Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P9WHU1 (PSA_MYCTU)

Entry version 41 (22 Apr 2020)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Proteasome subunit alpha

Gene

prcA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues (PubMed:16468985). In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice (PubMed:18059281). Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (PubMed:20711362) (By similarity). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis-independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome (PubMed:20711362).UniRule annotationBy similarity4 Publications

Miscellaneous

Was identified as a high-confidence drug target.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. In vitro, chymotryptic and tryptic activities of the proteasome are both completely inhibited by epoxomicin and by the peptidyl boronate inhibitor MLN-273. Also inhibited by Mg2+, Ca2+ and SDS. It was also shown that certain oxathiazol-2-one compounds can act as selective suicide-substrate inhibitors of the M.tuberculosis proteasome by irreversibly cyclocarbonylating its active site threonine. Proteasome activity is potently inhibited by fellutamide B (Ki=6.8 nM), a lipopeptide aldehyde that forms a reversible bond with the beta-OH of the active site threonine (PubMed:20558127).UniRule annotation3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=56 µM for succinyl-LLVY-7-amino-4-methylcoumarin1 Publication
  1. Vmax=0.24 nmol/min/mg enzyme with succinyl-LLVY-7-amino-4-methylcoumarin as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: proteasomal Pup-dependent pathway

This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processVirulence

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MTBH37RV:G185E-6315-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00997

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proteasome subunit alphaUniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome alpha subunitUniRule annotation
Proteasome core protein PrcAUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:prcAUniRule annotation
Ordered Locus Names:Rv2109c
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...TubercuListi		Rv2109c

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm, Proteasome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

In the course of search for new antibiotics, a class of oxathiazol-2-one compounds has been identified that selectively inhibits the M.tuberculosis proteasome over the human proteasome and that kills non-replicating M.tuberculosis.1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking the core proteasome prcBA subunits exhibit reduced growth and persistence in mice. They are also attenuated in interferon-gamma-deficient mice. They also display increased sensitivity to reactive nitrogen intermediates (RNI) and increased resistance to oxidative stress.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 8Missing : Markedly increases peptidolytic activity. Disappearance of the apparent obstruction in alpha rings. Designated open-gate mutant. 1 Publication8

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04732 N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003834822 – 248Proteasome subunit alphaAdd BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine; partialCombined sources1 Publication1
Modified residuei84Phosphothreonine1 Publication1
Modified residuei178Phosphothreonine1 Publication1
Modified residuei202Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by the PknB kinase at three threonine residues (Thr-84, Thr-202, and Thr-178) in a sequential manner. Phosphorylation enhances proteolytic activity of the proteasome.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P9WHU1

PRoteomics IDEntifications database

More...PRIDEi		P9WHU1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P9WHU1

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P9WHU1, 1 interactor

Molecular INTeraction database

More...MINTi		P9WHU1

STRING: functional protein association networks

More...STRINGi		83332.Rv2109c

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P9WHU1

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase T1A family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105F7N Bacteria
COG0638 LUCA

KEGG Orthology (KO)

More...KOi		K03432

Identification of Orthologs from Complete Genome Data

More...OMAi		KYNEFEN

Database for complete collections of gene phylogenies

More...PhylomeDBi		P9WHU1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.20.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00289_B Proteasome_A_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR022296 Proteasome_asu_bac
IPR001353 Proteasome_sua/b

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF69 PTHR11599:SF69, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00227 Proteasome, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56235 SSF56235, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03691 20S_bact_alpha, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51475 PROTEASOME_ALPHA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P9WHU1-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:248
Mass (Da):26,881
Last modified:April 16, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0356FED74869998A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP44884.1

Protein sequence database of the Protein Information Resource

More...PIRi		H70511

NCBI Reference Sequences

More...RefSeqi		NP_216625.1, NC_000962.3
WP_003906749.1, NZ_NVQJ01000058.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CCP44884; CCP44884; Rv2109c

Database of genes from NCBI RefSeq genomes

More...GeneIDi		887538

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mtu:Rv2109c
mtv:RVBD_2109c

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP44884.1
PIRiH70511
RefSeqiNP_216625.1, NC_000962.3
WP_003906749.1, NZ_NVQJ01000058.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FHGX-ray3.231/A/B/D/F/I/K/M/O/Q/S/U/W/Y2-248[»]
2FHHX-ray2.991/A/B/D/F/I/K/M/O/Q/S/U/W/Y2-248[»]
3H6FX-ray2.511/A/B/D/F/I/K/M/O/Q/S/U/W/Y1-248[»]
3H6IX-ray2.431/A/B/D/F/I/K/M/O/Q/S/U/W/Y1-248[»]
3HF9X-ray2.881/3/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/y10-248[»]
3HFAX-ray2.501/A/B/D/F/I/K/M/O/Q/S/U/W/Y10-248[»]
3KRDX-ray2.501/A/B/D/F/I/K/M/O/Q/S/U/W/Y1-248[»]
3MFEX-ray2.601/A/B/D/F/I/K/M/O/Q/S/U/W/Y10-248[»]
3MI0X-ray2.201/A/B/D/F/I/K/M/O/Q/S/U/W/Y1-248[»]
3MKAX-ray2.511/A/B/D/F/I/K/M/O/Q/S/U/W/Y1-248[»]
5LZPelectron microscopy3.450/2/4/6/8/B/D/H/J/M/Q/S/W/Y8-248[»]
5THOX-ray3.00A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
5TRGX-ray2.80A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
5TRRX-ray3.10A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
5TRSX-ray3.08A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
5TRYX-ray3.00A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
5TS0X-ray2.85A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
6BGLelectron microscopy3.40A/C/D/E/F/G/H/I/J/K/L/M/N/O1-248[»]
6BGOelectron microscopy4.20A/C/D/E/F/G/H/I/J/K/L/M/N/O1-248[»]
6OCWX-ray2.60A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
6OCZX-ray2.65A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
6ODEX-ray2.90A/B/C/D/E/F/G/O/P/Q/R/S/T/U10-248[»]
SMRiP9WHU1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP9WHU1, 1 interactor
MINTiP9WHU1
STRINGi83332.Rv2109c

Chemistry databases

DrugBankiDB04732 N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID

PTM databases

iPTMnetiP9WHU1

Proteomic databases

PaxDbiP9WHU1
PRIDEiP9WHU1

Genome annotation databases

EnsemblBacteriaiCCP44884; CCP44884; Rv2109c
GeneIDi887538
KEGGimtu:Rv2109c
mtv:RVBD_2109c

Organism-specific databases

TubercuListiRv2109c

Phylogenomic databases

eggNOGiENOG4105F7N Bacteria
COG0638 LUCA
KOiK03432
OMAiKYNEFEN
PhylomeDBiP9WHU1

Enzyme and pathway databases

UniPathwayiUPA00997
BioCyciMTBH37RV:G185E-6315-MONOMER

Family and domain databases

Gene3Di3.60.20.10, 1 hit
HAMAPiMF_00289_B Proteasome_A_B, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR022296 Proteasome_asu_bac
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF69 PTHR11599:SF69, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR03691 20S_bact_alpha, 1 hit
PROSITEiView protein in PROSITE
PS51475 PROTEASOME_ALPHA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPSA_MYCTU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P9WHU1
Secondary accession number(s): L0T8P4, O33244, Q7D7I3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: April 22, 2020
This is version 41 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again