PSA_GEOOG
ID PSA_GEOOG Reviewed; 287 AA.
AC D2S6E3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=Gobs_2683;
OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC Geodermatophilus.
OX NCBI_TaxID=526225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / NBRC
RC 13315 / NRRL B-3577 / G-20;
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 Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL Submitted (JAN-2010) 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; CP001867; ADB75317.1; -; Genomic_DNA.
DR RefSeq; WP_012948750.1; NC_013757.1.
DR AlphaFoldDB; D2S6E3; -.
DR SMR; D2S6E3; -.
DR STRING; 526225.Gobs_2683; -.
DR MEROPS; T01.980; -.
DR EnsemblBacteria; ADB75317; ADB75317; Gobs_2683.
DR KEGG; gob:Gobs_2683; -.
DR eggNOG; COG0638; Bacteria.
DR HOGENOM; CLU_071031_0_0_11; -.
DR OMA; QIYRLPH; -.
DR OrthoDB; 1243753at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001382; 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..287
FT /note="Proteasome subunit alpha"
FT /id="PRO_0000397140"
FT REGION 241..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 30406 MW; 8B93882485BE6385 CRC64;
MTMPYYASPE QLMRDKSEYA RKGISRGRSV AVVTYADGVL FIAENPSSTL HKVGELYDRI
GFAAVGRYSE FESLRVAGVR LADVRGYSYN RRDVTGRVIA NAYAQTLGEV FTQQMKPFEV
ELCVAEVGET PETDQLYRLT FDGSVVDEPD FVVMGGQAEA VSANLREHFL PGMGLAEALR
VGVQALSAVS PATSAGNGGP ALLTAEQLEV AVLDRRRPKR AFRRIAGAAL RPLLDRQEED
GVVAGEEPHT AAHAPSVPQP GAPAGLGDPG APDTGGTAGS GGEAPTT