PSB_ARCFU
ID PSB_ARCFU Reviewed; 213 AA.
AC Q9P996; O29769;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
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=AF_0481;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 12-213 IN COMPLEX WITH ALPHA
RP SUBUNIT AND CALPAIN-INHIBITOR I, AND SUBUNIT.
RX PubMed=12614609; DOI=10.1016/s0022-2836(03)00080-9;
RA Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R.;
RT "Investigations on the maturation and regulation of archaebacterial
RT proteasomes.";
RL J. Mol. Biol. 327:75-83(2003).
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 probably a gated structure,
CC the ends of the cylinder being occluded by the N-termini of the alpha-
CC subunits. Is likely capped at one or both ends by the proteasome
CC regulatory ATPase, PAN. {ECO:0000269|PubMed:12614609}.
CC -!- INTERACTION:
CC Q9P996; O29760: psmA; NbExp=2; IntAct=EBI-1035761, EBI-1035754;
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; AE000782; AAB90757.1; -; Genomic_DNA.
DR PIR; A69310; A69310.
DR PDB; 1J2Q; X-ray; 2.83 A; H/I/J/K/L/M/N=12-213.
DR PDB; 6HE5; EM; 4.12 A; 1/2/3/4/5/6/7=11-213.
DR PDB; 6HE7; EM; 3.69 A; 1/2/3/4/5/6/7=12-213.
DR PDB; 6HE8; EM; 6.86 A; 1/2/3/4/5/6/7/h/i/j/k/l/m/n=12-213.
DR PDB; 6HE9; EM; 6.35 A; 1/2/3/4/5/6/7/h/i/j/k/l/m/n=12-213.
DR PDB; 6HEA; EM; 7.04 A; 1/2/3/4/5/6/7/h/i/j/k/l/m/n=12-213.
DR PDB; 6HEC; EM; 6.95 A; 1/2/3/4/5/6/7/h/i/j/k/l/m/n=12-213.
DR PDB; 6HED; EM; 6.95 A; 1/2/3/4/5/6/7/h/i/j/k/l/m/n=12-213.
DR PDBsum; 1J2Q; -.
DR PDBsum; 6HE5; -.
DR PDBsum; 6HE7; -.
DR PDBsum; 6HE8; -.
DR PDBsum; 6HE9; -.
DR PDBsum; 6HEA; -.
DR PDBsum; 6HEC; -.
DR PDBsum; 6HED; -.
DR AlphaFoldDB; Q9P996; -.
DR SMR; Q9P996; -.
DR IntAct; Q9P996; 2.
DR STRING; 224325.AF_0481; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; AAB90757; AAB90757; AF_0481.
DR KEGG; afu:AF_0481; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR OMA; VDKTGPH; -.
DR PhylomeDB; Q9P996; -.
DR EvolutionaryTrace; Q9P996; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..11
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000026659"
FT CHAIN 12..213
FT /note="Proteasome subunit beta"
FT /id="PRO_0000026660"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 60..81
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:1J2Q"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:1J2Q"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1J2Q"
SQ SEQUENCE 213 AA; 23418 MW; DA03E480A88F8227 CRC64;
MSMIEEKIYK GTTTVGLVCK DGVVMATEKR ATMGNFIASK AAKKIYQIAD RMAMTTAGSV
GDAQFLARII KIEANLYEIR RERKPTVRAI ATLTSNLLNS YRYFPYLVQL LIGGIDSEGK
SIYSIDPIGG AIEEKDIVAT GSGSLTAYGV LEDRFTPEIG VDEAVELAVR AIYSAMKRDS
ASGDGIDVVK ITEDEFYQYS PEEVEQILAK FRK
