ID   PSA_MYCA1               Reviewed;         256 AA.
AC   A0QFB6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=MAV_2405;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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_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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000479; ABK69021.1; -; Genomic_DNA.
DR   RefSeq; WP_003878079.1; NC_008595.1.
DR   AlphaFoldDB; A0QFB6; -.
DR   SMR; A0QFB6; -.
DR   MEROPS; T01.980; -.
DR   EnsemblBacteria; ABK69021; ABK69021; MAV_2405.
DR   GeneID; 66693868; -.
DR   KEGG; mav:MAV_2405; -.
DR   HOGENOM; CLU_071031_0_0_11; -.
DR   OMA; QIYRLPH; -.
DR   OrthoDB; 1243753at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001574; 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.
FT   CHAIN           1..256
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_0000397146"
FT   REGION          235..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  28078 MW;  74B8A6ADF419D355 CRC64;
     MSFPYFISPE QAMRERSELA RKGIARGKSV VALVYAGGVL FVAENPSRSL QKISELYDRV
     GFAAAGKFNE FDNLRRGGIQ FADTRGYAYD RRDVTGRQLA NVYAQTLGTI FTEQAKPYEV
     ELCVAEVAHY GETKPPELYR ITYDGSIADE PHFVVMGGTT EPITTALKDS YAENANLREA
     TRIAVRALRA GSESSNGDQS ALDVGSLEVA ILDVNRPRRA FRRINRPTLE NLLRELDSNG
     SDGNGDAPEL NGGSSD