PSB1_RHOER
ID PSB1_RHOER Reviewed; 294 AA.
AC Q53079;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Proteasome subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=20S proteasome beta subunit 1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PrcB 1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=prcB1 {ECO:0000255|HAMAP-Rule:MF_02113};
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], PROTEIN SEQUENCE OF 66-75, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND 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) OF PROCESSED AND UNPROCESSED FORMS IN
RP COMPLEX WITH ALPHA 1 SUBUNIT, SUBUNIT, DOMAIN, AND PROTEASOME ASSEMBLY
RP 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) OF MUTANT ALA-210 IN COMPLEX WITH
RP ALPHA 1 SUBUNIT, PROTEASOME ASSEMBLY PROCESS, SUBUNIT, MUTAGENESIS OF
RP PHE-210 AND 216-LYS-LYS-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
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_02113,
CC ECO:0000269|PubMed:7583123, ECO:0000269|PubMed:9000518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113,
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_02113}.
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_02113}.
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 Q53079; Q53080: prcA1; NbExp=6; IntAct=EBI-1037574, EBI-1037564;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC -!- DOMAIN: In contrast to M.tuberculosis, the propeptide is required for
CC correct proteasome folding and assembly. The propeptide is positioned
CC strategically at the region where it can act as an assembly-promoting
CC factor by linking its own beta-subunit to two adjacent alpha-subunits
CC at the same time. {ECO:0000269|PubMed:14659753}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC Rule:MF_02113}.
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DR EMBL; U26421; AAC45740.1; -; Genomic_DNA.
DR PDB; 1Q5Q; X-ray; 2.60 A; H/I/J/K/L/M/N=66-294.
DR PDB; 1Q5R; X-ray; 3.10 A; H/I/J/K/L/M/N=1-293.
DR PDB; 2H6J; X-ray; 3.20 A; H/I/J/K/L/M/N=1-292.
DR PDBsum; 1Q5Q; -.
DR PDBsum; 1Q5R; -.
DR PDBsum; 2H6J; -.
DR AlphaFoldDB; Q53079; -.
DR SMR; Q53079; -.
DR DIP; DIP-29144N; -.
DR IntAct; Q53079; 1.
DR MEROPS; T01.005; -.
DR UniPathway; UPA00997; -.
DR EvolutionaryTrace; Q53079; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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_02113_B; Proteasome_B_B; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR022483; PSB_actinobac.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03690; 20S_bact_beta; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Protease; Proteasome; Threonine protease; Zymogen.
FT PROPEP 1..65
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113,
FT ECO:0000269|PubMed:7583123"
FT /id="PRO_0000397124"
FT CHAIN 66..294
FT /note="Proteasome subunit beta 1"
FT /id="PRO_0000397125"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT MUTAGEN 210
FT /note="F->A: Prevents full assembly of proteasome."
FT /evidence="ECO:0000269|PubMed:16843899"
FT MUTAGEN 216..217
FT /note="KK->AA: Prevents full assembly of proteasome."
FT /evidence="ECO:0000269|PubMed:16843899"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1Q5R"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1Q5R"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1Q5R"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 114..135
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1Q5R"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1Q5Q"
FT HELIX 272..287
FT /evidence="ECO:0007829|PDB:1Q5Q"
SQ SEQUENCE 294 AA; 31161 MW; 57914462BA4A05CD CRC64;
MTADRPALRT GDRDTRLSFG SNLSSFTDYL RGHAPELLPE NRIGHRSHST RGGDGMESGD
LAPHGTTIVA LTYKGGVLLA GDRRATQGNL IASRDVEKVY VTDEYSAAGI AGTAGIAIEL
VRLFAVELEH YEKIEGVPLT FDGKANRLAS MVRGNLGAAM QGLAVVPLLV GYDLDADDES
RAGRIVSYDV VGGRYEERAG YHAVGSGSLF AKSALKKIYS PDSDEETALR AAIESLYDAA
DDDSATGGPD LTRGIYPTAV TITQAGAVHV SEETTSELAR RIVAERTEQG GSAR
