UniProtKB - P9WHT9 (PSB_MYCTU)
Proteasome subunit beta
prcB
Functioni
Catalytic activityi
Activity regulationi
Kineticsi
- KM=56 µM for succinyl-LLVY-7-amino-4-methylcoumarin1 Publication
- Vmax=0.24 nmol/min/mg enzyme with succinyl-LLVY-7-amino-4-methylcoumarin as substrate1 Publication
: proteasomal Pup-dependent pathway Pathwayi
This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.UniRule annotationView all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 58 | Nucleophile1 Publication | 1 | |
Sitei | 58 | Covalent link with the inhibitor MLN-2731 Publication | 1 |
GO - Molecular functioni
- threonine-type endopeptidase activity Source: UniProtKB
- zymogen binding Source: CAFA
GO - Biological processi
- modification-dependent protein catabolic process Source: UniProtKB
- pathogenesis Source: MTBBASE
- proteasomal protein catabolic process Source: UniProtKB
- proteolysis involved in cellular protein catabolic process Source: MTBBASE
Keywordsi
Molecular function | Hydrolase, Protease, Threonine protease |
Biological process | Virulence |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
Names & Taxonomyi
Protein namesi | Recommended name: Proteasome subunit betaUniRule annotation (EC:3.4.25.1UniRule annotation)Alternative name(s): 20S proteasome beta subunitUniRule annotation Proteasome core protein PrcBUniRule annotation |
Gene namesi | Name:prcBUniRule annotation Ordered Locus Names:Rv2110c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2110c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
- extracellular region Source: CAFA
- plasma membrane Source: MTBBASE
- proteasome core complex, alpha-subunit complex Source: GO_Central
- proteasome core complex, beta-subunit complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, ProteasomePathology & Biotechi
Biotechnological usei
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 58 | T → A: Loss of proteasome proteolytic activity. This mutant enables optimal growth in vitro and in vivo, confers RNI resistance but is not sufficient for persistence in mice. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04732, N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
PropeptideiPRO_0000383485 | 1 – 57 | Removed in mature form; by autocatalysisUniRule annotation1 PublicationAdd BLAST | 57 | |
ChainiPRO_0000383486 | 58 – 291 | Proteasome subunit betaAdd BLAST | 234 |
Post-translational modificationi
Keywords - PTMi
Autocatalytic cleavage, Phosphoprotein, ZymogenProteomic databases
PaxDbi | P9WHT9 |
Interactioni
Subunit structurei
The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped by the proteasome-associated ATPase, ARC (Mpa).
UniRule annotation4 PublicationsBinary interactionsi
P9WHT9
With | #Exp. | IntAct |
---|---|---|
prcA [P9WHU1] | 6 | EBI-7947958,EBI-7948002 |
GO - Molecular functioni
- zymogen binding Source: CAFA
Protein-protein interaction databases
IntActi | P9WHT9, 1 interactor |
MINTi | P9WHT9 |
STRINGi | 83332.Rv2110c |
Structurei
Secondary structure
3D structure databases
SMRi | P9WHT9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0638, Bacteria |
OMAi | NLGMAMQ |
PhylomeDBi | P9WHT9 |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
HAMAPi | MF_02113_B, Proteasome_B_B, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR022483, Pept_T1A_Psome_suB_actinobac IPR001353, Proteasome_sua/b IPR023333, Proteasome_suB-type |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR03690, 20S_bact_beta, 1 hit |
PROSITEi | View protein in PROSITE PS51476, PROTEASOME_BETA_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MTWPLPDRLS INSLSGTPAV DLSSFTDFLR RQAPELLPAS ISGGAPLAGG
60 70 80 90 100
DAQLPHGTTI VALKYPGGVV MAGDRRSTQG NMISGRDVRK VYITDDYTAT
110 120 130 140 150
GIAGTAAVAV EFARLYAVEL EHYEKLEGVP LTFAGKINRL AIMVRGNLAA
160 170 180 190 200
AMQGLLALPL LAGYDIHASD PQSAGRIVSF DAAGGWNIEE EGYQAVGSGS
210 220 230 240 250
LFAKSSMKKL YSQVTDGDSG LRVAVEALYD AADDDSATGG PDLVRGIFPT
260 270 280 290
AVIIDADGAV DVPESRIAEL ARAIIESRSG ADTFGSDGGE K
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44885.1 |
PIRi | A70512 |
RefSeqi | NP_216626.1, NC_000962.3 WP_003411023.1, NZ_NVQJ01000058.1 |
Genome annotation databases
EnsemblBacteriai | CCP44885; CCP44885; Rv2110c |
GeneIDi | 23491702 887508 |
KEGGi | mtu:Rv2110c mtv:RVBD_2110c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44885.1 |
PIRi | A70512 |
RefSeqi | NP_216626.1, NC_000962.3 WP_003411023.1, NZ_NVQJ01000058.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2FHG | X-ray | 3.23 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 58-291 | [»] | |
2FHH | X-ray | 2.99 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 58-291 | [»] | |
2JAY | X-ray | 1.99 | A | 1-291 | [»] | |
3H6F | X-ray | 2.51 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 59-291 | [»] | |
3H6I | X-ray | 2.43 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 59-291 | [»] | |
3HF9 | X-ray | 2.88 | 2/4/C/E/G/H/J/L/N/P/R/T/V/X/Z/c/e/g/h/j/l/n/p/r/t/v/x/z | 59-291 | [»] | |
3HFA | X-ray | 2.50 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 58-291 | [»] | |
3KRD | X-ray | 2.50 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 58-291 | [»] | |
3MFE | X-ray | 2.60 | 2/C/E/H/J/L/N/P/R/T/X/Z | 59-291 | [»] | |
G/V | 58-291 | [»] | ||||
3MI0 | X-ray | 2.20 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 58-291 | [»] | |
3MKA | X-ray | 2.51 | 2/C/E/G/H/J/L/N/P/R/T/V/X/Z | 1-291 | [»] | |
5LZP | electron microscopy | 3.45 | A/C/E/F/G/I/K/L/N/O/P/R/T/U | 59-291 | [»] | |
5THO | X-ray | 3.00 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
5TRG | X-ray | 2.80 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
5TRR | X-ray | 3.10 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
5TRS | X-ray | 3.08 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
5TRY | X-ray | 3.00 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
5TS0 | X-ray | 2.85 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
6BGL | electron microscopy | 3.40 | P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c | 58-291 | [»] | |
6BGO | electron microscopy | 4.20 | P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c | 58-291 | [»] | |
6OCW | X-ray | 2.60 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
6OCZ | X-ray | 2.65 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
6ODE | X-ray | 2.90 | H/I/J/K/L/M/N/V/W/X/Y/Z/a/b | 58-291 | [»] | |
SMRi | P9WHT9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P9WHT9, 1 interactor |
MINTi | P9WHT9 |
STRINGi | 83332.Rv2110c |
Chemistry databases
DrugBanki | DB04732, N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID |
Proteomic databases
PaxDbi | P9WHT9 |
Genome annotation databases
EnsemblBacteriai | CCP44885; CCP44885; Rv2110c |
GeneIDi | 23491702 887508 |
KEGGi | mtu:Rv2110c mtv:RVBD_2110c |
Organism-specific databases
TubercuListi | Rv2110c |
Phylogenomic databases
eggNOGi | COG0638, Bacteria |
OMAi | NLGMAMQ |
PhylomeDBi | P9WHT9 |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
HAMAPi | MF_02113_B, Proteasome_B_B, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR022483, Pept_T1A_Psome_suB_actinobac IPR001353, Proteasome_sua/b IPR023333, Proteasome_suB-type |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR03690, 20S_bact_beta, 1 hit |
PROSITEi | View protein in PROSITE PS51476, PROTEASOME_BETA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PSB_MYCTU | |
Accessioni | P9WHT9Primary (citable) accession number: P9WHT9 Secondary accession number(s): L0T8V8, O33245, Q7D7I2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 44 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries