ID PSA_METJA Reviewed; 261 AA. AC Q60177; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 07-APR-2021, entry version 135. 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=MJ0591; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH PAN. RX PubMed=10692374; DOI=10.1128/jb.182.6.1680-1692.2000; RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.; RT "Biochemical and physical properties of the Methanococcus jannaschii 20S RT proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal RT 26S proteasome."; RL J. Bacteriol. 182:1680-1692(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, GATED RP STRUCTURE, AND SUBUNIT. RX PubMed=19481527; DOI=10.1016/j.molcel.2009.04.021; RA Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.; RT "Structural insights into the regulatory particle of the proteasome from RT Methanocaldococcus jannaschii."; RL Mol. Cell 34:473-484(2009). CC -!- FUNCTION: Component of the proteasome core, a large protease complex CC with broad specificity involved in protein degradation. The CC M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, CC Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays CC caspase-like and chymotrypsin-like activities and low level of trypsin- CC like activity. {ECO:0000255|HAMAP-Rule:MF_00289, CC ECO:0000269|PubMed:10692374}. 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, ECO:0000269|PubMed:10692374, CC ECO:0000269|PubMed:19481527}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L77117; AAB98581.1; -; Genomic_DNA. DR PIR; G64373; G64373. DR RefSeq; WP_010870095.1; NC_000909.1. DR PDB; 3H4P; X-ray; 4.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-261. DR PDBsum; 3H4P; -. DR SMR; Q60177; -. DR STRING; 243232.MJ_0591; -. DR EnsemblBacteria; AAB98581; AAB98581; MJ_0591. DR GeneID; 1451456; -. DR KEGG; mja:MJ_0591; -. DR eggNOG; arCOG00971; Archaea. DR HOGENOM; CLU_035750_4_1_2; -. DR InParanoid; Q60177; -. DR OMA; FQVEYAR; -. DR OrthoDB; 57654at2157; -. DR PhylomeDB; Q60177; -. DR BioCyc; MJAN243232:G1GKE-633-MONOMER; -. DR EvolutionaryTrace; Q60177; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Proteasome; Reference proteome. FT CHAIN 1..261 FT /note="Proteasome subunit alpha" FT /id="PRO_0000124174" SQ SEQUENCE 261 AA; 29321 MW; 93FC7DF277E01AD8 CRC64; MQMVPPSAYD RAITVFSPEG RLYQVEYARE AVRRGTTAIG IACKDGVVLA VDRRITSKLV KIRSIEKIFQ IDDHVAAATS GLVADARVLI DRARLEAQIY RLTYGEEISI EMLAKKICDI KQAYTQHGGV RPFGVSLLIA GIDKNEARLF ETDPSGALIE YKATAIGSGR PVVMELLEKE YRDDITLDEG LELAITALTK ANEDIKPENV DVCIITVKDA QFKKIPVEEI KKLIEKVKKK LNEENKKEEE NREETKEKQE E //