ID A0A1Q7M6T6_9CREN Unreviewed; 201 AA.
AC A0A1Q7M6T6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|HAMAP-Rule:MF_02113};
DE EC=3.4.25.1 {ECO:0000256|HAMAP-Rule:MF_02113};
DE AltName: Full=20S proteasome beta subunit {ECO:0000256|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PsmB {ECO:0000256|HAMAP-Rule:MF_02113};
GN Name=psmB {ECO:0000256|HAMAP-Rule:MF_02113};
GN ORFNames=AUI95_03335 {ECO:0000313|EMBL:OLD08369.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_4.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805097 {ECO:0000313|EMBL:OLD08369.1, ECO:0000313|Proteomes:UP000186346};
RN [1] {ECO:0000313|EMBL:OLD08369.1, ECO:0000313|Proteomes:UP000186346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001198,
CC ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02113}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000256|HAMAP-
CC Rule:MF_02113}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02113}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLD08369.1}.
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DR EMBL; MNGM01000048; OLD08369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7M6T6; -.
DR Proteomes; UP000186346; Unassembled WGS sequence.
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 Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_02113};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02113};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02113};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_02113}; Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}.
FT PROPEP 1..9
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5010389659"
FT CHAIN 10..201
FT /note="Proteasome subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5023269908"
SQ SEQUENCE 201 AA; 21497 MW; 1CFFC1F5456CDDD9 CRC64;
MSDEGFMPGA TTVGLVCKDG AILASERRYS YGTFVMSKVA KKVFKVTDNI GIGCAGIIGD
MQVLAREANA YMSIYRYERG RPGTVKNTAK LFASILSSRR LYPYLAQTII AGVDDGVPEL
FVLDPIGSVL GDKFAAVGTG AEIAMGVLES EYRDGLSVEE ARPLILRAIK SAVARDISSG
DGVDLLMITH SGIKEESQKF A
//
