PSA1_RHOER
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 25-MAY-2022, entry version 97.
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; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC 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 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 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