ID   PSB_GEOOG               Reviewed;         280 AA.
AC   D2S6E2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
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 PrcB {ECO:0000255|HAMAP-Rule:MF_02113};
DE   Flags: Precursor;
GN   Name=prcB {ECO:0000255|HAMAP-Rule:MF_02113};
GN   OrderedLocusNames=Gobs_2682;
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=526225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) 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 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:0000255|HAMAP-Rule:MF_02113}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {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 by the proteasome-associated ATPase, ARC. {ECO:0000255|HAMAP-
CC       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; CP001867; ADB75316.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2S6E2; -.
DR   SMR; D2S6E2; -.
DR   STRING; 526225.Gobs_2682; -.
DR   MEROPS; T01.005; -.
DR   KEGG; gob:Gobs_2682; -.
DR   eggNOG; COG0638; Bacteria.
DR   HOGENOM; CLU_035750_2_0_11; -.
DR   OrthoDB; 5174038at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001382; 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: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; Cytoplasm; Hydrolase; Protease; Proteasome;
KW   Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..53
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT                   /id="PRO_0000397510"
FT   CHAIN           54..280
FT                   /note="Proteasome subunit beta"
FT                   /id="PRO_0000397511"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   280 AA;  29436 MW;  D3F1DEB8112F9BE3 CRC64;
     MSEYSAGRSG FSPAYLDRVG SSFTDFLAAA APHLLPGSRP VPQIPVGNVT PHGTTIVSVT
     YDGGVLMGGD RRATMGNLIS SREIEKVYPA DAWSVIGIAG AAGIAIEMVR LYQVELEHYE
     KIEGLTLSLD GKANRLAQMI RGNLGAALQG LAVVPLFAGF DLDAAPGAAP GRIFSYDVTG
     GNYEERGYSA VGSGSLFARN SLKKTWRPNL DGDAATRSLV EALYDAADDD SATGGPDPVR
     RLYPIVYRVD AEGAVRVPDD EIAAVATRIT DERSAADGQG
//