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-JUN-2017, entry version 119.
DE RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289};
DE EC=3.4.25.1 {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 /
OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; 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.,
RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA Klenk H.-P., 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
RT 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the
RT eucaryal 26S proteasome.";
RL J. Bacteriol. 182:1680-1692(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT,
RP GATED 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
RT from Methanocaldococcus jannaschii.";
RL Mol. Cell 34:473-484(2009).
CC -!- FUNCTION: Component of the proteasome core, a large protease
CC complex with broad specificity involved in protein degradation.
CC The M.jannaschii proteasome is able to cleave oligopeptides after
CC Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala.
CC Thus, displays caspase-like and chymotrypsin-like activities and
CC low level of trypsin-like activity. {ECO:0000255|HAMAP-
CC Rule:MF_00289, ECO:0000269|PubMed:10692374}.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity. {ECO:0000255|HAMAP-Rule:MF_00289,
CC ECO:0000269|PubMed:10692374}.
CC -!- ENZYME REGULATION: The formation of the proteasomal ATPase PAN-20S
CC proteasome complex, via the docking of the C-termini of PAN into
CC the intersubunit pockets in the alpha-rings, triggers opening of
CC the gate for substrate entry. Interconversion between the open-
CC gate and close-gate conformations leads to a dynamic regulation of
CC the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP-
CC Rule:MF_00289}.
CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14
CC beta subunits that assemble into four stacked heptameric rings,
CC resulting in a barrel-shaped structure. The two inner rings, each
CC composed of seven catalytic beta subunits, are sandwiched by two
CC outer rings, each composed of seven alpha subunits. The catalytic
CC chamber with the active sites is on the inside of the barrel. Has
CC a gated structure, the ends of the cylinder being occluded by the
CC N-termini of the alpha-subunits. Is capped at one or both ends by
CC the proteasome regulatory ATPase, PAN. {ECO:0000255|HAMAP-
CC 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.
CC {ECO:0000255|HAMAP-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 ProteinModelPortal; 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 eggNOG; COG0638; LUCA.
DR InParanoid; Q60177; -.
DR KO; K03432; -.
DR OMA; QMGYDRA; -.
DR OrthoDB; POG093Z086S; -.
DR PhylomeDB; Q60177; -.
DR EvolutionaryTrace; Q60177; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Hydrolase; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT CHAIN 1 261 Proteasome subunit alpha.
FT /FTId=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
//