ID J9S815_9ACTN Unreviewed; 258 AA.
AC J9S815;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=KTR9_2373 {ECO:0000313|EMBL:AFR49010.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49010.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR49010.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR49010.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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|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; CP002907; AFR49010.1; -; Genomic_DNA.
DR RefSeq; WP_014926735.1; NC_018581.1.
DR AlphaFoldDB; J9S815; -.
DR STRING; 337191.KTR9_2373; -.
DR KEGG; gor:KTR9_2373; -.
DR PATRIC; fig|337191.3.peg.2691; -.
DR eggNOG; COG0638; Bacteria.
DR HOGENOM; CLU_071031_0_0_11; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000003281; 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 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 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}.
FT REGION 235..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 27753 MW; 93B3AD02D39CCE43 CRC64;
MTFPYYASAE QIMRDRSELA RKGIARGRSV VILTFADGVL FVAENPSNTL RKTSEIYDRI
GFAAVGKYNE FESLRKAGIQ IADMRGYSYD RADVSGLSLA NTYANALGSV FTEQAKPFEV
ELCVAEVARP GKPKRSQLYR ISYDGSITDE TRFLVMGGAT EPIAAALKES YEPDMELGRA
IGVAVDALTA PADNGGGTPT ERRALAAGDL EVAVLDHNRP RRAFRRLTTS TVEGLLPAAA
TATADSGESP GETPSTEQ
//