ID   PSA_KRIFD               Reviewed;         283 AA.
AC   D2Q4H5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
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};
GN   OrderedLocusNames=Kfla_3227;
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Kribbellaceae; Kribbella.
OX   NCBI_TaxID=479435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399;
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   Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) 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}.
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DR   EMBL; CP001736; ADB32289.1; -; Genomic_DNA.
DR   RefSeq; WP_012920845.1; NC_013729.1.
DR   AlphaFoldDB; D2Q4H5; -.
DR   SMR; D2Q4H5; -.
DR   STRING; 479435.Kfla_3227; -.
DR   MEROPS; T01.980; -.
DR   KEGG; kfl:Kfla_3227; -.
DR   eggNOG; COG0638; Bacteria.
DR   HOGENOM; CLU_071031_0_0_11; -.
DR   OrthoDB; 9775643at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000007967; 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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   NCBIfam; TIGR03691; 20S_bact_alpha; 1.
DR   PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Proteasome; Reference proteome.
FT   CHAIN           1..283
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_0000397144"
FT   REGION          228..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  30692 MW;  21E3FE4D188C5C62 CRC64;
     MSTPFYVSPE QLMRDRADFA RKGIAKGRSA IALQYADGIL FVAENRSPAL HKVAEIYDRM
     AFAAVGRYNE FENLRIAGVR LADMRGYSYD RRDVTGRALA NAYAQTLGAI FSSGGEKPLE
     VEILVAEVGT TAADDQIYRL TYDGSIADVR GYAVMGGPAE QVADYVGEHY QEGISLAGAL
     RLAVDALGHD SSEVRQLEPD QIEVAVLDRT RTQVRKFKRI SDQTLARILS ESRPDTAPSP
     ESSAHTEETE TVDGGSYESA AGTSAADDAP IAPPEDPDDN RPL
//