Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 27 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Pup--protein ligase

Gene

pafA

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

Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.4 Publications

Miscellaneous

The reaction mechanism probably proceeds via the activation of Pup by phosphorylation of its C-terminal glutamate, which is then subject to nucleophilic attack by the substrate lysine, resulting in an isopeptide bond and the release of phosphate as a good leaving group.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_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.
View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.

Pathwayi: protein pupylation

This protein is involved in the pathway protein pupylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein pupylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi9MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei53ATPBy similarity1
Metal bindingi55MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei57Proton acceptorBy similarity1
Metal bindingi63MagnesiumBy similarity1
Binding sitei66ATP; via carbonyl oxygenBy similarity1
Binding sitei419ATPBy similarity1

<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 functionLigase
Biological processUbl conjugation pathway, Virulence
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G185E-6303-MONOMER
MTBH37RV:G185E-6303-MONOMER

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

More...
UniPathwayi
UPA00997
UPA00998

<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:
Pup--protein ligase (EC:6.3.1.192 Publications)
Alternative name(s):
Proteasome accessory factor A
Pup-conjugating enzyme
<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:pafA
Synonyms:paf
Ordered Locus Names:Rv2097c
ORF Names:MTCY49.37c
<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
Rv2097c

<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

<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 have no detectable pupylated proteins and substrate proteins accumulate. These cells also become hypersensitive to reactive nitrogen intermediates (RNI) and fail to grow in both wild-type and nitric oxide synthase 2 deficient macrophages. 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>Mutagenesisi9E → A: Abolishes pupylation. 1 Publication1
Mutagenesisi11E → A: Abolishes pupylation. 1 Publication1
Mutagenesisi53R → E: Abolishes pupylation. 1 Publication1
Mutagenesisi55Y → K: Abolishes pupylation. 1 Publication1
Mutagenesisi57D → N: Abolishes pupylation. 1 Publication1
Mutagenesisi63E → A: Abolishes pupylation. 1 Publication1
Mutagenesisi123H → A: Abolishes pupylation. 1 Publication1
Mutagenesisi171R → A: Abolishes pupylation. 1 Publication1
Mutagenesisi187R → A: Abolishes pupylation. 1 Publication1
Mutagenesisi207H → E: Abolishes pupylation. 1 Publication1

<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_00001039661 – 452Pup--protein ligaseAdd BLAST452

Proteomic databases

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

More...
PaxDbi
P9WNU7

PRoteomics IDEntifications database

More...
PRIDEi
P9WNU7

<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

Interacts with the prokaryotic ubiquitin-like protein Pup.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2097c

<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

3D structure databases

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

More...
SMRi
P9WNU7

Database of comparative protein structure models

More...
ModBasei
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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DVV Bacteria
ENOG410XPTE LUCA

KEGG Orthology (KO)

More...
KOi
K13571

Identification of Orthologs from Complete Genome Data

More...
OMAi
CVSQRAE

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WNU7

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_02111 Pup_ligase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022279 Pup_ligase
IPR004347 Pup_ligase/deamidase

The PANTHER Classification System

More...
PANTHERi
PTHR42307 PTHR42307, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03136 Pup_ligase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF018077 UCP018077, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03686 pupylate_PafA, 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.

P9WNU7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRRIMGIET EFGVTCTFHG HRRLSPDEVA RYLFRRVVSW GRSSNVFLRN
60 70 80 90 100
GARLYLDVGS HPEYATAECD SLVQLVTHDR AGEWVLEDLL VDAEQRLADE
110 120 130 140 150
GIGGDIYLFK NNTDSAGNSY GCHENYLIVR AGEFSRISDV LLPFLVTRQL
160 170 180 190 200
ICGAGKVLQT PKAATYCLSQ RAEHIWEGVS SATTRSRPII NTRDEPHADA
210 220 230 240 250
EKYRRLHVIV GDSNMSETTT MLKVGTAALV LEMIESGVAF RDFSLDNPIR
260 270 280 290 300
AIREVSHDVT GRRPVRLAGG RQASALDIQR EYYTRAVEHL QTREPNAQIE
310 320 330 340 350
QVVDLWGRQL DAVESQDFAK VDTEIDWVIK RKLFQRYQDR YDMELSHPKI
360 370 380 390 400
AQLDLAYHDI KRGRGIFDLL QRKGLAARVT TDEEIAEAVD QPPQTTRARL
410 420 430 440 450
RGEFISAAQE AGRDFTVDWV HLKLNDQAQR TVLCKDPFRA VDERVKRLIA

SM
Length:452
Mass (Da):51,384
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:i12AF8B7872D2F5EA
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
DQ990836 Genomic DNA Translation: ABJ90140.1
AL123456 Genomic DNA Translation: CCP44872.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D70768

NCBI Reference Sequences

More...
RefSeqi
NP_216613.1, NC_000962.3
WP_003410781.1, NZ_NVQJ01000061.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP44872; CCP44872; Rv2097c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
888460

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2097c
mtv:RVBD_2097c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.111.peg.2337

<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
DQ990836 Genomic DNA Translation: ABJ90140.1
AL123456 Genomic DNA Translation: CCP44872.1
PIRiD70768
RefSeqiNP_216613.1, NC_000962.3
WP_003410781.1, NZ_NVQJ01000061.1

3D structure databases

SMRiP9WNU7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2097c

Proteomic databases

PaxDbiP9WNU7
PRIDEiP9WNU7

Genome annotation databases

EnsemblBacteriaiCCP44872; CCP44872; Rv2097c
GeneIDi888460
KEGGimtu:Rv2097c
mtv:RVBD_2097c
PATRICifig|83332.111.peg.2337

Organism-specific databases

TubercuListiRv2097c

Phylogenomic databases

eggNOGiENOG4105DVV Bacteria
ENOG410XPTE LUCA
KOiK13571
OMAiCVSQRAE
PhylomeDBiP9WNU7

Enzyme and pathway databases

UniPathwayiUPA00997
UPA00998
BioCyciMetaCyc:G185E-6303-MONOMER
MTBH37RV:G185E-6303-MONOMER

Family and domain databases

HAMAPiMF_02111 Pup_ligase, 1 hit
InterProiView protein in InterPro
IPR022279 Pup_ligase
IPR004347 Pup_ligase/deamidase
PANTHERiPTHR42307 PTHR42307, 1 hit
PfamiView protein in Pfam
PF03136 Pup_ligase, 1 hit
PIRSFiPIRSF018077 UCP018077, 1 hit
TIGRFAMsiTIGR03686 pupylate_PafA, 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 nameiPAFA_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: P9WNU7
Secondary accession number(s): A0A111
, L0T8N5, P64943, Q10706
<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 27 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

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
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