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Protein

Nitrate/nitrite transporter NarK

Gene

narK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. Functions as a nitrate/nitrite exchanger, and protons are probably not co-transported with the substrate.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891SubstrateCurated
Binding sitei305 – 3051SubstrateCurated

GO - Molecular functioni

GO - Biological processi

  • anion transmembrane transport Source: GOC
  • nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Nitrate assimilation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:NARK-MONOMER.
ECOL316407:JW1214-MONOMER.
MetaCyc:NARK-MONOMER.

Protein family/group databases

TCDBi2.A.1.8.1. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate/nitrite transporter NarK
Alternative name(s):
Nitrite extrusion protein 1
Nitrite facilitator 1
Gene namesi
Name:narK
Ordered Locus Names:b1223, JW1214
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10642. narK.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3737CytoplasmicSequence analysisAdd
BLAST
Transmembranei38 – 5821HelicalSequence analysisAdd
BLAST
Topological domaini59 – 7820PeriplasmicSequence analysisAdd
BLAST
Transmembranei79 – 9921HelicalSequence analysisAdd
BLAST
Topological domaini100 – 1034CytoplasmicSequence analysis
Transmembranei104 – 12421HelicalSequence analysisAdd
BLAST
Topological domaini125 – 1317PeriplasmicSequence analysis
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Topological domaini153 – 17725CytoplasmicSequence analysisAdd
BLAST
Transmembranei178 – 19821HelicalSequence analysisAdd
BLAST
Topological domaini199 – 21113PeriplasmicSequence analysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence analysisAdd
BLAST
Topological domaini233 – 25624CytoplasmicSequence analysisAdd
BLAST
Transmembranei257 – 27721HelicalSequence analysisAdd
BLAST
Topological domaini278 – 2836PeriplasmicSequence analysis
Transmembranei284 – 30421HelicalSequence analysisAdd
BLAST
Topological domaini305 – 31915CytoplasmicSequence analysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence analysisAdd
BLAST
Topological domaini341 – 3444PeriplasmicSequence analysis
Transmembranei345 – 36521HelicalSequence analysisAdd
BLAST
Topological domaini366 – 40439CytoplasmicSequence analysisAdd
BLAST
Transmembranei405 – 42521HelicalSequence analysisAdd
BLAST
Topological domaini426 – 43510PeriplasmicSequence analysis
Transmembranei436 – 45621HelicalSequence analysisAdd
BLAST
Topological domaini457 – 4637CytoplasmicSequence analysis

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Nitrate/nitrite transporter NarKPRO_0000096728Add
BLAST

Proteomic databases

PaxDbiP10903.

Expressioni

Inductioni

Highly expressed during anaerobic growth in the presence of nitrate.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4261633. 13 interactions.
STRINGi511145.b1223.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 164Combined sources
Helixi23 – 286Combined sources
Helixi30 – 5223Combined sources
Helixi55 – 617Combined sources
Turni63 – 664Combined sources
Helixi71 – 799Combined sources
Helixi81 – 9919Combined sources
Helixi101 – 11010Combined sources
Helixi113 – 12210Combined sources
Beta strandi125 – 1273Combined sources
Helixi130 – 14011Combined sources
Helixi141 – 1455Combined sources
Helixi146 – 15611Combined sources
Helixi160 – 17516Combined sources
Helixi177 – 18812Combined sources
Helixi195 – 1973Combined sources
Helixi214 – 2174Combined sources
Helixi219 – 23315Combined sources
Helixi249 – 2524Combined sources
Helixi254 – 28431Combined sources
Helixi290 – 2923Combined sources
Turni293 – 2953Combined sources
Helixi296 – 31520Combined sources
Helixi317 – 33418Combined sources
Helixi335 – 3384Combined sources
Beta strandi342 – 3443Combined sources
Helixi348 – 38740Combined sources
Helixi392 – 41423Combined sources
Helixi417 – 43216Combined sources
Beta strandi433 – 4353Combined sources
Helixi436 – 45924Combined sources
Helixi461 – 4633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JR9X-ray2.60A1-463[»]
4JREX-ray2.80A/D1-463[»]
4U4TX-ray2.40A1-463[»]
4U4VX-ray2.35A1-463[»]
4U4WX-ray2.40A/B1-463[»]
ProteinModelPortaliP10903.
SMRiP10903. Positions 13-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DQQ. Bacteria.
COG2223. LUCA.
HOGENOMiHOG000241722.
InParanoidiP10903.
KOiK02575.
OMAiFAFFGPF.
OrthoDBiEOG61042P.
PhylomeDBiP10903.

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.

P10903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHSSAPERA TGAVITDWRP EDPAFWQQRG QRIASRNLWI SVPCLLLAFC
60 70 80 90 100
VWMLFSAVAV NLPKVGFNFT TDQLFMLTAL PSVSGALLRV PYSFMVPIFG
110 120 130 140 150
GRRWTAFSTG ILIIPCVWLG FAVQDTSTPY SVFIIISLLC GFAGANFASS
160 170 180 190 200
MANISFFFPK QKQGGALGLN GGLGNMGVSV MQLVAPLVVS LSIFAVFGSQ
210 220 230 240 250
GVKQPDGTEL YLANASWIWV PFLAIFTIAA WFGMNDLATS KASIKEQLPV
260 270 280 290 300
LKRGHLWIMS LLYLATFGSF IGFSAGFAML SKTQFPDVQI LQYAFFGPFI
310 320 330 340 350
GALARSAGGA LSDRLGGTRV TLVNFILMAI FSGLLFLTLP TDGQGGSFMA
360 370 380 390 400
FFAVFLALFL TAGLGSGSTF QMISVIFRKL TMDRVKAEGG SDERAMREAA
410 420 430 440 450
TDTAAALGFI SAIGAIGGFF IPKAFGSSLA LTGSPVGAMK VFLIFYIACV
460
VITWAVYGRH SKK
Length:463
Mass (Da):49,693
Last modified:January 1, 1990 - v2
Checksum:iAF1DD67CAD40FE8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15996 Genomic DNA. Translation: CAA34126.1.
X69189 Genomic DNA. Translation: CAA48933.1.
U00096 Genomic DNA. Translation: AAC74307.1.
AP009048 Genomic DNA. Translation: BAA36091.1.
X13360 Genomic DNA. Translation: CAA31740.1.
PIRiS05239. GRECNK.
RefSeqiNP_415741.1. NC_000913.3.
WP_000019827.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74307; AAC74307; b1223.
BAA36091; BAA36091; BAA36091.
GeneIDi945783.
KEGGiecj:JW1214.
eco:b1223.
PATRICi32117706. VBIEscCol129921_1275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15996 Genomic DNA. Translation: CAA34126.1.
X69189 Genomic DNA. Translation: CAA48933.1.
U00096 Genomic DNA. Translation: AAC74307.1.
AP009048 Genomic DNA. Translation: BAA36091.1.
X13360 Genomic DNA. Translation: CAA31740.1.
PIRiS05239. GRECNK.
RefSeqiNP_415741.1. NC_000913.3.
WP_000019827.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JR9X-ray2.60A1-463[»]
4JREX-ray2.80A/D1-463[»]
4U4TX-ray2.40A1-463[»]
4U4VX-ray2.35A1-463[»]
4U4WX-ray2.40A/B1-463[»]
ProteinModelPortaliP10903.
SMRiP10903. Positions 13-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261633. 13 interactions.
STRINGi511145.b1223.

Protein family/group databases

TCDBi2.A.1.8.1. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbiP10903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74307; AAC74307; b1223.
BAA36091; BAA36091; BAA36091.
GeneIDi945783.
KEGGiecj:JW1214.
eco:b1223.
PATRICi32117706. VBIEscCol129921_1275.

Organism-specific databases

EchoBASEiEB0636.
EcoGeneiEG10642. narK.

Phylogenomic databases

eggNOGiENOG4105DQQ. Bacteria.
COG2223. LUCA.
HOGENOMiHOG000241722.
InParanoidiP10903.
KOiK02575.
OMAiFAFFGPF.
OrthoDBiEOG61042P.
PhylomeDBiP10903.

Enzyme and pathway databases

BioCyciEcoCyc:NARK-MONOMER.
ECOL316407:JW1214-MONOMER.
MetaCyc:NARK-MONOMER.

Miscellaneous databases

PROiP10903.

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. "The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells."
    Noji S., Nohno T., Saito T., Taniguchi S.
    FEBS Lett. 252:139-143(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
    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. "The narX and narL genes encoding the nitrate-sensing regulators of Escherichia coli are homologous to a family of prokaryotic two-component regulatory genes."
    Nohno T., Noji S., Taniguchi S., Saito T.
    Nucleic Acids Res. 17:2947-2957(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
    Strain: K12.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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: TOPOLOGY.
  11. "Crystal structure of a nitrate/nitrite exchanger."
    Zheng H., Wisedchaisri G., Gonen T.
    Nature 497:647-651(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN EXCHANGER, SUBSTRATE-BINDING SITES, CRYSTALLIZATION.
    Strain: K12.

Entry informationi

Entry nameiNARK_ECOLI
AccessioniPrimary (citable) accession number: P10903
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: January 20, 2016
This is version 128 of the entry and version 2 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.