ID   PSA1_RHOER              Reviewed;         259 AA.
AC   Q53080;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 102.
DE   RecName: Full=Proteasome subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit 1 {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PrcA 1 {ECO:0000255|HAMAP-Rule:MF_00289};
GN   Name=prcA1 {ECO:0000255|HAMAP-Rule:MF_00289};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, BLOCKAGE OF
RP   N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP   SUBUNIT.
RC   STRAIN=NI86/21;
RX   PubMed=7583123; DOI=10.1016/s0960-9822(95)00153-9;
RA   Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G.,
RA   Tanaka K., de Mot R., Baumeister W.;
RT   "The first characterization of a eubacterial proteasome: the 20S complex of
RT   Rhodococcus.";
RL   Curr. Biol. 5:766-774(1995).
RN   [2]
RP   SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP   PARAMETERS.
RC   STRAIN=NI86/21;
RX   PubMed=9000518; DOI=10.1016/s0014-5793(96)01403-2;
RA   Zuhl F., Tamura T., Dolenc I., Cejka Z., Nagy I., De Mot R., Baumeister W.;
RT   "Subunit topology of the Rhodococcus proteasome.";
RL   FEBS Lett. 400:83-90(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH BETA 1 SUBUNIT, AND
RP   PROTEASOME ASSEMBLY PROCESS.
RX   PubMed=14659753; DOI=10.1016/j.jmb.2003.08.029;
RA   Kwon Y.D., Nagy I., Adams P.D., Baumeister W., Jap B.K.;
RT   "Crystal structures of the Rhodococcus proteasome with and without its pro-
RT   peptides: implications for the role of the pro-peptide in proteasome
RT   assembly.";
RL   J. Mol. Biol. 335:233-245(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BETA 1 SUBUNIT, AND
RP   PROTEASOME ASSEMBLY PROCESS.
RX   PubMed=16843899; DOI=10.1016/j.str.2006.05.019;
RA   Witt S., Kwon Y.D., Sharon M., Felderer K., Beuttler M., Robinson C.V.,
RA   Baumeister W., Jap B.K.;
RT   "Proteasome assembly triggers a switch required for active-site
RT   maturation.";
RL   Structure 14:1179-1188(2006).
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation. The
CC       R.erythropolis proteasomes are able to cleave oligopeptides after Tyr,
CC       Phe and Leu, very poorly after Arg but not after Glu. Thus, displays
CC       chymotrypsin-like activity, low trypsin-like activity but no caspase-
CC       like activity. {ECO:0000255|HAMAP-Rule:MF_00289,
CC       ECO:0000269|PubMed:7583123, ECO:0000269|PubMed:9000518}.
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:0000255|HAMAP-Rule:MF_00289}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=61.4 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1
CC         proteasome subtype) {ECO:0000269|PubMed:9000518};
CC         KM=66.4 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha2
CC         proteasome subtype) {ECO:0000269|PubMed:9000518};
CC         KM=71.2 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2
CC         proteasome subtype) {ECO:0000269|PubMed:9000518};
CC         KM=84.3 uM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1
CC         proteasome subtype) {ECO:0000269|PubMed:9000518};
CC         Note=The Vmax observed with the beta2-alpha1 proteasome subtype is
CC         2.2-fold, 1.2-fold and 4-fold higher than that with the beta2-alpha2,
CC         beta1-alpha2 and beta1-alpha1 subtypes, respectively.;
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. All four combinations of alpha- and
CC       beta-subunits (beta2-alpha1, beta2-alpha2, beta1-alpha2 and beta1-
CC       alpha1) yield fully assembled and proteolytically active proteasomes.
CC       The catalytic chamber with the active sites is on the inside of the
CC       barrel. Has probably a gated structure, the ends of the cylinder being
CC       occluded by the N-termini of the alpha-subunits. Is likely capped by
CC       the proteasome-associated ATPase, ARC. {ECO:0000269|PubMed:14659753,
CC       ECO:0000269|PubMed:16843899, ECO:0000269|PubMed:7583123,
CC       ECO:0000269|PubMed:9000518}.
CC   -!- INTERACTION:
CC       Q53080; Q53079: prcB1; NbExp=6; IntAct=EBI-1037564, EBI-1037574;
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; U26421; AAC45741.1; -; Genomic_DNA.
DR   PDB; 1Q5Q; X-ray; 2.60 A; A/B/C/D/E/F/G=1-259.
DR   PDB; 1Q5R; X-ray; 3.10 A; A/B/C/D/E/F/G=8-259.
DR   PDB; 2H6J; X-ray; 3.20 A; A/B/C/D/E/F/G=1-259.
DR   PDBsum; 1Q5Q; -.
DR   PDBsum; 1Q5R; -.
DR   PDBsum; 2H6J; -.
DR   AlphaFoldDB; Q53080; -.
DR   SMR; Q53080; -.
DR   DIP; DIP-29143N; -.
DR   IntAct; Q53080; 1.
DR   UniPathway; UPA00997; -.
DR   EvolutionaryTrace; Q53080; -.
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:InterPro.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR   CDD; cd01901; Ntn_hydrolase; 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   PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Proteasome.
FT   CHAIN           1..259
FT                   /note="Proteasome subunit alpha 1"
FT                   /id="PRO_0000397128"
FT   REGION          231..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           10..25
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           68..88
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:2H6J"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:2H6J"
FT   STRAND          147..159
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
FT   HELIX           225..229
FT                   /evidence="ECO:0007829|PDB:1Q5Q"
SQ   SEQUENCE   259 AA;  28312 MW;  C1A97CACA2D77050 CRC64;
     MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTFRDGVL FVAENPSTAL HKVSELYDRL
     GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA NAYAQTLGTI FTEQPKPYEV
     EICVAEVGRV GSPKAPQLYR ITYDGSIVDE QHFVVMGGTT EPIATAMRES YRADLDLEAA
     VGIAVNALRQ GGAGEGEKRN VDVASLEVAV LDQSRPRRAF RRIAGTALEQ LVPAEPAAAS
     ESAPEPKPDT ETKPADTQD
//