PSA_METB6
ID PSA_METB6 Reviewed; 240 AA.
AC A7I9C7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 PsmA {ECO:0000255|HAMAP-Rule:MF_00289};
GN Name=psmA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=Mboo_1822;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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 PAN-20S
CC proteasome complex, via the docking of the C-termini of PAN into the
CC intersubunit pockets in the alpha-rings, triggers opening of the gate
CC for substrate entry. Interconversion between the open-gate and close-
CC gate conformations leads to a dynamic regulation of the 20S proteasome
CC proteolysis activity. {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 at one or both ends by the proteasome regulatory ATPase, PAN.
CC {ECO:0000255|HAMAP-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; CP000780; ABS56338.1; -; Genomic_DNA.
DR RefSeq; WP_012107389.1; NC_009712.1.
DR AlphaFoldDB; A7I9C7; -.
DR SMR; A7I9C7; -.
DR STRING; 456442.Mboo_1822; -.
DR PRIDE; A7I9C7; -.
DR EnsemblBacteria; ABS56338; ABS56338; Mboo_1822.
DR GeneID; 5411038; -.
DR KEGG; mbn:Mboo_1822; -.
DR eggNOG; arCOG00971; Archaea.
DR HOGENOM; CLU_035750_4_1_2; -.
DR OMA; FQVEYAR; -.
DR OrthoDB; 57654at2157; -.
DR Proteomes; UP000002408; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03756; proteasome_alpha_archeal; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00289_A; Proteasome_A_A; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR019982; Proteasome_asu_arc.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03633; arc_protsome_A; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Proteasome; Reference proteome.
FT CHAIN 1..240
FT /note="Proteasome subunit alpha"
FT /id="PRO_1000021786"
SQ SEQUENCE 240 AA; 26319 MW; DC5D011CDCD08FE5 CRC64;
MQPQYQMGYD RAITVFSPDG RLYQVEYARE AVKRGTTAVG IKAHDGVVLI VDKRVSSKLL
ESSSIEKIFK IDEHIGVASS GLVGDARALV DRARIECQIN RVSYDERIEV EALAKKLCDH
MQTLTQYGGI RPYGTALLIA GVSDGESRLF ETDPSGTLLE YKATGIGIGR PAAMKVFEEE
YTADLALKDA ILLGLKALHS ATEGKFDVDT VEMGIVESST AQFKKMTKEE VASYVGQFKQ