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Entry version 134 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Antitoxin MqsA

Gene

mqsA

Organism
Escherichia coli (strain K12)
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

Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MqsR mRNA interferase toxin and neutralizes its endoribonuclease activity. Overexpression prevents MqsR-mediated cessation of cell growth and inhibition of cell proliferation. Initially reported to act as a cotranscription factor with MqsA (PubMed:19690171, PubMed:20105222). Following further experiments, the MqsR-MqsA complex does not bind DNA and all reported data are actually due to a small fraction of free MqsA alone binding DNA. Addition of MqsR to a preformed MqsA-promoter DNA complex causes dissociation of the MqsA-DNA complex, probably causing derepression of MqsA-repressed transcripts (PubMed:23172222). MqsA binds to 2 palindromes in the promoter region of the mqsRA operon activating its transcription. Binds to other promoters, inducing mcbR and spy and repressing cspD among others (PubMed:20105222). Binds to and represses the rpoS promoter, the master stress regulator, resulting in decreased cyclic-di-GMP, reduced stress resistance, increased cell motility and decreased biofilm formation; in these experiments 5 TA systems are missing (lacks MazEF, RelEB, ChpB, YoeB-YefM, YafQ-DinJ) (PubMed:21516113). An earlier study showed overexpression alone increases biofilm formation, perhaps by repressing cspD; in these experiments the 5 TA systems are present (PubMed:20105222). Represses the csgD promoter. In the presence of stress, when this protein is degraded, the promoters it represses are derepressed, leading to biofilm formation (Probable). This TA system mediates cell growth during bile acid deoxycholate stress by degrading mRNA for probable deoxycholate-binding protein YgiS; bile acid detergents such as deoxycholate are important for host defense against bacterial growth in the gall bladder and duodenum (PubMed:25534751).1 Publication6 Publications

<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

Zn2+4 PublicationsNote: Binds 1 Zn2+ ion per subunit.4 Publications

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

The MqsR-MqsA complex is exceptionally thermostable with a Tm of 83.4 degress Celsius versus 48.1 degress Celsius for MqsR and 61.1 degress Celsius for MqsA.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 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 bindingi3Zinc; structural4 Publications1
Metal bindingi6Zinc; structural4 Publications1
Metal bindingi37Zinc; structural4 Publications1
Metal bindingi40Zinc; structural4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi85 – 104H-T-H motifPROSITE-ProRule annotationAdd BLAST20

<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

  • metal ion binding Source: UniProtKB-KW
  • sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • regulation of transcription, DNA-templated Source: EcoCyc

<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 functionDNA-binding, Repressor
Biological processStress response, Toxin-antitoxin system, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G7571-MONOMER
ECOL316407:JW2989-MONOMER
MetaCyc:G7571-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:
Antitoxin MqsA1 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:mqsA1 Publication
Synonyms:ygiT
Ordered Locus Names:b3021, JW2989
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

<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

Essential for growth, it cannot be disrupted (PubMed:16768798). A double mqsR-mqsA deletion leads to increased rpoS mRNA levels, resulting in increased cyclic-di-GMP levels, increasing stress resistance, increased biofilm formation (PubMed:21516113). The double mutant has increased metabolism and respiration in the presence of the bile acid deoxycholate and consequently grows less well. Decreases cell survival in the presence of 20% deoxycholate (PubMed:25534751).3 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>Mutagenesisi61R → A or D: Decreases DNA-binding, decreases thermostability of MqsR-MqsA complex. 1 Publication1
Mutagenesisi97 – 101NAFSR → AAFSA: Abolishes DNA-binding, including binding to the rpoS promoter. 2 Publications5
Mutagenesisi97N → A: 50-fold reduction in DNA-binding. 1 Publication1
Mutagenesisi101R → A: 10-fold reduction in DNA-binding. 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_00001497621 – 131Antitoxin MqsAAdd BLAST131

<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

Degraded in the presence of oxidative stress, maybe by the Lon and/or ClpX proteases.2 Publications

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q46864

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

More...
PaxDbi
Q46864

PRoteomics IDEntifications database

More...
PRIDEi
Q46864

<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 by amino acid starvation, glucose starvation and when translation is blocked. Induction is decreased in the absence of the Lon protease suggesting, by homology to other toxin-antitoxin systems, that Lon may degrade the MqsA antitoxin. Transcription is activated by MqsA (PubMed:20105222). It has been suggested that MqsA represses its own operon (PubMed:19690171). Not more induced in persister cells (PubMed:16768798). A member of the mqsRA operon. This operon induced by ectopic expression of toxins RelE, HicA and YafQ but not by MazF or HicA (PubMed:23432955).1 Publication4 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. Crystallizes as a heterotetramer with MqsA, MqsR-MqsA2-MqsR (PubMed:20041169). Purifies as a probable heterohexamer of 2 MqsR dimers and 1 MqsA dimer (PubMed:19690171). Binds promoter DNA as a dimer (PubMed:21068382). When the 2 dissociate the MsqR mRNA interferase becomes active.

4 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

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259247, 153 interactors
850181, 51 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1084 MqsRA toxin-antitoxin complex

Database of interacting proteins

More...
DIPi
DIP-12226N

Protein interaction database and analysis system

More...
IntActi
Q46864, 54 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3021

<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

1131
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

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SMRi
Q46864

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q46864

<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>Domaini74 – 127HTH cro/C1-typePROSITE-ProRule annotationAdd BLAST54

<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 Zn-binding N-terminal domain (residues 1-65) binds to the MqsR mRNA interferase toxin and makes contact with the DNA phosphate backbone, while the C-terminus (residues 70-131) binds the promoter in a sequence-specific manner. They are linked by a short flexible domain (PubMed:22789559).3 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105WJ3 Bacteria
COG1396 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000151625

KEGG Orthology (KO)

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KOi
K13655

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00093 HTH_XRE, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.260.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001387 Cro/C1-type_HTH
IPR010982 Lambda_DNA-bd_dom_sf
IPR022452 MqsA
IPR032758 MqsA/HigA-2
IPR022453 Znf_MqsA-type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15731 MqsA_antitoxin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00530 HTH_XRE, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47413 SSF47413, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03830 CxxCG_CxxCG_HTH, 1 hit
TIGR03831 YgiT_finger, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50943 HTH_CROC1, 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.

Q46864-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKCPVCHQGE MVSGIKDIPY TFRGRKTVLK GIHGLYCVHC EESIMNKEES
60 70 80 90 100
DAFMAQVKAF RASVNAETVA PEFIVKVRKK LSLTQKEASE IFGGGVNAFS
110 120 130
RYEKGNAQPH PSTIKLLRVL DKHPELLNEI R
Length:131
Mass (Da):14,703
Last modified:November 1, 1996 - 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:iAA26A2793AD84447
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U28377 Genomic DNA Translation: AAA69189.1
U00096 Genomic DNA Translation: AAC76057.1
AP009048 Genomic DNA Translation: BAE77077.1

Protein sequence database of the Protein Information Resource

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PIRi
C65089

NCBI Reference Sequences

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RefSeqi
NP_417493.1, NC_000913.3
WP_000650107.1, NZ_STEB01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76057; AAC76057; b3021
BAE77077; BAE77077; BAE77077

Database of genes from NCBI RefSeq genomes

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GeneIDi
945814

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2989
eco:b3021

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3709

<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
U28377 Genomic DNA Translation: AAA69189.1
U00096 Genomic DNA Translation: AAC76057.1
AP009048 Genomic DNA Translation: BAE77077.1
PIRiC65089
RefSeqiNP_417493.1, NC_000913.3
WP_000650107.1, NZ_STEB01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ8NMR-A1-131[»]
3FMYX-ray1.40A62-131[»]
3GA8X-ray1.70A1-76[»]
3GN5X-ray2.15A/B1-131[»]
3HI2X-ray2.00A/C1-76[»]
3O9XX-ray2.10A/B1-131[»]
SMRiQ46864
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4259247, 153 interactors
850181, 51 interactors
ComplexPortaliCPX-1084 MqsRA toxin-antitoxin complex
DIPiDIP-12226N
IntActiQ46864, 54 interactors
STRINGi511145.b3021

Proteomic databases

jPOSTiQ46864
PaxDbiQ46864
PRIDEiQ46864

Genome annotation databases

EnsemblBacteriaiAAC76057; AAC76057; b3021
BAE77077; BAE77077; BAE77077
GeneIDi945814
KEGGiecj:JW2989
eco:b3021
PATRICifig|1411691.4.peg.3709

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2840

Phylogenomic databases

eggNOGiENOG4105WJ3 Bacteria
COG1396 LUCA
HOGENOMiHOG000151625
KOiK13655

Enzyme and pathway databases

BioCyciEcoCyc:G7571-MONOMER
ECOL316407:JW2989-MONOMER
MetaCyc:G7571-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ46864

Protein Ontology

More...
PROi
PR:Q46864

Family and domain databases

CDDicd00093 HTH_XRE, 1 hit
Gene3Di1.10.260.40, 1 hit
InterProiView protein in InterPro
IPR001387 Cro/C1-type_HTH
IPR010982 Lambda_DNA-bd_dom_sf
IPR022452 MqsA
IPR032758 MqsA/HigA-2
IPR022453 Znf_MqsA-type
PfamiView protein in Pfam
PF15731 MqsA_antitoxin, 1 hit
SMARTiView protein in SMART
SM00530 HTH_XRE, 1 hit
SUPFAMiSSF47413 SSF47413, 1 hit
TIGRFAMsiTIGR03830 CxxCG_CxxCG_HTH, 1 hit
TIGR03831 YgiT_finger, 1 hit
PROSITEiView protein in PROSITE
PS50943 HTH_CROC1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiMQSA_ECOLI
<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: Q46864
Secondary accession number(s): Q2M9H9
<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: July 15, 1999
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 134 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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