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Entry version 35 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Proteasome-associated ATPase

Gene

mpa

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

ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Is required but not sufficient to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.UniRule annotation5 Publications

Miscellaneous

Was identified as a natural substrate of the M.tuberculosis proteasome.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

ATPase activity is inhibited by EDTA, N-ethylmaleimide (NEM) and sodium azide.1 Publication

<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=330 µM for ATP1 Publication
  1. Vmax=62 pmol/min/µg enzyme1 Publication

pH dependencei

Optimum pH is 7.4-7.5.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi296 – 301ATPUniRule annotation6

<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

GO - Biological processi

<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 functionChaperone
Biological processVirulence
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-6321-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_and_taxonomy_section">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-associated ATPaseUniRule annotation
Alternative name(s):
AAA ATPase forming ring-shaped complexesUniRule annotation
Short name:
ARCUniRule annotation
Mycobacterial proteasome ATPaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:mpaUniRule annotation
Ordered Locus Names:Rv2115c
ORF Names:MTCY261.11c
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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
Rv2115c

<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

Keywords - Cellular componenti

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 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 this gene accumulate pupylated proteins. These cells also become hypersensitive to reactive nitrogen intermediates (RNI) and are severely attenuated in both wild-type and nitric oxide synthase 2 deficient mice. Moreover, they display increased resistance to hydrogen peroxide.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi120R → A: Does not dramatically affect proteasome substrate degradation. 1 Publication1
Mutagenesisi173R → E: Impairs Mpa hexamerization; when associated with A-187 and E-235. 1 Publication1
Mutagenesisi187W → A: Impairs Mpa hexamerization; when associated with E-173 and E-235. 1 Publication1
Mutagenesisi225K → A: Does not dramatically affect proteasome substrate degradation. 1 Publication1
Mutagenesisi235K → E: Impairs Mpa hexamerization; when associated with E-173 and A-187. 1 Publication1
Mutagenesisi299K → Q: Reduces both ATPase activity and ATP affinity. Abolishes proteasome substrate degradation and protection against RNI. 2 Publications1
Mutagenesisi341F → A: Abolishes unfolding capacity. 1 Publication1
Mutagenesisi341F → Y: No effect on unfolding capacity. 1 Publication1
Mutagenesisi342V → A: Abolishes proteasome substrate degradation. 1 Publication1
Mutagenesisi371D → A: Severely reduces ATPase activity. Abolishes proteasome substrate degradation and protection against RNI. 2 Publications1
Mutagenesisi372E → A: Severely reduces ATPase activity. Abolishes protection against RNI. 1 Publication1
Mutagenesisi372E → Q: Abolishes protection against RNI. 1 Publication1
Mutagenesisi608 – 609Missing : Retains ATPase and unfolding activities, yet abolishes proteasome substrate degradation and protection against RNI. Is also highly attenuated in mice. 3 Publications2
Mutagenesisi608Y → E or F: Abolishes proteasome substrate degradation and protection against RNI. 2 Publications1

<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 ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000847781 – 609Proteasome-associated ATPaseAdd BLAST609

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki591Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Pupylated at Lys-591 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome. Mpa thus promotes its own turnover.1 Publication
Mpa is a target of RNI, thereby is S-nitrosylated in the phagosome of immunologically activated host macrophages, which causes enzyme inhibition.1 Publication

Keywords - PTMi

Isopeptide bond, S-nitrosylation, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P9WQN5

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. Assembles into a hexameric ring structure that caps the 20S proteasome core. Strongly interacts with the prokaryotic ubiquitin-like protein Pup through a hydrophobic interface; the interacting region of Mpa lies in its N-terminal coiled-coil domain. There is one Pup binding site per Mpa hexamer ring; the K(D) measured is about 3.8 µM. Upon ATP-binding, the C-terminus of Mpa interacts with the alpha-rings of the proteasome core, possibly by binding to the intersubunit pockets.

UniRule annotation7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P9WQN5, 1 interactor

Molecular INTeraction database

More...
MINTi
P9WQN5

STRING: functional protein association networks

More...
STRINGi
83332.Rv2115c

<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

1609
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
P9WQN5

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni608 – 609Docks into pockets in the proteasome alpha-ringUniRule annotation2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili20 – 96UniRule annotationAdd BLAST77

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of three main regions, an N-terminal coiled-coil domain (residues 1-96) that binds to protein Pup and functions as a docking station, an interdomain (residues 97-245) involved in Mpa hexamerization, and a C-terminal ATPase domain of the AAA type (residues 246-609).3 Publications

<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 AAA ATPase family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DHM Bacteria
COG0464 LUCA

KEGG Orthology (KO)

More...
KOi
K13527

Identification of Orthologs from Complete Genome Data

More...
OMAi
CVDEFKE

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WQN5

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_02112 ARC_ATPase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase
IPR032501 Prot_ATP_ID_OB
IPR041626 Prot_ATP_OB_N
IPR022482 Proteasome_ATPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF16450 Prot_ATP_ID_OB, 1 hit
PF17758 Prot_ATP_OB_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03689 pup_AAA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00674 AAA, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P9WQN5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT
60 70 80 90 100
RSARDIHQLE ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG
110 120 130 140 150
YGVLLATHDD DTVDVFTSGR KMRLTCSPNI DAASLKKGQT VRLNEALTVV
160 170 180 190 200
EAGTFEAVGE ISTLREILAD GHRALVVGHA DEERVVWLAD PLIAEDLPDG
210 220 230 240 250
LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED LVLEEVPDVS
260 270 280 290 300
YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT
310 320 330 340 350
LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR
360 370 380 390 400
LIFQRAREKA SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI
410 420 430 440 450
DGVEGLENVI VIGASNREDM IDPAILRPGR LDVKIKIERP DAEAAQDIYS
460 470 480 490 500
KYLTEFLPVH ADDLAEFDGD RSACIKAMIE KVVDRMYAEI DDNRFLEVTY
510 520 530 540 550
ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP GLRIQHLLDS
560 570 580 590 600
IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID

TESNLGQYL
Length:609
Mass (Da):67,401
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:i4D5F4E630614C58D
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
DQ888314 Genomic DNA Translation: ABI36485.1
AL123456 Genomic DNA Translation: CCP44890.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F70512

NCBI Reference Sequences

More...
RefSeqi
NP_216631.1, NC_000962.3
WP_003411035.1, NZ_NVQJ01000058.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44890; CCP44890; Rv2115c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
887297

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2115c
mtv:RVBD_2115c

<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
DQ888314 Genomic DNA Translation: ABI36485.1
AL123456 Genomic DNA Translation: CCP44890.1
PIRiF70512
RefSeqiNP_216631.1, NC_000962.3
WP_003411035.1, 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
3FP9X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L98-245[»]
3M91X-ray1.80A/C46-96[»]
3M9BX-ray3.94A/B/C/D/E/F/G/H/I/J/K/L1-234[»]
3M9DX-ray4.50A/B/C/D/E/F/J/K/L/M/N/O1-234[»]
3M9HX-ray2.00A/B/C/D/E/F46-96[»]
5KWAX-ray2.90A/B95-602[»]
5KZFX-ray3.49A/B/C/D/E/F/G/H/I/J/K/L98-609[»]
SMRiP9WQN5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP9WQN5, 1 interactor
MINTiP9WQN5
STRINGi83332.Rv2115c

Proteomic databases

PaxDbiP9WQN5

Genome annotation databases

EnsemblBacteriaiCCP44890; CCP44890; Rv2115c
GeneIDi887297
KEGGimtu:Rv2115c
mtv:RVBD_2115c

Organism-specific databases

TubercuListiRv2115c

Phylogenomic databases

eggNOGiENOG4105DHM Bacteria
COG0464 LUCA
KOiK13527
OMAiCVDEFKE
PhylomeDBiP9WQN5

Enzyme and pathway databases

UniPathwayiUPA00997
BioCyciMTBH37RV:G185E-6321-MONOMER

Family and domain databases

HAMAPiMF_02112 ARC_ATPase, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase
IPR032501 Prot_ATP_ID_OB
IPR041626 Prot_ATP_OB_N
IPR022482 Proteasome_ATPase
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF16450 Prot_ATP_ID_OB, 1 hit
PF17758 Prot_ATP_OB_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR03689 pup_AAA, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 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 nameiARC_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: P9WQN5
Secondary accession number(s): L0T8W3
, O33250, P63345, Q0G9Y7
<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_and_isoforms">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: September 18, 2019
This is version 35 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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