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Protein

Nitrate/nitrite transporter NarU

Gene

narU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. May function as a nitrate/H+ and nitrite/H+ channel. Could confer a selective advantage during severe nutrient starvation or slow growth.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Nitrate assimilation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:NARU-MONOMER.
ECOL316407:JW1464-MONOMER.
MetaCyc:NARU-MONOMER.

Protein family/group databases

TCDBi2.A.1.8.10. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate/nitrite transporter NarU
Alternative name(s):
Nitrite extrusion protein 2
Nitrite facilitator 2
Gene namesi
Name:narU
Synonyms:yddF
Ordered Locus Names:b1469, JW1464
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12153. narU.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535CytoplasmicSequence analysisAdd
BLAST
Transmembranei36 – 5621HelicalSequence analysisAdd
BLAST
Topological domaini57 – 7620PeriplasmicSequence analysisAdd
BLAST
Transmembranei77 – 9721HelicalSequence analysisAdd
BLAST
Topological domaini98 – 1014CytoplasmicSequence analysis
Transmembranei102 – 12221HelicalSequence analysisAdd
BLAST
Topological domaini123 – 1253PeriplasmicSequence analysis
Transmembranei126 – 14621HelicalSequence analysisAdd
BLAST
Topological domaini147 – 18034CytoplasmicSequence analysisAdd
BLAST
Transmembranei181 – 20121HelicalSequence analysisAdd
BLAST
Topological domaini202 – 2065PeriplasmicSequence analysis
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Topological domaini228 – 25831CytoplasmicSequence analysisAdd
BLAST
Transmembranei259 – 27921HelicalSequence analysisAdd
BLAST
Topological domaini280 – 2878PeriplasmicSequence analysis
Transmembranei288 – 30821HelicalSequence analysisAdd
BLAST
Topological domaini309 – 3179CytoplasmicSequence analysis
Transmembranei318 – 33821HelicalSequence analysisAdd
BLAST
Topological domaini339 – 3446PeriplasmicSequence analysis
Transmembranei345 – 36521HelicalSequence analysisAdd
BLAST
Topological domaini366 – 40136CytoplasmicSequence analysisAdd
BLAST
Transmembranei402 – 42221HelicalSequence analysisAdd
BLAST
Topological domaini423 – 43210PeriplasmicSequence analysis
Transmembranei433 – 45321HelicalSequence analysisAdd
BLAST
Topological domaini454 – 4629CytoplasmicSequence analysis

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871R → F, H, K, L, N, P or Q: Loss of activity. 2 Publications
Mutagenesisi99 – 991G → A: No change in activity. 1 Publication
Mutagenesisi99 – 991G → T: Decrease in activity. 1 Publication
Mutagenesisi113 – 1131P → A: No change in activity. 1 Publication
Mutagenesisi113 – 1131P → C or L: Decrease in activity. 1 Publication
Mutagenesisi139 – 1391G → E or I: Loss of activity. 1 Publication
Mutagenesisi145 – 1451F → E or W: Loss of activity. 1 Publication
Mutagenesisi162 – 1621G → A or S: Loss of activity. 1 Publication
Mutagenesisi172 – 1721G → A: No change in activity. 1 Publication
Mutagenesisi172 – 1721G → V: Loss of activity. 1 Publication
Mutagenesisi175 – 1751G → A or S: Loss of activity. 1 Publication
Mutagenesisi261 – 2611Y → N: No change in activity. 1 Publication
Mutagenesisi266 – 2661G → A, P or T: Loss of activity. 1 Publication
Mutagenesisi303 – 3031R → C, D, K, L, N, P or Q: Loss of activity. 2 Publications
Mutagenesisi307 – 3071G → L: Loss of activity. 1 Publication
Mutagenesisi311 – 3111D → G or K: Loss of activity. 1 Publication
Mutagenesisi405 – 4051G → A, L or V: Loss of activity. 1 Publication
Mutagenesisi414 – 4141G → L: No change in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Nitrate/nitrite transporter NarUPRO_0000096729Add
BLAST

Proteomic databases

PaxDbiP37758.

Expressioni

Inductioni

Expressed preferentially during the stationary phase in the absence of nitrate.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4260180. 13 interactions.
STRINGi511145.b1469.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 277Combined sources
Helixi29 – 5022Combined sources
Helixi52 – 554Combined sources
Helixi57 – 604Combined sources
Turni61 – 644Combined sources
Helixi69 – 779Combined sources
Helixi79 – 835Combined sources
Turni84 – 863Combined sources
Helixi87 – 10822Combined sources
Helixi111 – 12010Combined sources
Helixi128 – 13912Combined sources
Helixi140 – 1423Combined sources
Helixi144 – 15310Combined sources
Turni158 – 1603Combined sources
Helixi161 – 17212Combined sources
Helixi174 – 18613Combined sources
Helixi193 – 1953Combined sources
Beta strandi200 – 2023Combined sources
Turni203 – 2053Combined sources
Beta strandi206 – 2083Combined sources
Helixi212 – 2154Combined sources
Helixi217 – 23115Combined sources
Helixi245 – 2506Combined sources
Helixi255 – 2584Combined sources
Turni259 – 2657Combined sources
Helixi266 – 28116Combined sources
Helixi288 – 2903Combined sources
Turni291 – 2933Combined sources
Helixi294 – 30916Combined sources
Turni310 – 3123Combined sources
Helixi315 – 33218Combined sources
Helixi333 – 3353Combined sources
Beta strandi337 – 3415Combined sources
Helixi345 – 37430Combined sources
Helixi396 – 40914Combined sources
Turni410 – 4134Combined sources
Helixi414 – 42815Combined sources
Beta strandi429 – 4324Combined sources
Helixi433 – 45220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IU8X-ray3.11A/B1-462[»]
4IU9X-ray3.00A/B1-462[»]
ProteinModelPortaliP37758.
SMRiP37758. Positions 12-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107QND. Bacteria.
COG2223. LUCA.
HOGENOMiHOG000241722.
InParanoidiP37758.
KOiK02575.
OMAiQNAAFLW.
OrthoDBiEOG61042P.
PhylomeDBiP37758.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR004737. NO3_transporter.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00886. 2A0108. 1 hit.

Sequencei

Sequence statusi: Complete.

P37758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALQNEKNSR YLLRDWKPEN PAFWENKGKH IARRNLWISV SCLLLAFCVW
60 70 80 90 100
MLFSAVTVNL NKIGFNFTTD QLFLLTALPS VSGALLRVPY SFMVPIFGGR
110 120 130 140 150
RWTVFSTAIL IIPCVWLGIA VQNPNTPFGI FIVIALLCGF AGANFASSMG
160 170 180 190 200
NISFFFPKAK QGSALGINGG LGNLGVSVMQ LVAPLVIFVP VFAFLGVNGV
210 220 230 240 250
PQADGSVMSL ANAAWIWVPL LAIATIAAWS GMNDIASSRA SIADQLPVLQ
260 270 280 290 300
RLHLWLLSLL YLATFGSFIG FSAGFAMLAK TQFPDVNILR LAFFGPFIGA
310 320 330 340 350
IARSVGGAIS DKFGGVRVTL INFIFMAIFS ALLFLTLPGT GSGNFIAFYA
360 370 380 390 400
VFMGLFLTAG LGSGSTFQMI AVIFRQITIY RVKMKGGSDE QAHKEAVTET
410 420 430 440 450
AAALGFISAI GAVGGFFIPQ AFGMSLNMTG SPVGAMKVFL IFYIVCVLLT
460
WLVYGRRKFS QK
Length:462
Mass (Da):49,890
Last modified:November 1, 1997 - v3
Checksum:i33FBE3C140FBC4DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901Missing (Ref. 1) Curated
Sequence conflicti293 – 2931F → FR (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94992 Genomic DNA. Translation: CAA64448.1.
U00096 Genomic DNA. Translation: AAD13433.1.
AP009048 Genomic DNA. Translation: BAA15118.1.
X17110 Genomic DNA. No translation available.
PIRiH64899. S11431.
RefSeqiNP_415986.1. NC_000913.3.
WP_001207901.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAD13433; AAD13433; b1469.
BAA15118; BAA15118; BAA15118.
GeneIDi945799.
KEGGiecj:JW1464.
eco:b1469.
PATRICi32118230. VBIEscCol129921_1535.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94992 Genomic DNA. Translation: CAA64448.1.
U00096 Genomic DNA. Translation: AAD13433.1.
AP009048 Genomic DNA. Translation: BAA15118.1.
X17110 Genomic DNA. No translation available.
PIRiH64899. S11431.
RefSeqiNP_415986.1. NC_000913.3.
WP_001207901.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IU8X-ray3.11A/B1-462[»]
4IU9X-ray3.00A/B1-462[»]
ProteinModelPortaliP37758.
SMRiP37758. Positions 12-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260180. 13 interactions.
STRINGi511145.b1469.

Protein family/group databases

TCDBi2.A.1.8.10. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbiP37758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13433; AAD13433; b1469.
BAA15118; BAA15118; BAA15118.
GeneIDi945799.
KEGGiecj:JW1464.
eco:b1469.
PATRICi32118230. VBIEscCol129921_1535.

Organism-specific databases

EchoBASEiEB2073.
EcoGeneiEG12153. narU.

Phylogenomic databases

eggNOGiENOG4107QND. Bacteria.
COG2223. LUCA.
HOGENOMiHOG000241722.
InParanoidiP37758.
KOiK02575.
OMAiQNAAFLW.
OrthoDBiEOG61042P.
PhylomeDBiP37758.

Enzyme and pathway databases

BioCyciEcoCyc:NARU-MONOMER.
ECOL316407:JW1464-MONOMER.
MetaCyc:NARU-MONOMER.

Miscellaneous databases

PROiP37758.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR004737. NO3_transporter.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00886. 2A0108. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Bonnefoy V., Ratouchniak J., Blasco F., Chippaux M.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon."
    Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.
    Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-462.
  6. Cited for: IDENTIFICATION.
  7. "The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters."
    Clegg S., Yu F., Griffiths L., Cole J.A.
    Mol. Microbiol. 44:143-155(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.
  8. "Nitrate and nitrite transport in Escherichia coli."
    Jia W., Cole J.A.
    Biochem. Soc. Trans. 33:159-161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-87 AND ARG-303.
  9. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  10. "Role of the Escherichia coli nitrate transport protein, NarU, in survival during severe nutrient starvation and slow growth."
    Clegg S.J., Jia W., Cole J.A.
    Microbiology 152:2091-2100(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: K12.
  11. "A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake."
    Jia W., Tovell N., Clegg S., Trimmer M., Cole J.
    Biochem. J. 417:297-304(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-87; GLY-99; PRO-113; GLY-139; PHE-145; GLY-162; GLY-172; GLY-175; TYR-261; GLY-266; ARG-303; GLY-307; ASP-311; GLY-405 AND GLY-414.

Entry informationi

Entry nameiNARU_ECOLI
AccessioniPrimary (citable) accession number: P37758
Secondary accession number(s): P77696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: February 17, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.