ID   PSB_STRCO               Reviewed;         281 AA.
AC   Q7AKQ5; O87598;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=SCO1644; ORFNames=SCI41.27;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 54-61, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, ACTIVITY REGULATION,
RP   AND TEMPERATURE DEPENDENCE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=9765579; DOI=10.1128/jb.180.20.5448-5453.1998;
RA   Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R.;
RT   "The 20S proteasome of Streptomyces coelicolor.";
RL   J. Bacteriol. 180:5448-5453(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation. The
CC       S.coelicolor proteasome is able to cleave oligopeptides after
CC       hydrophobic residues, but not after basic or acidic residues, thus
CC       displaying chymotrypsin-like activity but not trypsin-like activity.
CC       {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:9765579}.
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         ECO:0000269|PubMed:9765579};
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 (By similarity). Peptidolytic activity
CC       is completely inhibited by lactacystin, and to a lesser extent, by N-
CC       acetyl-Leu-Leu-norleucinal (Ac-LLnL) and benzoyloxycarbonyl-Leu-Leu-
CC       Leu-vinylsulfone (Z-LLL-VS) in vitro. {ECO:0000255|HAMAP-Rule:MF_02113,
CC       ECO:0000269|PubMed:9765579}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:9765579};
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 probably a gated structure,
CC       the ends of the cylinder being occluded by the N-termini of the alpha-
CC       subunits. Is likely capped by the proteasome-associated ATPase, ARC.
CC       {ECO:0000269|PubMed:9765579}.
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; AF086832; AAC64284.1; -; Genomic_DNA.
DR   EMBL; AL939109; CAB59497.1; -; Genomic_DNA.
DR   RefSeq; NP_625919.1; NC_003888.3.
DR   RefSeq; WP_003977182.1; NZ_VNID01000018.1.
DR   AlphaFoldDB; Q7AKQ5; -.
DR   SMR; Q7AKQ5; -.
DR   STRING; 100226.gene:17759237; -.
DR   MEROPS; T01.005; -.
DR   PaxDb; 100226-SCO1644; -.
DR   PATRIC; fig|100226.15.peg.1659; -.
DR   eggNOG; COG0638; Bacteria.
DR   HOGENOM; CLU_035750_2_0_11; -.
DR   InParanoid; Q7AKQ5; -.
DR   OrthoDB; 5174038at2; -.
DR   PhylomeDB; Q7AKQ5; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
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; IPR000243; Pept_T1A_subB.
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   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Protease; Proteasome; 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                   ECO:0000269|PubMed:9765579"
FT                   /id="PRO_0000383489"
FT   CHAIN           54..281
FT                   /note="Proteasome subunit beta"
FT                   /id="PRO_5000055072"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   281 AA;  30086 MW;  860B58A2B45CD8F8 CRC64;
     MEANTRSTGR LPAAFLTPGS SSFMDFLGEH QPEMLPGNRQ LPPVQGVIEA PHGTTIVAVT
     FPGGVVLAGD RRATMGNMIA QRDIEKVFPA DEYSAVGIAG TAGLAVEMVK LFQLELEHFE
     KVEGAQLSLE GKANRLSTMI RSNLGMAMQG LAVVPLFAGY DVDRGRGRIF SYDVTGGRSE
     ERHFATTGSG SVFARGAMKK LFRDDLTEEQ ATTLVVQALY DAADDDSATG GPDVARRIYP
     IITVITEDGF RRLGEDEAAE LAGSVLQARL EQPDGPRAAL L
//