.
DR PDB; 6BDF; EM; 2.80 A; 1/B/D/F/H/J/L/N/P/R/T/V/X/Z=1-211.
DR PDB; 6UTF; EM; 3.40 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=1-211.
DR PDB; 6UTG; EM; 3.40 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDB; 6UTH; EM; 3.40 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDB; 6UTI; EM; 3.40 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=9-211.
DR PDB; 6UTJ; EM; 2.90 A; 1/2/H/I/J/K/L/M/N/V/W/X/Y/Z=9-211.
DR PDBsum; 1PMA; -.
DR PDBsum; 1YA7; -.
DR PDBsum; 1YAR; -.
DR PDBsum; 1YAU; -.
DR PDBsum; 3C91; -.
DR PDBsum; 3C92; -.
DR PDBsum; 3IPM; -.
DR PDBsum; 3J9I; -.
DR PDBsum; 3JRM; -.
DR PDBsum; 3JSE; -.
DR PDBsum; 3JTL; -.
DR PDBsum; 5VY3; -.
DR PDBsum; 5VY4; -.
DR PDBsum; 6BDF; -.
DR PDBsum; 6UTF; -.
DR PDBsum; 6UTG; -.
DR PDBsum; 6UTH; -.
DR PDBsum; 6UTI; -.
DR PDBsum; 6UTJ; -.
DR AlphaFoldDB; P28061; -.
DR BMRB; P28061; -.
DR SMR; P28061; -.
DR STRING; 273075.Ta0612; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; CAC11751; CAC11751; CAC11751.
DR GeneID; 1456195; -.
DR KEGG; tac:Ta0612; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 89767at2157; -.
DR BRENDA; 3.4.25.1; 6324.
DR EvolutionaryTrace; P28061; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Protease; Proteasome; Reference proteome; Threonine protease;
KW Zymogen.
FT PROPEP 1..8
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113,
FT ECO:0000269|PubMed:8999862"
FT /id="PRO_0000026675"
FT CHAIN 9..211
FT /note="Proteasome subunit beta"
FT /id="PRO_0000026676"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113,
FT ECO:0000269|PubMed:7725107"
FT MUTAGEN 9
FT /note="T->S: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:7725107"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1YAR"
FT HELIX 57..78
FT /evidence="ECO:0007829|PDB:1YAR"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:1YAR"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 105..121
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6UTI"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:1YAR"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1YAR"
FT HELIX 156..173
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3J9I"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1YAR"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1YAR"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1YAR"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:1YAR"
SQ SEQUENCE 211 AA; 23147 MW; F81B9360641873DD CRC64;
MNQTLETGTT TVGITLKDAV IMATERRVTM ENFIMHKNGK KLFQIDTYTG MTIAGLVGDA
QVLVRYMKAE LELYRLQRRV NMPIEAVATL LSNMLNQVKY MPYMVQLLVG GIDTAPHVFS
IDAAGGSVED IYASTGSGSP FVYGVLESQY SEKMTVDEGV DLVIRAISAA KQRDSASGGM
IDVAVITRKD GYVQLPTDQI ESRIRKLGLI L
