ID G7H0K6_9ACTN Unreviewed; 259 AA.
AC G7H0K6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Proteasome subunit alpha {ECO:0000256|HAMAP-Rule:MF_00289};
DE AltName: Full=20S proteasome alpha subunit {ECO:0000256|HAMAP-Rule:MF_00289};
DE AltName: Full=Proteasome core protein PrcA {ECO:0000256|HAMAP-Rule:MF_00289};
GN Name=prcA {ECO:0000256|HAMAP-Rule:MF_00289,
GN ECO:0000313|EMBL:GAB09381.1};
GN ORFNames=GOARA_036_01130 {ECO:0000313|EMBL:GAB09381.1};
OS Gordonia araii NBRC 100433.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB09381.1, ECO:0000313|Proteomes:UP000035088};
RN [1] {ECO:0000313|EMBL:GAB09381.1, ECO:0000313|Proteomes:UP000035088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB09381.1,
RC ECO:0000313|Proteomes:UP000035088};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation.
CC {ECO:0000256|HAMAP-Rule:MF_00289}.
CC -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S
CC proteasome complex, likely via the docking of the C-termini of ARC into
CC the intersubunit pockets in the alpha-rings, may trigger opening of the
CC gate for substrate entry. Interconversion between the open-gate and
CC close-gate conformations leads to a dynamic regulation of the 20S
CC proteasome proteolysis activity. {ECO:0000256|HAMAP-Rule:MF_00289}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000256|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 by the proteasome-associated ATPase, ARC. {ECO:0000256|HAMAP-
CC Rule:MF_00289}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00289}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|HAMAP-
CC Rule:MF_00289, ECO:0000256|PROSITE-ProRule:PRU00808}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB09381.1}.
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DR EMBL; BAEE01000036; GAB09381.1; -; Genomic_DNA.
DR RefSeq; WP_007321457.1; NZ_JABELY010000006.1.
DR AlphaFoldDB; G7H0K6; -.
DR STRING; 1073574.GOARA_036_01130; -.
DR OrthoDB; 9775643at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000035088; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01906; proteasome_protease_HslV; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00289_B; Proteasome_A_B; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR022296; Proteasome_asu_bac.
DR InterPro; IPR001353; Proteasome_sua/b.
DR NCBIfam; TIGR03691; 20S_bact_alpha; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00289};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_00289}.
FT REGION 192..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 27822 MW; 85CAD094552AE084 CRC64;
MTFPYYASAE QIMRDRSELA RKGIARGRSV VTLTYADGVL FVAENPSNTL RKVSEIYDRI
GFAAVGKYNE FESLRRAGIQ LADLRGYSYD RADVSGLSLA NAYATTLGTV FTEQPKPYEV
ELCVAEVAKP GRDTPSQLYR IGYDGSVVDE TRFLVMGGHT EAITAALTES FEPDLALTAA
LGIAVTALAN PTPPAQPDAG RATSNGAAND SSPTTPRELA ATDLEVAVLD RTRPRRAFRR
LGHDEVAALL ADAGKSKKG
//
