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   25-MAY-2022, entry version 138.
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}.
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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   AlphaFoldDB; Q60177; -.
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   EvolutionaryTrace; Q60177; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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   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"
FT   REGION          242..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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