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UniProtKB - P9WGK3 (DEVS_MYCTU)

Entry version 39 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Oxygen sensor histidine kinase response regulator DevS/DosS

Gene

devS

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

Member of the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response (PubMed:12953092). Regulates an approximately 48-member regulon (PubMed:12953092, PubMed:11416222, PubMed:15033981, PubMed:18400743). Required for full induction of the DevR (DosR) regulon; acts later than DosT to positively regulate expression of the DevR regulon during adaptation to anaerobiosis (PubMed:19487478). Characterized as an oxygen sensor; O2 acts as a switch, with O2-bound Fe2+ protein inactive in autophosphorylation (PubMed:17371046, PubMed:17600145, PubMed:18975917, PubMed:19463006, PubMed:28977726). Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor (PubMed:17609369). Autophosphorylates under anaerobic but not aerobic conditions, binding of NO or CO does not dramatically change the level of autophosphorylation of Fe2+ protein, binding of O2 inactivates kinase activity (PubMed:17600145, PubMed:18975917, PubMed:27235395). Binds O2, NO, CO (PubMed:17371046, PubMed:17609369, PubMed:17600145, PubMed:18975917, PubMed:27235395). It is probably reduced by flavin nucleotides such as FMN and FAD (PubMed:19276084). May be the primary sensor for CO (PubMed:18400743). Donates a phosphate group to transcriptional regulator DevR (DosR) (PubMed:15033981, PubMed:15073296, PubMed:28977726).14 Publications

Miscellaneous

Was identified as a high-confidence drug target.1 Publication
A tyrosine residue (Tyr-171) is required for discrimination between bound gaseous ligands (PubMed:18975917). The Tyr is part of a probable hydrogen bonding network which includes Glu-87, His-89 and Arg-204 that is probably also important for signaling to the kinase domain (PubMed:19276084, PubMed:27235395).2 Publications1 Publication
The dev nomenclature derives from the increased expression (differentially expressed in virulent strain, dev) of these genes in virulent H37Rv versus avirulent H37Ra. The dos nomenclature derives from experiments in M.bovis showing the same genes are essential for dormancy survival.1 Publication

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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=73 µM for ATP for autophosphorylation by deoxy-DevS1 Publication

    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 bindingi149Iron (heme axial ligand); via tele nitrogen3 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

    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 functionKinase, Transferase
    Biological processTwo-component regulatory system
    LigandATP-binding, Heme, Iron, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MTBH37RV:G185E-7396-MONOMER

    <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:
    Oxygen sensor histidine kinase response regulator DevS/DosS1 Publication (EC:2.7.13.31 Publication)
    <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:devS1 Publication
    Synonyms:dosS
    Ordered Locus Names:Rv3132c
    <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 lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium 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    		Rv3132c

    <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

    <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 show no changes in gene induction following hypoxia, or exposure to NO or CO (PubMed:11416222, PubMed:15033981, PubMed:18474359). Another publication shows a severely attenuated response to CO (PubMed:18400743). Cells lacking both this gene and DosT have no response to hypoxia, or exposure to NO or CO showing both proteins are required for the hypoxic, NO and CO responses (PubMed:15033981). 95% decreased induction of the DevR (DosR) regulon during anaerobic growth, 50% decreased induction of the DevR regulon upon exposure to NO during aerobic growth (PubMed:19487478).5 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>Mutagenesisi87E → A: No change in autophosphorylation when NO-bound, decreased autophosphorylation in deoxy or CO-bound state, slightly increased activity in O(2)-bound state. 1 Publication1
    Mutagenesisi87E → D: No change in autophosphorylation when NO-bound, loss of autophosphorylation in deoxy or CO-bound state. 1 Publication1
    Mutagenesisi87E → G: No change in autophosphorylation when deoxy or NO-bound, decreased autophosphorylation when CO-bound, increased activity in O(2)-bound state. 1 Publication1
    Mutagenesisi89H → A: No autophosphorylation activity no matter the bound gaseous ligand, protein more easily oxidized to Fe(3+) state. 1 Publication1
    Mutagenesisi89H → R: Decreased autophosphorylation when CO- or NO-bound, none in the deoxy or O(2)-bound state, protein more easily oxidized to Fe(3+) state. 1 Publication1
    Mutagenesisi139H → A: No change in heme binding. 1 Publication1
    Mutagenesisi149H → A: Weaker than wild-type heme binding. 2 Publications1
    Mutagenesisi171Y → F: No autophosphorylation when Fe(2+) protein is bound to CO or NO; no change in autophosphorylation of deoxy-protein. No change in auto-oxidation, slightly higher affinity for O(2) and CO. 2 Publications1
    Mutagenesisi204R → A: No autophosphorylation activity no matter the bound gaseous ligand. 1 Publication1
    Mutagenesisi395 – 397HDH → KDK: No autophosphorylation, no transfer to DevR (DosR). 1 Publication3
    Mutagenesisi395H → Q: No autophosphorylation. Isolated kinase core binds ATP. 2 Publications1
    Mutagenesisi397H → A or Q: No change in phosphorylation. 1 Publication1
    Mutagenesisi440R → C: Can form a disulfide bond; when associated with C-537. Loss of autophosphorylation; when associated with C-524 or C-524 and C-537. 1 Publication1
    Mutagenesisi503N → D: No autophosphorylation. 1 Publication1
    Mutagenesisi524C → S: Isolated kinase core no longer forms dimers, autophosphorylation unaffected. Decreased autophosphorylation; when associated with C-537. Loss of autophosphorylation; when associated with C-440 or C-440 and C-537. 1 Publication1
    Mutagenesisi537E → C: Can form a disulfide bond; when associated with C-440. Decreased autophosphorylation; when associated with C-524. Loss of autophosphorylation; when associated with C-440 or C-440 and C-524. 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 <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 methionineiRemovedCombined sources
    <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_00003926232 – 578Oxygen sensor histidine kinase response regulator DevS/DosSAdd BLAST577

    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-acetylthreonineCombined sources1
    Modified residuei395Phosphohistidine; by autocatalysis2 Publications1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

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

    More...    PaxDbi    		P9WGK3

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P9WGK3

    <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

    A member of the dormancy regulon, expression is controlled by devR (PubMed:12953092, PubMed:19487478). Induced in response to reduced oxygen tension (hypoxia) (PubMed:11416222, PubMed:12953092, PubMed:19487478). Induced in response to low levels of nitric oxide (NO) and carbon monoxide (CO) (PubMed:12953092, PubMed:18400743). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. Member of the Rv3134c-devR-devS operon (PubMed:10970762).5 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

    The isolated histidine kinase core (HKC, residues 386-578) is a dimer and autophosphorylates, suggesting the protein may function as a homodimer (PubMed:23486471).

    1 Publication

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...    IntActi    		P9WGK3, 1 interactor

    STRING: functional protein association networks

    More...    STRINGi    		83332.Rv3132c

    <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

    1578
    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    		P9WGK3

    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>Domaini63 – 200GAF 1Add BLAST138
    Domaini231 – 369GAF 2Add BLAST139
    Domaini383 – 578Histidine kinasePROSITE-ProRule annotationAdd BLAST196

    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>Regioni386 – 452Histidine acceptor domain1 PublicationAdd BLAST67
    Regioni454 – 578ATP-binding domain1 PublicationAdd BLAST125

    <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

    The first GAF domain protects the heme moiety from auto-oxidation, contributing to the full-length protein's very long half-life (more than 36 hours in buffers without transition metals) (PubMed:19463006). The isolated ATP-binding subdomain (residues 454-578) crystallized in a closed form that is unable to bind ATP, suggesting that ATP-binding requires conformational changes in this loop region; in this closed conformation it binds a zinc atom (PubMed:23486471). The isolated histidine kinase core (HKC, residues 386-578) both autophosphorylates and phosphorylates the isolated histidine acceptor subdomain (residues 386-452) (PubMed:23486471). The relative arrangements of the 2 subdomains of the HKC may control not only kinase activity but exposure of the ATP binding site (PubMed:23486471).2 Publications

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4107EFD Bacteria
    COG2203 LUCA
    COG4585 LUCA

    KEGG Orthology (KO)

    More...    KOi    		K07682

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		WIDGSVA

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P9WGK3

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.30.450.40, 2 hits
    3.30.565.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003018 GAF
    IPR029016 GAF-like_dom_sf
    IPR003594 HATPase_C
    IPR036890 HATPase_C_sf
    IPR005467 His_kinase_dom
    IPR011712 Sig_transdc_His_kin_sub3_dim/P

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF13185 GAF_2, 2 hits
    PF02518 HATPase_c, 1 hit
    PF07730 HisKA_3, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00065 GAF, 2 hits
    SM00387 HATPase_c, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF55874 SSF55874, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50109 HIS_KIN, 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.

    P9WGK3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTTGGLVDEN DGAAMRPLRH TLSQLRLHEL LVEVQDRVEQ IVEGRDRLDG 
            60         70         80         90        100
    LVEAMLVVTA GLDLEATLRA IVHSATSLVD ARYGAMEVHD RQHRVLHFVY 
           110        120        130        140        150
    EGIDEETVRR IGHLPKGLGV IGLLIEDPKP LRLDDVSAHP ASIGFPPYHP 
           160        170        180        190        200
    PMRTFLGVPV RVRDESFGTL YLTDKTNGQP FSDDDEVLVQ ALAAAAGIAV 
           210        220        230        240        250
    ANARLYQQAK ARQSWIEATR DIATELLSGT EPATVFRLVA AEALKLTAAD 
           260        270        280        290        300
    AALVAVPVDE DMPAADVGEL LVIETVGSAV ASIVGRTIPV AGAVLREVFV 
           310        320        330        340        350
    NGIPRRVDRV DLEGLDELAD AGPALLLPLR ARGTVAGVVV VLSQGGPGAF 
           360        370        380        390        400
    TDEQLEMMAA FADQAALAWQ LATSQRRMRE LDVLTDRDRI ARDLHDHVIQ 
           410        420        430        440        450
    RLFAIGLALQ GAVPHERNPE VQQRLSDVVD DLQDVIQEIR TTIYDLHGAS 
           460        470        480        490        500
    QGITRLRQRI DAAVAQFADS GLRTSVQFVG PLSVVDSALA DQAEAVVREA 
           510        520        530        540        550
    VSNAVRHAKA STLTVRVKVD DDLCIEVTDN GRGLPDEFTG SGLTNLRQRA 
           560        570 
    EQAGGEFTLA SVPGASGTVL RWSAPLSQ
    Length:578
    Mass (Da):62,241
    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:i4C04B836791B9B32
    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: CCP45942.1
    U22037 Genomic DNA Translation: AAD17453.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		E70645

    NCBI Reference Sequences

    More...    RefSeqi    		NP_217648.1, NC_000962.3
    WP_003899933.1, NZ_NVQJ01000019.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		CCP45942; CCP45942; Rv3132c

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		888829

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mtu:Rv3132c
    mtv:RVBD_3132c

    <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: CCP45942.1
    U22037 Genomic DNA Translation: AAD17453.1
    PIRiE70645
    RefSeqiNP_217648.1, NC_000962.3
    WP_003899933.1, NZ_NVQJ01000019.1

    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
    2W3DX-ray2.00A/B63-210[»]
    2W3EX-ray1.60A/B63-210[»]
    2W3FX-ray1.60A/B63-210[»]
    2W3GX-ray1.40A/B63-210[»]
    2W3HX-ray1.80A/B63-210[»]
    2Y79X-ray1.80A/B63-210[»]
    2Y8HX-ray1.90A/B63-210[»]
    3ZXOX-ray1.90A/B454-578[»]
    4YNRX-ray1.92A/B63-210[»]
    4YOFX-ray1.90A/B63-210[»]
    SMRiP9WGK3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP9WGK3, 1 interactor
    STRINGi83332.Rv3132c

    PTM databases

    iPTMnetiP9WGK3

    Proteomic databases

    PaxDbiP9WGK3

    Genome annotation databases

    EnsemblBacteriaiCCP45942; CCP45942; Rv3132c
    GeneIDi888829
    KEGGimtu:Rv3132c
    mtv:RVBD_3132c

    Organism-specific databases

    TubercuListiRv3132c

    Phylogenomic databases

    eggNOGiENOG4107EFD Bacteria
    COG2203 LUCA
    COG4585 LUCA
    KOiK07682
    OMAiWIDGSVA
    PhylomeDBiP9WGK3

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-7396-MONOMER

    Family and domain databases

    Gene3Di3.30.450.40, 2 hits
    3.30.565.10, 1 hit
    InterProiView protein in InterPro
    IPR003018 GAF
    IPR029016 GAF-like_dom_sf
    IPR003594 HATPase_C
    IPR036890 HATPase_C_sf
    IPR005467 His_kinase_dom
    IPR011712 Sig_transdc_His_kin_sub3_dim/P
    PfamiView protein in Pfam
    PF13185 GAF_2, 2 hits
    PF02518 HATPase_c, 1 hit
    PF07730 HisKA_3, 1 hit
    SMARTiView protein in SMART
    SM00065 GAF, 2 hits
    SM00387 HATPase_c, 1 hit
    SUPFAMiSSF55874 SSF55874, 1 hit
    PROSITEiView protein in PROSITE
    PS50109 HIS_KIN, 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 nameiDEVS_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: P9WGK3
    Secondary accession number(s): L0TBM4
    , P95194, Q79CX7, Q7D626
    <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: October 16, 2019
    This is version 39 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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