PSB1_THEKO
ID PSB1_THEKO Reviewed; 203 AA.
AC Q5JDJ9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Proteasome subunit beta 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PsmB 1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=psmB1 {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=TK1429;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85618.1; -; Genomic_DNA.
DR RefSeq; WP_011250380.1; NC_006624.1.
DR AlphaFoldDB; Q5JDJ9; -.
DR SMR; Q5JDJ9; -.
DR STRING; 69014.TK1429; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; BAD85618; BAD85618; TK1429.
DR GeneID; 3234476; -.
DR KEGG; tko:TK1429; -.
DR PATRIC; fig|69014.16.peg.1390; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR InParanoid; Q5JDJ9; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 89767at2157; -.
DR PhylomeDB; Q5JDJ9; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
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 Reference proteome; 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_0000397414"
FT CHAIN 8..203
FT /note="Proteasome subunit beta 1"
FT /id="PRO_0000397415"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 203 AA; 21927 MW; 4090DB8EEDE29654 CRC64;
MTEKLKGTTT VGIVCKDGVV LAADRRASLG NMVLSERVTK VFQIDDHLAI AGAGTVGDIL
SLVRLLRAEA KLYRAKVSRE MSVKALATLT SNILHSGRGF AYMAWFLVGG YDSAPRLYSI
DAAGGVTEDR FTAAGSGMEF AFSVLEENYR DGIPLEEGVK LALRAIKAAT KRDVFTGGGV
TLVTITEEGY REWSEEELKS LLE
