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Entry version 35 (13 Nov 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Alkyl hydroperoxide reductase C

Gene

ahpC

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

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. Does not however seem to play a role in detoxification of isoniazid.3 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide (PubMed:15178486, PubMed:15886207). The disulfide can subsequently be reduced through a mixed disulfide with the C-terminal cysteine of AhpD, resolved by its second cysteine (PubMed:15178486) or by thioredoxin (TrxC) (PubMed:14871480).1 Publication2 Publications

<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 ‘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

kcat is 0.6 sec(-1) with tert-butyl hydroperoxide as substrate and AhpD as reductant and 0.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant.1 Publication
  1. KM=5.38 mM for tert-butyl hydroperoxide1 Publication
  2. KM=0.2 µM for tert-butyl hydroperoxide (using AhpD as electron donor)1 Publication
  3. KM=5.1 µM for tert-butyl hydroperoxide (using thioredoxin TrxC as electron donor)1 Publication
  4. KM=65.7 µM for AhpD (using tert-butyl hydroperoxide as substrate)1 Publication
  5. KM=5.6 µM for TrxC (using tert-butyl hydroperoxide as substrate)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei61Cysteine sulfenic acid (-SOH) intermediate3 Publications1

    <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 functionAntioxidant, Oxidoreductase, Peroxidase
    Biological processStress response

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MTBH37RV:G185E-6659-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1222387 Tolerance of reactive oxygen produced by macrophages
    R-HSA-1222538 Tolerance by Mtb to nitric oxide produced by macrophages
    R-HSA-1222541 Cell redox homeostasis

    <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:
    Alkyl hydroperoxide reductase C (EC:1.11.1.152 Publications)
    Short name:
    MtAhpC
    Alternative name(s):
    Peroxiredoxin
    Thioredoxin peroxidase
    <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:ahpC
    Ordered Locus Names:Rv2428
    <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
    Rv2428

    <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

    • Cytoplasm By similarity

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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

    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>Mutagenesisi61C → A or S: No enzyme activity. 3 Publications1
    Mutagenesisi174 – 176CAC → AAA: 50% reduction in oxidation activity of dithiothreitol and 60% reduction in oxidation of thiocyanate. 1 Publication3
    Mutagenesisi174C → A: Very poor oxidation activity of dithiothreitol and thiocyanate. 3 Publications1
    Mutagenesisi174C → S in reconstituted in vitro system retains no enzyme activity. 3 Publications1
    Mutagenesisi176C → A: 50% reduction in oxidation activity of dithiothreitol and thiocyanate. 3 Publications1
    Mutagenesisi176C → S: Retains about 10% activity with tert-butylhydroperoxide. In reconstituted in vitro system retains 30% enzyme activity. 3 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 <a href="http://www.uniprot.org/help/ptm_processing_section">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 methionineiRemoved1 Publication
    <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_00003929132 – 195Alkyl hydroperoxide reductase CAdd BLAST194

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi61Interchain (with C-133 in AhpD); transient1 Publication
    Disulfide bondi61Interchain (with C-174); in linked formCombined sources3 Publications
    Disulfide bondi174Interchain (with C-61); in linked formCombined sources3 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

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

    More...
    PaxDbi
    P9WQB7

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P9WQB7

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced in isoniazid (INH)-resistant, KatG-deficient strains as well as in INH-sensitive strains when challenged with the drug. Increased expression in these strains probably compensates for loss of katG activity in detoxification of organic peroxides. A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia). It is hoped that this regulon will give insight into the latent, or dormant phase of infection.2 Publications

    <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

    Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer (PubMed:11171096, PubMed:15886207).

    Identified in a complex with AhpD, DlaT and Lpd (PubMed:11799204).

    3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv2428

    <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

    1195
    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
    P9WQB7

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 170ThioredoxinPROSITE-ProRule annotationAdd BLAST167

    <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

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105D3R Bacteria
    COG0450 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K03386

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WYPKDFT

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WQB7

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.30.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000866 AhpC/TSA
    IPR024706 Peroxiredoxin_AhpC-typ
    IPR036249 Thioredoxin-like_sf
    IPR013766 Thioredoxin_domain

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00578 AhpC-TSA, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000239 AHPC, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52833 SSF52833, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51352 THIOREDOXIN_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_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.

    <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 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.

    P9WQB7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPLLTIGDQF PAYQLTALIG GDLSKVDAKQ PGDYFTTITS DEHPGKWRVV
    60 70 80 90 100
    FFWPKDFTFV CPTEIAAFSK LNDEFEDRDA QILGVSIDSE FAHFQWRAQH
    110 120 130 140 150
    NDLKTLPFPM LSDIKRELSQ AAGVLNADGV ADRVTFIVDP NNEIQFVSAT
    160 170 180 190
    AGSVGRNVDE VLRVLDALQS DELCACNWRK GDPTLDAGEL LKASA
    Length:195
    Mass (Da):21,566
    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:i011C1014F07C7095
    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
    U18264 Genomic DNA Translation: AAA79919.1
    U16243 Genomic DNA Translation: AAC43585.1
    AF313459 Genomic DNA Translation: AAG34172.1
    AF313460 Genomic DNA Translation: AAG34173.1
    AF313461 Genomic DNA Translation: AAG34174.1
    AF313462 Genomic DNA Translation: AAG34175.1
    AF313463 Genomic DNA Translation: AAG34176.1
    AL123456 Genomic DNA Translation: CCP45220.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216944.1, NC_000962.3
    WP_003412529.1, NZ_NVQJ01000024.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP45220; CCP45220; Rv2428

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    885717

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv2428
    mtv:RVBD_2428

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|83332.111.peg.2715

    <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
    U18264 Genomic DNA Translation: AAA79919.1
    U16243 Genomic DNA Translation: AAC43585.1
    AF313459 Genomic DNA Translation: AAG34172.1
    AF313460 Genomic DNA Translation: AAG34173.1
    AF313461 Genomic DNA Translation: AAG34174.1
    AF313462 Genomic DNA Translation: AAG34175.1
    AF313463 Genomic DNA Translation: AAG34176.1
    AL123456 Genomic DNA Translation: CCP45220.1
    RefSeqiNP_216944.1, NC_000962.3
    WP_003412529.1, NZ_NVQJ01000024.1

    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
    2BMXX-ray2.40A/B/C1-195[»]
    SMRiP9WQB7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2428

    Proteomic databases

    PaxDbiP9WQB7
    PRIDEiP9WQB7

    Genome annotation databases

    EnsemblBacteriaiCCP45220; CCP45220; Rv2428
    GeneIDi885717
    KEGGimtu:Rv2428
    mtv:RVBD_2428
    PATRICifig|83332.111.peg.2715

    Organism-specific databases

    TubercuListiRv2428

    Phylogenomic databases

    eggNOGiENOG4105D3R Bacteria
    COG0450 LUCA
    KOiK03386
    OMAiWYPKDFT
    PhylomeDBiP9WQB7

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-6659-MONOMER
    ReactomeiR-HSA-1222387 Tolerance of reactive oxygen produced by macrophages
    R-HSA-1222538 Tolerance by Mtb to nitric oxide produced by macrophages
    R-HSA-1222541 Cell redox homeostasis

    Family and domain databases

    Gene3Di3.40.30.10, 1 hit
    InterProiView protein in InterPro
    IPR000866 AhpC/TSA
    IPR024706 Peroxiredoxin_AhpC-typ
    IPR036249 Thioredoxin-like_sf
    IPR013766 Thioredoxin_domain
    PfamiView protein in Pfam
    PF00578 AhpC-TSA, 1 hit
    PIRSFiPIRSF000239 AHPC, 1 hit
    SUPFAMiSSF52833 SSF52833, 1 hit
    PROSITEiView protein in PROSITE
    PS51352 THIOREDOXIN_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 nameiAHPC_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: P9WQB7
    Secondary accession number(s): L0T9L3
    , Q79FE2, Q7BHK8, Q7D758
    <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: November 13, 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, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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