ID A0A256IIE5_9EURY Unreviewed; 243 AA.
AC A0A256IIE5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=DJ70_09680 {ECO:0000313|EMBL:OYR56299.1};
OS Halorubrum halodurans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1383851 {ECO:0000313|EMBL:OYR56299.1, ECO:0000313|Proteomes:UP000216308};
RN [1] {ECO:0000313|EMBL:OYR56299.1, ECO:0000313|Proteomes:UP000216308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cb34 {ECO:0000313|EMBL:OYR56299.1,
RC ECO:0000313|Proteomes:UP000216308};
RX PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA Ventosa A., Gogarten J.P., Papke R.T.;
RT "Population and genomic analysis of the genus Halorubrum.";
RL Front. Microbiol. 5:140-140(2014).
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 -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000256|HAMAP-
CC 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:OYR56299.1}.
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DR EMBL; NHPJ01000092; OYR56299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256IIE5; -.
DR OrthoDB; 6330at2157; -.
DR Proteomes; UP000216308; 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; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR NCBIfam; TIGR03634; arc_protsome_B; 1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000216308};
KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}.
FT PROPEP 1..49
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5011800566"
FT CHAIN 50..243
FT /note="Proteasome subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT /id="PRO_5023255436"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02113,
FT ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 243 AA; 25692 MW; F3853F502441583D CRC64;
MRTPTDDLSD GASLELGRDQ PVFGPELGEF EHSERRAAQA DGEGEMKTGT TTVGIRTADG
VVMATDMRAS LGGMVSSKDV QKVEEVHPRG ALTIAGSVSA AQNLISTLKA ETNLYEARRG
KDMSMEALST LTGNLLRTGA FFIVQPILGG VDDEGAHIYS IDALGGTTEE EYTVTGSGSQ
YALGVLEQEY HDDVTVEEAK GIAAKAIQSA VERDLASGNG INVAVVTDEG VEITRHKDFD
DLL
//
