ID   PSA_STRSW               Reviewed;         248 AA.
AC   C9Z4D1;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PrcA {ECO:0000255|HAMAP-Rule:MF_00289};
GN   Name=prcA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=SCAB_73481;
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=680198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22;
RX   PubMed=20064060; DOI=10.1094/mpmi-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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_00289}.
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_00289}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_00289}.
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_00289}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00289}.
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DR   EMBL; FN554889; CBG74333.1; -; Genomic_DNA.
DR   RefSeq; WP_013004873.1; NC_013929.1.
DR   AlphaFoldDB; C9Z4D1; -.
DR   SMR; C9Z4D1; -.
DR   STRING; 680198.SCAB_73481; -.
DR   EnsemblBacteria; CBG74333; CBG74333; SCAB_73481.
DR   GeneID; 24308973; -.
DR   KEGG; scb:SCAB_73481; -.
DR   eggNOG; COG0638; Bacteria.
DR   HOGENOM; CLU_071031_0_0_11; -.
DR   OMA; QIYRLPH; -.
DR   OrthoDB; 1243753at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00289_B; Proteasome_A_B; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR022296; Proteasome_asu_bac.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF69; PTHR11599:SF69; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03691; 20S_bact_alpha; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Proteasome; Reference proteome.
FT   CHAIN           1..248
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_0000397178"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   248 AA;  27436 MW;  518CF77A8D13B63A CRC64;
     MSTPFYVSPQ QAMADRAEYA RKGIARGRSL VVLQYADGIV FVGENPSRAL HKFSEIYDRI
     GFAAAGKYNE YENLRIGGVR YADLRGYTYD RDDVTARGLA NVYAQTLGTI FSSAAEKPYE
     VELVVAEVGE TPEGDQIYRL PHDGSIVDEH GSVAVGGNAE QISSYLDQRH QDGMSLAEAL
     KLAVQALSRD TNGTQREIPA ERLEVAVLDR TRPQQRKFKR IVGRQLDRLL EADGATTEAE
     SSAEEEDE