UniProtKB - P9WHU1 (PSA_MYCTU)
Proteasome subunit alpha
prcA
Functioni
Miscellaneous
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.
GO - Molecular functioni
- threonine-type endopeptidase activity Source: UniProtKB
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
Biological process | Virulence |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
Names & Taxonomyi
Protein namesi | Recommended name: Proteasome subunit alphaUniRule annotationAlternative name(s): 20S proteasome alpha subunitUniRule annotation Proteasome core protein PrcAUniRule annotation |
Gene namesi | Name:prcAUniRule annotation Ordered Locus Names:Rv2109c |
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 | Rv2109c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cell wall Source: MTBBASE
- cytoplasm Source: UniProtKB-SubCell
- plasma membrane Source: MTBBASE
- proteasome core complex, alpha-subunit complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, ProteasomePathology & Biotechi
Biotechnological usei
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1 – 8 | Missing : Markedly increases peptidolytic activity. Disappearance of the apparent obstruction in alpha rings. Designated open-gate mutant. 1 Publication | 8 |
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 |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources1 Publication | |||
ChainiPRO_0000383482 | 2 – 248 | Proteasome subunit alphaAdd BLAST | 247 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine; partialCombined sources1 Publication | 1 | |
Modified residuei | 84 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 178 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 202 | Phosphothreonine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | P9WHU1 |
PTM databases
iPTMneti | P9WHU1 |
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). Can also interact with the bacterial proteasome activator Bpa through the C-terminal hydrophobic-tyrosine-X motif (HbYX motif) of Bpa; Bpa forms a homooligomeric ring-like structure which stacks co-axially with the proteasomal alpha-rings (PubMed:25469515).
UniRule annotation5 PublicationsBinary interactionsi
P9WHU1
With | #Exp. | IntAct |
---|---|---|
prcB [P9WHT9] | 6 | EBI-7948002,EBI-7947958 |
Protein-protein interaction databases
IntActi | P9WHU1, 1 interactor |
MINTi | P9WHU1 |
STRINGi | 83332.Rv2109c |
Structurei
Secondary structure
3D structure databases
SMRi | P9WHU1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0638, Bacteria |
OMAi | KYNEFEN |
PhylomeDBi | P9WHU1 |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
HAMAPi | MF_00289_B, Proteasome_A_B, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR023332, Proteasome_alpha-type IPR022296, Proteasome_asu_bac IPR001353, Proteasome_sua/b |
PANTHERi | PTHR11599:SF69, PTHR11599:SF69, 1 hit |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR03691, 20S_bact_alpha, 1 hit |
PROSITEi | View protein in PROSITE PS51475, PROTEASOME_ALPHA_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
MSFPYFISPE QAMRERSELA RKGIARAKSV VALAYAGGVL FVAENPSRSL
60 70 80 90 100
QKISELYDRV GFAAAGKFNE FDNLRRGGIQ FADTRGYAYD RRDVTGRQLA
110 120 130 140 150
NVYAQTLGTI FTEQAKPYEV ELCVAEVAHY GETKRPELYR ITYDGSIADE
160 170 180 190 200
PHFVVMGGTT EPIANALKES YAENASLTDA LRIAVAALRA GSADTSGGDQ
210 220 230 240
PTLGVASLEV AVLDANRPRR AFRRITGSAL QALLVDQESP QSDGESSG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44884.1 |
PIRi | H70511 |
RefSeqi | NP_216625.1, NC_000962.3 WP_003906749.1, NZ_NVQJ01000058.1 |
Genome annotation databases
EnsemblBacteriai | CCP44884; CCP44884; Rv2109c |
GeneIDi | 23491703 887538 |
KEGGi | mtu:Rv2109c mtv:RVBD_2109c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44884.1 |
PIRi | H70511 |
RefSeqi | NP_216625.1, NC_000962.3 WP_003906749.1, 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 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 2-248 | [»] | |
2FHH | X-ray | 2.99 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 2-248 | [»] | |
3H6F | X-ray | 2.51 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 1-248 | [»] | |
3H6I | X-ray | 2.43 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 1-248 | [»] | |
3HF9 | X-ray | 2.88 | 1/3/A/B/D/F/I/K/M/O/Q/S/U/W/Y/a/b/d/f/i/k/m/o/q/s/u/w/y | 10-248 | [»] | |
3HFA | X-ray | 2.50 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 10-248 | [»] | |
3KRD | X-ray | 2.50 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 1-248 | [»] | |
3MFE | X-ray | 2.60 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 10-248 | [»] | |
3MI0 | X-ray | 2.20 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 1-248 | [»] | |
3MKA | X-ray | 2.51 | 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y | 1-248 | [»] | |
5LZP | electron microscopy | 3.45 | 0/2/4/6/8/B/D/H/J/M/Q/S/W/Y | 8-248 | [»] | |
5THO | X-ray | 3.00 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
5TRG | X-ray | 2.80 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
5TRR | X-ray | 3.10 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
5TRS | X-ray | 3.08 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
5TRY | X-ray | 3.00 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
5TS0 | X-ray | 2.85 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
6BGL | electron microscopy | 3.40 | A/C/D/E/F/G/H/I/J/K/L/M/N/O | 1-248 | [»] | |
6BGO | electron microscopy | 4.20 | A/C/D/E/F/G/H/I/J/K/L/M/N/O | 1-248 | [»] | |
6OCW | X-ray | 2.60 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
6OCZ | X-ray | 2.65 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
6ODE | X-ray | 2.90 | A/B/C/D/E/F/G/O/P/Q/R/S/T/U | 10-248 | [»] | |
SMRi | P9WHU1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P9WHU1, 1 interactor |
MINTi | P9WHU1 |
STRINGi | 83332.Rv2109c |
Chemistry databases
DrugBanki | DB04732, N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID |
PTM databases
iPTMneti | P9WHU1 |
Proteomic databases
PaxDbi | P9WHU1 |
Genome annotation databases
EnsemblBacteriai | CCP44884; CCP44884; Rv2109c |
GeneIDi | 23491703 887538 |
KEGGi | mtu:Rv2109c mtv:RVBD_2109c |
Organism-specific databases
TubercuListi | Rv2109c |
Phylogenomic databases
eggNOGi | COG0638, Bacteria |
OMAi | KYNEFEN |
PhylomeDBi | P9WHU1 |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
Family and domain databases
Gene3Di | 3.60.20.10, 1 hit |
HAMAPi | MF_00289_B, Proteasome_A_B, 1 hit |
InterProi | View protein in InterPro IPR029055, Ntn_hydrolases_N IPR023332, Proteasome_alpha-type IPR022296, Proteasome_asu_bac IPR001353, Proteasome_sua/b |
PANTHERi | PTHR11599:SF69, PTHR11599:SF69, 1 hit |
Pfami | View protein in Pfam PF00227, Proteasome, 1 hit |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR03691, 20S_bact_alpha, 1 hit |
PROSITEi | View protein in PROSITE PS51475, PROTEASOME_ALPHA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PSA_MYCTU | |
Accessioni | P9WHU1Primary (citable) accession number: P9WHU1 Secondary accession number(s): L0T8P4, O33244, Q7D7I3 | |
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