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Entry version 122 (07 Oct 2020)
Sequence version 1 (19 Jul 2005)
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Protein

DNA-binding transcriptional dual regulator ModE

Gene

modE

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

Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate (PubMed:8550508). Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9210473, PubMed:9044285). Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate (PubMed:9044285). The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3' (PubMed:9210473, PubMed:9044285, PubMed:16205910). Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly (PubMed:9466267, PubMed:10206709, PubMed:16205910). ModE also binds tungstate (PubMed:9210473, PubMed:11259434).7 Publications

<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

The ModE dimer binds two molecules of molybdate (MoO42-) with a Kd of 0.8 µM, which results in major changes in the conformation of the DNA-binding domain and confers high-affinity DNA-binding to the transcription factor (PubMed:9210473, PubMed:9044285, PubMed:11259434, PubMed:12581638). Additionally molybdate binding moves the 2 Mop domains closer together, trapping the ligand between them (PubMed:12581638). Can also bind tungstate (PubMed:9210473, PubMed:11259434). Molybdate is bound at the dimer interface using residues from each monomer (PubMed:11259434, PubMed:12581638).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi126MolybdateCombined sources2 Publications1
Metal bindingi128Molybdate; via amide nitrogenCombined sources2 Publications1
Metal bindingi163MolybdateCombined sources2 Publications1
Metal bindingi166MolybdateCombined sources2 Publications1
Metal bindingi183MolybdateCombined sources2 Publications1
Metal bindingi184Molybdate; via amide nitrogenCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi33 – 79H-T-H motifAdd BLAST47

<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 functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation, Transport
LigandMetal-binding, Molybdenum

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:MONOMER0-185

<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:
DNA-binding transcriptional dual regulator ModE
<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:modE1 Publication
Synonyms:modR1 Publication
Ordered Locus Names:b0761, JW0744
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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

  • Cytoplasm 1 Publication

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

<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

Loss of repression of the modABC operon (PubMed:8564363, PubMed:8931336). Not essential for molybdopterin cofactor synthesis (PubMed:8931336). Increased dmsA expression under aerobic conditions and reduced expression under anaerobic conditions (PubMed:9466267). Decreased expression of hyc and narG (PubMed:10206709).4 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>Mutagenesisi76A → V: Partial loss of repression by ModE. 1 Publication1
Mutagenesisi125T → I: Transcription repression by ModE even in the absence of molybdate. 1 Publication1
Mutagenesisi133G → D: Transcription repression by ModE even in the absence of molybdate. 1 Publication1
Mutagenesisi216 – 262Missing : Transcription repression by ModE even in the absence of molybdate. 1 PublicationAdd BLAST47

<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_00002011251 – 262DNA-binding transcriptional dual regulator ModEAdd BLAST262

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9G8

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

More...
PaxDbi
P0A9G8

PRoteomics IDEntifications database

More...
PRIDEi
P0A9G8

<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

Constitutively expressed at low levels; probably part of the modE-modF operon (PubMed:8564363, PubMed:8931336) (Probable). Does not seem to be autoregulated (PubMed:8931336).1 Publication2 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

Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259327, 4 interactors
849742, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2115, ModE complex

Database of interacting proteins

More...
DIPi
DIP-10238N

Protein interaction database and analysis system

More...
IntActi
P0A9G8, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b0761

<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

1262
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
P0A9G8

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
P0A9G8

<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%5Fand%5Fdomains%5Fsection">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>Domaini124 – 191Mop 1PROSITE-ProRule annotationAdd BLAST68
Domaini196 – 260Mop 2PROSITE-ProRule annotationAdd BLAST65

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>Regioni1 – 121I1 PublicationAdd BLAST121
Regioni125 – 133Required for dimer formation and molybdate binding9

<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

Deletion of the C-terminus (from residues 122 on) results in constitutive repression of modA (PubMed:8931336). Contains two major domains: the N-terminal domain I forms a winged helix-turn-helix motif and interacts with DNA (Probable). The C-terminal domain II is the olybdate-binding component and contains a tandem repeat of the Mop domain, each of which forms a beta-barrel (Probable) (PubMed:12581638). The N-terminal domain plays a major role in the dimerization of the protein whereas the C-terminal domain contributes to the stability of the complex (Probable).2 Publications2 Publications

<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 ModE family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2005, Bacteria
COG3585, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_087839_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9G8

KEGG Orthology (KO)

More...
KOi
K02019

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9G8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004606, Mo-pterin-bd
IPR008995, Mo/tungstate-bd_C_term_dom
IPR016462, ModE
IPR003725, ModE-bd_N
IPR005116, Transp-assoc_OB_typ1
IPR000847, Tscrpt_reg_HTH_LysR
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00126, HTH_1, 1 hit
PF03459, TOBE, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005763, Txn_reg_ModE, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785, SSF46785, 1 hit
SSF50331, SSF50331, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00637, ModE_repress, 1 hit
TIGR00638, Mop, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51866, MOP, 2 hits

<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.

P0A9G8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQAEILLTLK LQQKLFADPR RISLLKHIAL SGSISQGAKD AGISYKSAWD
60 70 80 90 100
AINEMNQLSE HILVERATGG KGGGGAVLTR YGQRLIQLYD LLAQIQQKAF
110 120 130 140 150
DVLSDDDALP LNSLLAAISR FSLQTSARNQ WFGTITARDH DDVQQHVDVL
160 170 180 190 200
LADGKTRLKV AITAQSGARL GLDEGKEVLI LLKAPWVGIT QDEAVAQNAD
210 220 230 240 250
NQLPGIISHI ERGAEQCEVL MALPDGQTLC ATVPVNEATS LQQGQNVTAY
260
FNADSVIIAT LC
Length:262
Mass (Da):28,281
Last modified:July 19, 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:i9A17636162F4233E
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 28271 Da. Determined by MALDI. 1 Publication

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
U07867 Genomic DNA Translation: AAB06892.1
U27192 Genomic DNA Translation: AAB60175.1
U34275 Genomic DNA Translation: AAA77051.1
U00096 Genomic DNA Translation: AAC73848.1
AP009048 Genomic DNA Translation: BAA35425.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC6037

NCBI Reference Sequences

More...
RefSeqi
NP_415282.1, NC_000913.3
WP_001147439.1, NZ_SSZK01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73848; AAC73848; b0761
BAA35425; BAA35425; BAA35425

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
48106995
945366

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0744
eco:b0761

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1517

<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
U07867 Genomic DNA Translation: AAB06892.1
U27192 Genomic DNA Translation: AAB60175.1
U34275 Genomic DNA Translation: AAA77051.1
U00096 Genomic DNA Translation: AAC73848.1
AP009048 Genomic DNA Translation: BAA35425.1
PIRiJC6037
RefSeqiNP_415282.1, NC_000913.3
WP_001147439.1, NZ_SSZK01000002.1

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
1B9MX-ray1.75A/B1-262[»]
1B9NX-ray2.09A/B1-262[»]
1H9RX-ray1.90A/B124-262[»]
1H9SX-ray1.82A/B124-262[»]
1O7LX-ray2.75A/B/C/D1-262[»]
SMRiP0A9G8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259327, 4 interactors
849742, 1 interactor
ComplexPortaliCPX-2115, ModE complex
DIPiDIP-10238N
IntActiP0A9G8, 1 interactor
STRINGi511145.b0761

Proteomic databases

jPOSTiP0A9G8
PaxDbiP0A9G8
PRIDEiP0A9G8

Genome annotation databases

EnsemblBacteriaiAAC73848; AAC73848; b0761
BAA35425; BAA35425; BAA35425
GeneIDi48106995
945366
KEGGiecj:JW0744
eco:b0761
PATRICifig|1411691.4.peg.1517

Organism-specific databases

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

More...
EchoBASEi
EB3017

Phylogenomic databases

eggNOGiCOG2005, Bacteria
COG3585, Bacteria
HOGENOMiCLU_087839_0_0_6
InParanoidiP0A9G8
KOiK02019
PhylomeDBiP0A9G8

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-185

Miscellaneous databases

EvolutionaryTraceiP0A9G8

Protein Ontology

More...
PROi
PR:P0A9G8

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR004606, Mo-pterin-bd
IPR008995, Mo/tungstate-bd_C_term_dom
IPR016462, ModE
IPR003725, ModE-bd_N
IPR005116, Transp-assoc_OB_typ1
IPR000847, Tscrpt_reg_HTH_LysR
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf
PfamiView protein in Pfam
PF00126, HTH_1, 1 hit
PF03459, TOBE, 2 hits
PIRSFiPIRSF005763, Txn_reg_ModE, 1 hit
SUPFAMiSSF46785, SSF46785, 1 hit
SSF50331, SSF50331, 2 hits
TIGRFAMsiTIGR00637, ModE_repress, 1 hit
TIGR00638, Mop, 1 hit
PROSITEiView protein in PROSITE
PS51866, MOP, 2 hits

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 nameiMODE_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: P0A9G8
Secondary accession number(s): P46930
<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: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 7, 2020
This is version 122 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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