PSA_ARCFU
ID PSA_ARCFU Reviewed; 246 AA.
AC O29760;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 149.
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=AF_0490;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH
RP BETA SUBUNIT AND CALPAIN-INHIBITOR I, AND SUBUNIT.
RX PubMed=12614609; DOI=10.1016/s0022-2836(03)00080-9;
RA Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R.;
RT "Investigations on the maturation and regulation of archaebacterial
RT proteasomes.";
RL J. Mol. Biol. 327:75-83(2003).
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 probably a gated structure,
CC the ends of the cylinder being occluded by the N-termini of the alpha-
CC subunits. Is likely capped at one or both ends by the proteasome
CC regulatory ATPase, PAN. {ECO:0000269|PubMed:12614609}.
CC -!- INTERACTION:
CC O29760; Q9P996: psmB; NbExp=2; IntAct=EBI-1035754, EBI-1035761;
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; AE000782; AAB90747.1; -; Genomic_DNA.
DR PIR; B69311; B69311.
DR RefSeq; WP_010877997.1; NC_000917.1.
DR PDB; 1J2P; X-ray; 2.60 A; A/B/C/D/E/F/G=1-246.
DR PDB; 1J2Q; X-ray; 2.83 A; A/B/C/D/E/F/G=10-246.
DR PDB; 6HE5; EM; 4.12 A; A/B/C/D/E/F/G=2-246.
DR PDB; 6HE7; EM; 3.69 A; A/B/C/D/E/F/G=12-246.
DR PDB; 6HE8; EM; 6.86 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=5-246.
DR PDB; 6HE9; EM; 6.35 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=5-246.
DR PDB; 6HEA; EM; 7.04 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=5-246.
DR PDB; 6HEC; EM; 6.95 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=5-246.
DR PDB; 6HED; EM; 6.95 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=5-246.
DR PDBsum; 1J2P; -.
DR PDBsum; 1J2Q; -.
DR PDBsum; 6HE5; -.
DR PDBsum; 6HE7; -.
DR PDBsum; 6HE8; -.
DR PDBsum; 6HE9; -.
DR PDBsum; 6HEA; -.
DR PDBsum; 6HEC; -.
DR PDBsum; 6HED; -.
DR AlphaFoldDB; O29760; -.
DR SMR; O29760; -.
DR IntAct; O29760; 2.
DR STRING; 224325.AF_0490; -.
DR MEROPS; T01.970; -.
DR EnsemblBacteria; AAB90747; AAB90747; AF_0490.
DR GeneID; 24794030; -.
DR KEGG; afu:AF_0490; -.
DR eggNOG; arCOG00971; Archaea.
DR HOGENOM; CLU_035750_4_1_2; -.
DR OMA; FQVEYAR; -.
DR OrthoDB; 57654at2157; -.
DR PhylomeDB; O29760; -.
DR EvolutionaryTrace; O29760; -.
DR Proteomes; UP000002199; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Proteasome; Reference proteome.
FT CHAIN 1..246
FT /note="Proteasome subunit alpha"
FT /id="PRO_0000124167"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:1J2P"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1J2Q"
FT STRAND 134..150
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1J2P"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1J2P"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1J2P"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:1J2P"
SQ SEQUENCE 246 AA; 27599 MW; 9F24A7F120ADBE5E CRC64;
MHLPQMGYDR AITVFSPDGR LFQVEYAREA VKRGATAIGI KCKEGVILIA DKRVGSKLLE
ADTIEKIYKI DEHICAATSG LVADARVLID RARIEAQINR LTYDEPITVK ELAKKICDFK
QQYTQYGGVR PFGVSLLIAG VDEVPKLYET DPSGALLEYK ATAIGMGRNA VTEFFEKEYR
DDLSFDDAMV LGLVAMGLSI ESELVPENIE VGYVKVDDRT FKEVSPEELK PYVERANERI
RELLKK
