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Entry version 111 (08 May 2019)
Sequence version 1 (19 Jul 2005)
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Protein

Fumarate and nitrate reduction regulatory protein

Gene

fnr

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

Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O2, is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration.

Miscellaneous

FNR senses the oxygen concentration directly via the disassembly and reassembly of the [4Fe-4S] clusters. Anaerobic, de novo acquisition of the iron-sulfur cluster converts monomeric, inactive apo-FNR into a dimeric form containing two [4Fe-4S] clusters. This, in turn, enhances the affinity of FNR for specific DNA targets and mediates transcription regulation by establishing direct FNR-RNA polymerase contacts. With the increase in intracellular oxygen concentration, the [4Fe-4S] cluster is oxidized, producing a [2Fe-2S] cluster, which decays to apo-FNR. Apo-FNR [4SH] can be reversibly oxidized to a disulfide form [2SH,S-S], suggesting that FNR may be able to sense oxidative stress as well as normoxia. This interconversion may be mediated by agents such as glutathione or thioredoxin.

<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

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi20Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi23Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi29Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi122Iron-sulfur (4Fe-4S)Sequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi197 – 216H-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

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
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:PD00197
ECOL316407:JW1328-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:
Fumarate and nitrate reduction regulatory protein
<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:fnr
Synonyms:nirR
Ordered Locus Names:b1334, JW1328
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10325 fnr

<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

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi16C → A: No effect. 1 Publication1
Mutagenesisi20C → S: Loss of activity. 1 Publication1
Mutagenesisi22D → G: Loss of regulation by O(2). 1 Publication1
Mutagenesisi23C → G: Loss of activity. 1 Publication1
Mutagenesisi28L → H: Loss of regulation by O(2). 1 Publication1
Mutagenesisi29C → G: Loss of activity. 1 Publication1
Mutagenesisi43D → G: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi64E → Q: No effect. 1 Publication1
Mutagenesisi72R → H: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi73S → F: Decrease in activity; no effect on DNA-binding. 2 Publications1
Mutagenesisi81I → T: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi82T → P: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi85G → A: Decrease in activity; no effect on DNA-binding. Trace activity; when associated with P-187. 2 Publications1
Mutagenesisi86D → A: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi87E → K: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi88Q → E: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi93H → R: Loss of regulation by O(2). 1 Publication1
Mutagenesisi96G → D: Loss of activity. 1 Publication1
Mutagenesisi118T → A or P: Decrease in activity; no effect on DNA-binding. 2 Publications1
Mutagenesisi120M → I, R, T or V: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi122C → A or S: Loss of activity. 1 Publication1
Mutagenesisi140R → A: Decrease in activity. 1
Mutagenesisi143M → A: Decrease in activity. 1
Mutagenesisi144M → A: Decrease in activity due to faulty dimerization. 1
Mutagenesisi145R → A: Decrease in activity. 1
Mutagenesisi146L → A: Decrease in activity. 1
Mutagenesisi147M → A: Decrease in activity due to faulty dimerization. 1
Mutagenesisi150E → K: Loss of regulation by O(2). 1 Publication1
Mutagenesisi151I → A: Decrease in activity due to faulty dimerization. 1
Mutagenesisi154D → A, G or V: Loss of regulation by O(2). 2 Publications1
Mutagenesisi158I → A: Decrease in activity due to faulty dimerization. 1
Mutagenesisi181F → L: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi186F → S: Decrease in activity; no effect on DNA-binding. 1 Publication1
Mutagenesisi187S → P: Decrease in activity; no effect on DNA-binding. Trace activity; when associated with A-85. 2 Publications1
Mutagenesisi191F → L: Decrease in activity; no effect on 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_00001001611 – 250Fumarate and nitrate reduction regulatory proteinAdd BLAST250

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9E5

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

More...
PaxDbi
P0A9E5

PRoteomics IDEntifications database

More...
PRIDEi
P0A9E5

<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

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...
CollecTFi
EXPREG_000007e0

<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.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261852, 11 interactors

Database of interacting proteins

More...
DIPi
DIP-9669N

Protein interaction database and analysis system

More...
IntActi
P0A9E5, 8 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1334

<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

3D structure databases

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

More...
SMRi
P0A9E5

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini164 – 237HTH crp-typePROSITE-ProRule annotationAdd BLAST74

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>Regioni20 – 29Essential for the oxygen-regulated activity10
Regioni47 – 50Activating region 2ASequence analysis4
Regioni60 – 61Activating region 3ASequence analysis2
Regioni71 – 75Activating region 1ASequence analysis5
Regioni81Activating region 3BSequence analysis1
Regioni85 – 87Activating region 3CSequence analysis3
Regioni112Activating region 3DSequence analysis1
Regioni116 – 121Activating region 1BSequence analysis6
Regioni123 – 124Activating region 2BSequence analysis2
Regioni127 – 128Activating region 2CSequence analysis2
Regioni140 – 159DimerizationSequence analysisAdd BLAST20
Regioni181 – 191Activating region 1CSequence analysisAdd BLAST11

<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 amino acid residues contacting the FNR target site on the DNA (5'-TTGATNNNNATCAA-3') are located in the putative DNA-recognition helix (alphaF), which contains the FNR motif (EXXSR). Three surface-exposed loops forming activating region 1 (AR1) in the downstream subunit of the dimer contact the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase for activation of class I promoters (the 161-121 loop is the major AR1 activating determinant). At class II promoters, the AR1 of the upstream subunit contacts alphaCTD, promoting open complex formation; activating region 3 (AR3) of the downstream subunit contacts region 4 of the sigma70 subunit of RNA polymerase, to effect direct activation. At promoters repressed by FNR, tandem FNR dimers might interact with each other at AR1 to restrict access to a promoter or jam the promoter by their dual interaction with RNA polymerase alphaCTD.

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DS0 Bacteria
COG0664 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000186461

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9E5

KEGG Orthology (KO)

More...
KOi
K01420

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9E5

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00038 CAP_ED, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
2.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018490 cNMP-bd-like
IPR000595 cNMP-bd_dom
IPR012318 HTH_CRP
IPR014710 RmlC-like_jellyroll
IPR018335 Tscrpt_reg_HTH_Crp-type_CS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00027 cNMP_binding, 1 hit
PF13545 HTH_Crp_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00034 HTHCRP

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50042 CNMP_BINDING_3, 1 hit
PS00042 HTH_CRP_1, 1 hit
PS51063 HTH_CRP_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

P0A9E5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIPEKRIIRR IQSGGCAIHC QDCSISQLCI PFTLNEHELD QLDNIIERKK
60 70 80 90 100
PIQKGQTLFK AGDELKSLYA IRSGTIKSYT ITEQGDEQIT GFHLAGDLVG
110 120 130 140 150
FDAIGSGHHP SFAQALETSM VCEIPFETLD DLSGKMPNLR QQMMRLMSGE
160 170 180 190 200
IKGDQDMILL LSKKNAEERL AAFIYNLSRR FAQRGFSPRE FRLTMTRGDI
210 220 230 240 250
GNYLGLTVET ISRLLGRFQK SGMLAVKGKY ITIENNDALA QLAGHTRNVA
Length:250
Mass (Da):27,967
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:i33F7BFA2972FF703
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 26823±6 Da from positions 10 - 250. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J01608 Genomic DNA Translation: AAA87981.1 Sequence problems.
U00096 Genomic DNA Translation: AAC74416.1
AP009048 Genomic DNA Translation: BAA14927.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A64883 RGECF

NCBI Reference Sequences

More...
RefSeqi
NP_415850.1, NC_000913.3
WP_000611911.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74416; AAC74416; b1334
BAA14927; BAA14927; BAA14927

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945908

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1328
eco:b1334

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.943

<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
J01608 Genomic DNA Translation: AAA87981.1 Sequence problems.
U00096 Genomic DNA Translation: AAC74416.1
AP009048 Genomic DNA Translation: BAA14927.1
PIRiA64883 RGECF
RefSeqiNP_415850.1, NC_000913.3
WP_000611911.1, NZ_LN832404.1

3D structure databases

SMRiP0A9E5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261852, 11 interactors
DIPiDIP-9669N
IntActiP0A9E5, 8 interactors
STRINGi511145.b1334

Proteomic databases

jPOSTiP0A9E5
PaxDbiP0A9E5
PRIDEiP0A9E5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74416; AAC74416; b1334
BAA14927; BAA14927; BAA14927
GeneIDi945908
KEGGiecj:JW1328
eco:b1334
PATRICifig|1411691.4.peg.943

Organism-specific databases

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

More...
EchoBASEi
EB0321
EcoGeneiEG10325 fnr

Phylogenomic databases

eggNOGiENOG4105DS0 Bacteria
COG0664 LUCA
HOGENOMiHOG000186461
InParanoidiP0A9E5
KOiK01420
PhylomeDBiP0A9E5

Enzyme and pathway databases

BioCyciEcoCyc:PD00197
ECOL316407:JW1328-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9E5

Gene expression databases

CollecTFiEXPREG_000007e0

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di1.10.10.10, 1 hit
2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR018490 cNMP-bd-like
IPR000595 cNMP-bd_dom
IPR012318 HTH_CRP
IPR014710 RmlC-like_jellyroll
IPR018335 Tscrpt_reg_HTH_Crp-type_CS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF13545 HTH_Crp_2, 1 hit
PRINTSiPR00034 HTHCRP
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit
PROSITEiView protein in PROSITE
PS50042 CNMP_BINDING_3, 1 hit
PS00042 HTH_CRP_1, 1 hit
PS51063 HTH_CRP_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiFNR_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: P0A9E5
Secondary accession number(s): P03019
<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 21, 1986
Last sequence update: July 19, 2005
Last modified: May 8, 2019
This is version 111 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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