PSB_META3
ID PSB_META3 Reviewed; 217 AA.
AC A6UT20;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Maeo_0050;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000743; ABR55642.1; -; Genomic_DNA.
DR RefSeq; WP_011972774.1; NC_009635.1.
DR AlphaFoldDB; A6UT20; -.
DR SMR; A6UT20; -.
DR STRING; 419665.Maeo_0050; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; ABR55642; ABR55642; Maeo_0050.
DR GeneID; 5327362; -.
DR KEGG; mae:Maeo_0050; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 89767at2157; -.
DR Proteomes; UP000001106; 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 Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..14
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000397344"
FT CHAIN 15..217
FT /note="Proteasome subunit beta"
FT /id="PRO_0000397345"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 217 AA; 23479 MW; CE9AA04E4373E758 CRC64;
MIANNDQYKE YMKGTTTVGI VCNDGIVLAT DKRATMGNLI ADKEAKKLYK IDDYMAMTIA
GSVGDAQSLV RIISAEANLY KLRTGNNIPP HSCAMLLSNV LHGSRHFPFL IQLIIGGYDT
IHGAKLFSLD AVGGLNEETS FTATGSGSPT AFGVLEEEYK KDMTINKGKL LAIKSLTAAM
KRDAFSGNGI SLAVIDKNGV KIYSDEEIEE LSNILYK