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Database: UniProt
Entry: A0A1G7RCG8_9ACTN
LinkDB: A0A1G7RCG8_9ACTN
Original site: A0A1G7RCG8_9ACTN 
ID   A0A1G7RCG8_9ACTN        Unreviewed;       285 AA.
AC   A0A1G7RCG8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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 PrcB {ECO:0000256|HAMAP-Rule:MF_02113};
GN   Name=prcB {ECO:0000256|HAMAP-Rule:MF_02113};
GN   ORFNames=SAMN05660662_0263 {ECO:0000313|EMBL:SDG08468.1};
OS   Blastococcus aurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDG08468.1, ECO:0000313|Proteomes:UP000199406};
RN   [1] {ECO:0000313|EMBL:SDG08468.1, ECO:0000313|Proteomes:UP000199406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44268 {ECO:0000313|EMBL:SDG08468.1,
RC   ECO:0000313|Proteomes:UP000199406};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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: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|HAMAP-Rule:MF_02113};
CC   -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S
CC       proteasome complex, likely via the docking of the C-termini of ARC into
CC       the intersubunit pockets in the alpha-rings, may trigger opening of the
CC       gate for substrate entry. Interconversion between the open-gate and
CC       close-gate conformations leads to a dynamic regulation of the 20S
CC       proteasome proteolysis activity. {ECO:0000256|HAMAP-Rule:MF_02113}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {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 by the proteasome-associated ATPase, ARC. {ECO:0000256|HAMAP-
CC       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}.
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DR   EMBL; FNBT01000011; SDG08468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7RCG8; -.
DR   STRING; 1550231.SAMN05660662_0263; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000199406; 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:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01906; proteasome_protease_HslV; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_02113_B; Proteasome_B_B; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   InterPro; IPR022483; PSB_actinobac.
DR   NCBIfam; TIGR03690; 20S_bact_beta; 1.
DR   PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   Pfam; PF00227; Proteasome; 1.
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|HAMAP-Rule:MF_02113};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_02113};
KW   Proteasome {ECO:0000256|HAMAP-Rule:MF_02113, ECO:0000313|EMBL:SDG08468.1};
KW   Threonine protease {ECO:0000256|HAMAP-Rule:MF_02113};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_02113}.
FT   PROPEP          1..53
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT                   /id="PRO_5011804049"
FT   CHAIN           54..285
FT                   /note="Proteasome subunit beta"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
FT                   /id="PRO_5023542645"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   285 AA;  30046 MW;  2CD58C1817CA276B CRC64;
     MNESSAGRSG FPPAYLDRVG SSFTDFLSTT APDLLPGRRP VPTMPVGDLA PHGTTIVAVT
     YEGGVLMGGD RRATMGNLIS SRDIEKVYPA DSYSVIGIAG AAGIAIEMVK LYQVELEHYE
     KIEGLTMSLD GKANRLAQMI RGNLGAAMQG LAVVPLFAGF DLDAAEGTAP GRIFSYDVTG
     GNYEERGYAA VGSGSLFAKN SLKKTWRTGL PADAATRTVV EALYDAADDD SATGGPDPVR
     KLYPIVYRVD AEGAVRLTDA EVAAVADTIV TERAEADRQN MDRGA
//
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