ID   A0A7U3VM37_9ACTN        Unreviewed;       249 AA.
AC   A0A7U3VM37;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   27-NOV-2024, entry version 14.
DE   RecName: Full=Proteasome subunit alpha {ECO:0000256|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit {ECO:0000256|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PrcA {ECO:0000256|HAMAP-Rule:MF_00289};
GN   Name=prcA {ECO:0000256|HAMAP-Rule:MF_00289};
GN   ORFNames=RVR_1336 {ECO:0000313|EMBL:BBA96162.1};
OS   Streptomyces sp. SN-593.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=659352 {ECO:0000313|EMBL:BBA96162.1, ECO:0000313|Proteomes:UP000595703};
RN   [1] {ECO:0000313|EMBL:BBA96162.1, ECO:0000313|Proteomes:UP000595703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN-593 {ECO:0000313|EMBL:BBA96162.1,
RC   ECO:0000313|Proteomes:UP000595703};
RX   PubMed=20348259; DOI=10.1128/JB.01557-09;
RA   Takahashi S., Takagi H., Toyoda A., Uramoto M., Nogawa T., Ueki M.,
RA   Sakaki Y., Osada H.;
RT   "Biochemical characterization of a novel indole prenyltransferase from
RT   Streptomyces sp. SN-593.";
RL   J. Bacteriol. 192:2839-2851(2010).
RN   [2] {ECO:0000313|EMBL:BBA96162.1, ECO:0000313|Proteomes:UP000595703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN-593 {ECO:0000313|EMBL:BBA96162.1,
RC   ECO:0000313|Proteomes:UP000595703};
RA   Panthee S., Takahashi S., Takagi H., Nogawa T., Oowada E., Uramoto M.,
RA   Osada H.;
RT   "Furaquinocins I and J: novel polyketide isoprenoid hybrid compounds from
RT   Streptomyces reveromyceticus SN-593.";
RL   J. Antibiot. 64:509-513(2011).
RN   [3] {ECO:0000313|EMBL:BBA96162.1, ECO:0000313|Proteomes:UP000595703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN-593 {ECO:0000313|EMBL:BBA96162.1,
RC   ECO:0000313|Proteomes:UP000595703};
RX   PubMed=21642985; DOI=10.1038/nchembio.583;
RA   Takahashi S., Toyoda A., Sekiyama Y., Takagi H., Nogawa T., Uramoto M.,
RA   Suzuki R., Koshino H., Kumano T., Panthee S., Dairi T., Ishikawa J.,
RA   Ikeda H., Sakaki Y., Osada H.;
RT   "Reveromycin A biosynthesis uses RevG and RevJ for stereospecific
RT   spiroacetal formation.";
RL   Nat. Chem. Biol. 7:461-468(2011).
RN   [4] {ECO:0000313|EMBL:BBA96162.1, ECO:0000313|Proteomes:UP000595703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN-593 {ECO:0000313|EMBL:BBA96162.1,
RC   ECO:0000313|Proteomes:UP000595703};
RA   Panthee S., Kito N., Hayashi T., Shimizu T., Ishikawa J., Hamamoto H.,
RA   Osada H., Takahashi S.;
RT   "beta-carboline chemical signals induce reveromycin production through a
RT   LuxR family regulator in Streptomyces sp. SN-593.";
RL   Sci. Rep. 10:0-10230(2020).
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00289}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00289}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00289}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|HAMAP-
CC       Rule:MF_00289, ECO:0000256|PROSITE-ProRule:PRU00808}.
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DR   EMBL; AP018365; BBA96162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7U3VM37; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000595703; 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   CDD; cd01906; proteasome_protease_HslV; 1.
DR   FunFam; 3.60.20.10:FF:000023; Proteasome subunit alpha; 1.
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; IPR050115; Proteasome_alpha.
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 {ECO:0000256|HAMAP-Rule:MF_00289};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW   Rule:MF_00289}; Reference proteome {ECO:0000313|Proteomes:UP000595703}.
SQ   SEQUENCE   249 AA;  27444 MW;  41BD36629A8F9E7F CRC64;
     MSTPFYVSPQ QAMADRAEYA RKGIARGRSV VVLQYTDGIV FVAENPSRAL HKVSEIYDRI
     AFAAVGKYNE FENLRIGGVR YADLRGYTYD RDDVTARGLA NVYAQTLGTI FSSVGEKPYE
     VELIVAEVGA APEDDQIYRL PHDGSIVDEH GAVAVGGNSD QIGSYLDQRH RDGMTLAEAL
     ALAVESLGRD ANGGSDRQLT AEQLEVAVLD RTRPQQRKFR RILGRQLSRL LDTESAATTK
     TDEPSDEEE
//