PSA_STRCO
ID PSA_STRCO Reviewed; 254 AA.
AC Q7AKQ6; O87599;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
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 PrcA {ECO:0000255|HAMAP-Rule:MF_00289};
GN Name=prcA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=SCO1643;
GN ORFNames=SCI41.26;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, SUBUNIT, ACTIVITY REGULATION, TEMPERATURE DEPENDENCE, AND
RP BLOCKAGE OF N-TERMINUS.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9765579; DOI=10.1128/jb.180.20.5448-5453.1998;
RA Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R.;
RT "The 20S proteasome of Streptomyces coelicolor.";
RL J. Bacteriol. 180:5448-5453(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The
CC S.coelicolor proteasome is able to cleave oligopeptides after
CC hydrophobic residues, but not after basic or acidic residues, thus
CC displaying chymotrypsin-like activity but not trypsin-like activity.
CC {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:9765579}.
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 (By similarity). Peptidolytic activity
CC is completely inhibited by lactacystin, and to a lesser extent, by N-
CC acetyl-Leu-Leu-norleucinal (Ac-LLnL) and benzoyloxycarbonyl-Leu-Leu-
CC Leu-vinylsulfone (Z-LLL-VS) in vitro. {ECO:0000255|HAMAP-Rule:MF_00289,
CC ECO:0000269|PubMed:9765579}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:9765579};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {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 by the proteasome-associated ATPase, ARC.
CC {ECO:0000269|PubMed:9765579}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP-
CC Rule:MF_00289}.
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DR EMBL; AF086832; AAC64278.1; -; Genomic_DNA.
DR EMBL; AL939109; CAB59496.1; -; Genomic_DNA.
DR RefSeq; NP_625918.1; NC_003888.3.
DR RefSeq; WP_011027897.1; NZ_VNID01000018.1.
DR AlphaFoldDB; Q7AKQ6; -.
DR SMR; Q7AKQ6; -.
DR STRING; 100226.SCO1643; -.
DR MEROPS; T01.011; -.
DR GeneID; 1097074; -.
DR KEGG; sco:SCO1643; -.
DR PATRIC; fig|100226.15.peg.1658; -.
DR eggNOG; COG0638; Bacteria.
DR HOGENOM; CLU_071031_0_0_11; -.
DR InParanoid; Q7AKQ6; -.
DR OMA; QIYRLPH; -.
DR PhylomeDB; Q7AKQ6; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001973; 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:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.60.20.10; -; 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 PANTHER; PTHR11599:SF69; PTHR11599:SF69; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03691; 20S_bact_alpha; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Proteasome; Reference proteome.
FT CHAIN 1..254
FT /note="Proteasome subunit alpha"
FT /id="PRO_0000383484"
FT REGION 231..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 27883 MW; 97460DA9883C33D8 CRC64;
MSTPFYVSPQ QAMADRAEYA RKGIARGRSL VVLQYADGIV FVGENPSRAL HKFSEIYDRI
GFAAAGKYNE YENLRIGGVR YADLRGYTYD RDDVTARGLA NVYAQTLGTI FSSQAEKPYE
VELVVAEVGD SPENDQIYRL PHDGSIVDEH GSVAVGGNAE QISGYLDQRH RDGMTLAEAL
KLAVQALSRD TNGTEREIPA ERLEVAVLDR TRPQQRKFKR IVGGQLSRLL ESGAASADGE
AETEAETDSG SDEE
