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UniProtKB - P0AE70 (MAZF_ECOLI)

Entry version 120 (02 Jun 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Endoribonuclease toxin MazF

Gene

mazF

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

Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single-strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs (PubMed:18854355).

Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A (PubMed:15537630, PubMed:23280569).

Digests 16S rRNA in vivo 43 nts upstream of the C-terminus; this removes the anti-Shine-Dalgarno sequence forming a mixed population of wild-type and 'stress ribosomes'. Stress ribosomes do not translate leader-containing mRNA but are proficient in translation of leaderless mRNA, which alters the protein expression profile of the cell; MazF produces some leaderless mRNA (PubMed:21944167).

The toxic endoribonuclease activity is inhibited by its labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium overexpression of MazF leads to programmed cell death (PubMed:8650219, PubMed:11222603).

MazF-mediated cell death occurs following a number of stress conditions in a relA-dependent fashion and only when cells are in log phase; sigma factor S (rpoS) protects stationary phase cells from MazF-killing (PubMed:15150257, PubMed:19251848).

Cell growth and viability are not affected when MazF and MazE are coexpressed. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their own transcription. MazE has higher affinity for promoter DNA in the presence of MazF (PubMed:25564525).

Cross-talk can occur between different TA systems, ectopic expression of this toxin induces transcription of the relBEF TA system operon with specific cleavage of the mRNA produced (PubMed:23432955).

11 Publications

Might also serve to protect cells against bacteriophage; in the presence of MazE-MazF fewer P1 phages are produced than in a disrupted strain. For strain K38 most wild-type cells are killed but not by phage lysis; it was suggested that MazE-MazF causes P1 phage exclusion from the bacterial population. This phenomenon is strain dependent.

1 Publication

The physiological role of this TA system is debated. Programmed cell death (PCD) occurs when cells are at high density and depends on the presence of MazE-MazF and a quorum sensing pentapeptide, the extracellular death factor (EDF) with sequence Asn-Asn-Trp-Asn-Asn (NNWNN), probably produced from the zwf gene product glucose-6-phosphate 1-dehydrogenase (PubMed:17962566, PubMed:18310334).

Cell death governed by the MazE-MazF and DinJ-YafQ TA systems seems to play a role in biofilm formation, while MazE-MazF is also implicated in cell death in liquid media (PubMed:19707553).

Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847, PubMed:23416055).

In conjunction with EDF prevents apoptotic-like death (ALD) in the presence of DNA damaging agents, probably by reducing recA mRNA levels in a non-endonuclease-mediated manner (PubMed:22412352).

Other studies (in strains BW25113 and MC4100, the latter makes EDF) demonstrate MazF does not cause PCD but instead bacteriostasis and possibly a dormant state as well as persister cell generation (PubMed:24375411).

9 Publications

Caution

Strain K12 / MG1655 is deficient in both production and response to EDF, unlike strains K12 / MC4100, K12 / W3110 and K12 / K38, all of which make and respond to EDF.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

(Microbial infection) RNA cleavage activity is reduced when ADP-ribosylated.1 Publication
Inhibited by Mg2+ (PubMed:15537630). Stimulated in vitro in a concentration-dependent fashion by EDF, which is able to overcome inhibition by cognate antitoxin MazE (PubMed:21419338). The TA system is antagonized by stress response kinase SrkA, but probably not by phosphorylation of MazF (PubMed:23416055).3 Publications

<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 functionDNA-binding, Endonuclease, Hydrolase, Nuclease, Repressor, RNA-binding
Biological processAntiviral defense, Quorum sensing, Stress response, Toxin-antitoxin system, Transcription, Transcription regulation, Translation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11249-MONOMER
MetaCyc:EG11249-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%5Fand%5Ftaxonomy%5Fsection">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:
Endoribonuclease toxin MazF (EC:3.1.27.-1 Publication)
Alternative name(s):
Toxin MazF
mRNA interferase MazF1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mazF
Synonyms:chpA, chpAK
Ordered Locus Names:b2782, JW2753
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 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

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Can be used to produce large quantities of a single protein if the gene coding for the protein does not contain any ACA codons. Up to 90% of expressed bacterial cellular protein can be the target, which can be produced for up to 4 days. The system also works in eukaryotic cells.1 Publication

<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

Decreased sensitivity to dramatic intracellular increases of ppGpp. Cells missing mazE-mazF survive high temperature, various DNA-damaging agents and H2O2 exposure better than wild-type cells. Cells missing mazE-mazF produce more P1 phage than wild-type cells, while introduction of lysogens into a growing non-lysogenic disruption culture is lethal (PubMed:15316771). Cells missing mazE-mazF show reduced biofilm formation, and survive antibiotic treatment in log phase better than wild-type cells (PubMed:11222603, PubMed:19707553). However lag phase cells disrupted only for mazF had a lower survival rate than wild-type cells (PubMed:24375411). Cells missing mazE-mazF survive hydroxyurea treatment better than wild-type; further disruption of relE-relB and tonB yields even better survival (PubMed:20005847). Cells missing mazE-mazF undergo an apoptotic-like death (ALD) upon DNA damage characterized by membrane depolarization and DNA fragmentation; further disruption of recA prevents membrane depolarization (PubMed:22412352). Unlike the single srkA disruption mutant, a triple srkA-mazE-mazF disruption mutant shows no hyperlethality in the presence of nalidixic acid or UV light, suggesting SrkA has a negative effect on MazF (PubMed:23416055).10 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi17 – 28FDPTK…EQAGH → GGGGGGGGGGG: Changes loop 1 to poly-G; loss of endoribonuclease activity. 1 PublicationAdd BLAST12
Mutagenesisi17 – 28FDPTK…EQAGH → LGPPSGSQPAKR: Changes loop 1 to MazF6 M.tuberculosis sequence; loss of endoribonuclease activity. 1 PublicationAdd BLAST12
Mutagenesisi17 – 28FDPTK…EQAGH → PDDSRGPVPSYS: Changes loop 1 to MazF M.xanthus sequence; loss of endoribonuclease activity. 1 PublicationAdd BLAST12
Mutagenesisi24E → A: Greatly reduces toxicity, about 10-fold less RNA cleavage activity. Expression in the presence of wt MazF has a dominant-negative phenotype, causing cell death as it titrates out the MazE antitoxin; still activates operon transcription. 2 Publications1
Mutagenesisi28H → A: No changes in toxicity. 1 Publication1
Mutagenesisi53 – 61TQSKGYPFE → GGGGGGGG or GGGGGGGGGGG: Changes loop 2 to poly-G; reduces endoribonuclease activity, alters cleavage sites. 1 Publication9
Mutagenesisi53 – 61TQSKGYPFE → SNLHRASEPGN: Changes loop 2 to MazF M.xanthus sequence; reduces endoribonuclease activity, alters cleavage sites. 1 Publication9
Mutagenesisi53 – 61TQSKGYPFE → SNTALAAMPGN: Changes loop 2 to MazF6 M.tuberculosis sequence; reduces endoribonuclease activity, alters cleavage sites. 1 Publication9

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1795096

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002018971 – 111Endoribonuclease toxin MazFAdd BLAST111

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 residuei4ADP-ribosylarginine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

(Microbial infection) ADP-ribosylated by enterobacteria phage T4.1 Publication

Keywords - PTMi

ADP-ribosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AE70

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

More...PaxDbi		P0AE70

PRoteomics IDEntifications database

More...PRIDEi		P0AE70

<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

Expressed in exponentially growing cells. Induction has been reported to occur after amino acid starvation in a ppGpp-independent fashion and to be Lon protease-dependent (PubMed:12972253), but also to not occur after amino acid starvation and to be regulated by ppGpp (PubMed:8650219). Also induced in M9 minimal medium and by chloramphenicol treatment (PubMed:21944167). MazE alone and in combination with MazF, represses transcription of the mazE-mazF operon. Fis activates transcription. Part of the relA-mazE-mazF-mazG operon, there is also a second mazE-mazF specific promoter which is negatively autoregulated (PubMed:2844820, PubMed:8650219). Operon induced by ectopic expression of toxin RelE; operon induction by amino acid starvation requires the relBEF operon (PubMed:23432955).7 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Probably a dimer.

Forms a heterohexamer composed of alternating toxin and antitoxin homodimers MazF2-MazE2-MazF2. The binding site of MazE and ssRNA or ssDNA are largely overlapping; the presence of only 1 MazE molecule inhibits mRNA endoribonuclease activity. Binds to EDF but not a mutated EDF (NNGNN) (PubMed:21419338).

5 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262300, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1086, MazEF toxin-antitoxin complex

Protein interaction database and analysis system

More...IntActi		P0AE70, 2 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2782

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0AE70

<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

1111
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P0AE70

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

More...SMRi		P0AE70

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AE70

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni17 – 28Loop 1, participates in catalytic activity1 PublicationAdd BLAST12
Regioni53 – 61Loop 2, involved in substrate recognition1 Publication9

<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

Loop 1 (residues 17-28) effects catalytic activity while recognition of the ACA cleavage site is influenced by loop 2 (residues 53-61). Alterations of loop 2 generate new cleavage sites in addition to retaining the original cleavage site.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PemK/MazF family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG2337, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_121823_2_3_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AE70

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AE70

Family and domain databases

Database of protein disorder

More...DisProti		DP00299

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.110, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003477, PemK-like
IPR011067, Plasmid_toxin/cell-grow_inhib

The PANTHER Classification System

More...PANTHERi		PTHR33988, PTHR33988, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02452, PemK_toxin, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0AE70-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSRYVPDMG DLIWVDFDPT KGSEQAGHRP AVVLSPFMYN NKTGMCLCVP 
        60         70         80         90        100
CTTQSKGYPF EVVLSGQERD GVALADQVKS IAWRARGATK KGTVAPEELQ 
       110 
LIKAKINVLI G
Length:111
Mass (Da):12,098
Last modified:December 6, 2005 - 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:i1579C867DD6B96AC
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
D16450 Genomic DNA Translation: BAA03918.1
J04039 Unassigned DNA Translation: AAA03239.1
U29580 Genomic DNA Translation: AAA69292.1
U00096 Genomic DNA Translation: AAC75824.1
AP009048 Genomic DNA Translation: BAE76856.1

Protein sequence database of the Protein Information Resource

More...PIRi		B49339

NCBI Reference Sequences

More...RefSeqi		NP_417262.1, NC_000913.3
WP_000254738.1, NZ_STEB01000030.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75824; AAC75824; b2782
BAE76856; BAE76856; BAE76856

Database of genes from NCBI RefSeq genomes

More...GeneIDi		61731222
947252

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2753
eco:b2782

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3953

<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
D16450 Genomic DNA Translation: BAA03918.1
J04039 Unassigned DNA Translation: AAA03239.1
U29580 Genomic DNA Translation: AAA69292.1
U00096 Genomic DNA Translation: AAC75824.1
AP009048 Genomic DNA Translation: BAE76856.1
PIRiB49339
RefSeqiNP_417262.1, NC_000913.3
WP_000254738.1, NZ_STEB01000030.1

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
1UB4X-ray1.70A/B2-111[»]
3NFCX-ray2.00A/B/C/D/E/F1-111[»]
5CK9X-ray1.90A/B1-111[»]
5CKBX-ray2.80A/B1-111[»]
5CKDX-ray1.70A/B1-111[»]
5CKEX-ray2.31A/B1-111[»]
5CKFX-ray2.80A/B1-111[»]
5CKHX-ray2.45A/B1-111[»]
5CO7X-ray3.49A/B/C/D/E/F1-111[»]
5CQXX-ray1.63A/B1-111[»]
5CQYX-ray2.48A/B1-111[»]
5CR2X-ray2.90A/B/C1-111[»]
BMRBiP0AE70
SMRiP0AE70
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262300, 13 interactors
ComplexPortaliCPX-1086, MazEF toxin-antitoxin complex
IntActiP0AE70, 2 interactors
STRINGi511145.b2782

Chemistry databases

BindingDBiP0AE70
ChEMBLiCHEMBL1795096

Proteomic databases

jPOSTiP0AE70
PaxDbiP0AE70
PRIDEiP0AE70

Genome annotation databases

EnsemblBacteriaiAAC75824; AAC75824; b2782
BAE76856; BAE76856; BAE76856
GeneIDi61731222
947252
KEGGiecj:JW2753
eco:b2782
PATRICifig|1411691.4.peg.3953

Organism-specific databases

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

More...EchoBASEi		EB1229

Phylogenomic databases

eggNOGiCOG2337, Bacteria
HOGENOMiCLU_121823_2_3_6
InParanoidiP0AE70
PhylomeDBiP0AE70

Enzyme and pathway databases

BioCyciEcoCyc:EG11249-MONOMER
MetaCyc:EG11249-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AE70

Protein Ontology

More...PROi		PR:P0AE70

Family and domain databases

DisProtiDP00299
Gene3Di2.30.30.110, 1 hit
InterProiView protein in InterPro
IPR003477, PemK-like
IPR011067, Plasmid_toxin/cell-grow_inhib
PANTHERiPTHR33988, PTHR33988, 1 hit
PfamiView protein in Pfam
PF02452, PemK_toxin, 1 hit

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 nameiMAZF_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: P0AE70
Secondary accession number(s): P33645, Q2MA50
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 2, 2021
This is version 120 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
  2. SIMILARITY comments
    Index of protein domains and families
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