PSA2_RHOER
ID PSA2_RHOER Reviewed; 255 AA.
AC Q53084;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Proteasome subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=20S proteasome alpha subunit 2 {ECO:0000255|HAMAP-Rule:MF_00289};
DE AltName: Full=Proteasome core protein PrcA 2 {ECO:0000255|HAMAP-Rule:MF_00289};
GN Name=prcA2 {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).
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:7583123,
CC ECO:0000269|PubMed:9000518}.
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; U26422; AAC45737.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53084; -.
DR SMR; Q53084; -.
DR STRING; 1833.XU06_14795; -.
DR MEROPS; T01.980; -.
DR UniPathway; UPA00997; -.
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 Cytoplasm; Direct protein sequencing; Proteasome.
FT CHAIN 1..255
FT /note="Proteasome subunit alpha 2"
FT /id="PRO_0000397129"
FT REGION 229..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 27859 MW; BCACDFEBDDB767B5 CRC64;
MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTYRDGVL FVAENPSRAL HKVSELYDRL
GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA NAYAQTLGTI FTEQPKPYEV
EICVAEIGRF GSSTPAQLYR ITYDGSIADE QEFVVMGGTT EPIVTAMRES YQRDLDLESA
VRLAVGALQK GGPAPAGTTE AEPRTLDVSA LEVAVLDSNR PRRAFKRIAG SSLEEMLPTP
AATEDAPPAN GDAPS
