NARU_ECOLI
ID NARU_ECOLI Reviewed; 462 AA.
AC P37758; P77696;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Nitrate/nitrite transporter NarU;
DE AltName: Full=Nitrite extrusion protein 2;
DE AltName: Full=Nitrite facilitator 2;
GN Name=narU; Synonyms=yddF; OrderedLocusNames=b1469, JW1464;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Bonnefoy V., Ratouchniak J., Blasco F., Chippaux M.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-462.
RX PubMed=2233673; DOI=10.1007/bf00283030;
RA Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.;
RT "Nitrate reductases of Escherichia coli: sequence of the second nitrate
RT reductase and comparison with that encoded by the narGHJI operon.";
RL Mol. Gen. Genet. 222:104-111(1990).
RN [6]
RP IDENTIFICATION.
RX PubMed=7747940; DOI=10.1007/bf00871632;
RA Bonnefoy V., Demoss J.A.;
RT "Nitrate reductases in Escherichia coli.";
RL Antonie Van Leeuwenhoek 66:47-56(1994).
RN [7]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=11967075; DOI=10.1046/j.1365-2958.2002.02858.x;
RA Clegg S., Yu F., Griffiths L., Cole J.A.;
RT "The roles of the polytopic membrane proteins NarK, NarU and NirC in
RT Escherichia coli K-12: two nitrate and three nitrite transporters.";
RL Mol. Microbiol. 44:143-155(2002).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-87 AND ARG-303.
RX PubMed=15667293; DOI=10.1042/bst0330159;
RA Jia W., Cole J.A.;
RT "Nitrate and nitrite transport in Escherichia coli.";
RL Biochem. Soc. Trans. 33:159-161(2005).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=16804183; DOI=10.1099/mic.0.28688-0;
RA Clegg S.J., Jia W., Cole J.A.;
RT "Role of the Escherichia coli nitrate transport protein, NarU, in survival
RT during severe nutrient starvation and slow growth.";
RL Microbiology 152:2091-2100(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-87; GLY-99; PRO-113;
RP GLY-139; PHE-145; GLY-162; GLY-172; GLY-175; TYR-261; GLY-266; ARG-303;
RP GLY-307; ASP-311; GLY-405 AND GLY-414.
RX PubMed=18691156; DOI=10.1042/bj20080746;
RA Jia W., Tovell N., Clegg S., Trimmer M., Cole J.;
RT "A single channel for nitrate uptake, nitrite export and nitrite uptake by
RT Escherichia coli NarU and a role for NirC in nitrite export and uptake.";
RL Biochem. J. 417:297-304(2009).
CC -!- FUNCTION: Catalyzes nitrate uptake, nitrite uptake and nitrite export
CC across the cytoplasmic membrane. May function as a nitrate/H(+) and
CC nitrite/H(+) channel. Could confer a selective advantage during severe
CC nutrient starvation or slow growth. {ECO:0000269|PubMed:11967075,
CC ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:16804183,
CC ECO:0000269|PubMed:18691156}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:18691156}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:18691156}.
CC -!- INDUCTION: Expressed preferentially during the stationary phase in the
CC absence of nitrate. {ECO:0000269|PubMed:16804183}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nitrate/nitrite porter (TC 2.A.1.8) family. {ECO:0000305}.
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DR EMBL; X94992; CAA64448.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13433.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15118.1; -; Genomic_DNA.
DR EMBL; X17110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H64899; S11431.
DR RefSeq; NP_415986.1; NC_000913.3.
DR RefSeq; WP_001207901.1; NZ_SSZK01000038.1.
DR PDB; 4IU8; X-ray; 3.11 A; A/B=1-462.
DR PDB; 4IU9; X-ray; 3.00 A; A/B=1-462.
DR PDBsum; 4IU8; -.
DR PDBsum; 4IU9; -.
DR AlphaFoldDB; P37758; -.
DR SMR; P37758; -.
DR BioGRID; 4260180; 13.
DR STRING; 511145.b1469; -.
DR TCDB; 2.A.1.8.10; the major facilitator superfamily (mfs).
DR jPOST; P37758; -.
DR PaxDb; P37758; -.
DR PRIDE; P37758; -.
DR EnsemblBacteria; AAD13433; AAD13433; b1469.
DR EnsemblBacteria; BAA15118; BAA15118; BAA15118.
DR GeneID; 945799; -.
DR KEGG; ecj:JW1464; -.
DR KEGG; eco:b1469; -.
DR PATRIC; fig|1411691.4.peg.799; -.
DR EchoBASE; EB2073; -.
DR eggNOG; COG2223; Bacteria.
DR HOGENOM; CLU_033198_1_0_6; -.
DR InParanoid; P37758; -.
DR OMA; WWYYARR; -.
DR PhylomeDB; P37758; -.
DR BioCyc; EcoCyc:NARU-MON; -.
DR BioCyc; MetaCyc:NARU-MON; -.
DR BRENDA; 7.3.2.4; 2026.
DR PRO; PR:P37758; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015514; F:nitrite efflux transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0015706; P:nitrate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015707; P:nitrite transport; IBA:GO_Central.
DR CDD; cd17341; MFS_NRT2_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044772; NO3_transporter.
DR InterPro; IPR004737; NO3_transporter_NarK/NarU-like.
DR PANTHER; PTHR23515; PTHR23515; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00886; 2A0108; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Nitrate assimilation; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..462
FT /note="Nitrate/nitrite transporter NarU"
FT /id="PRO_0000096729"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..76
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..125
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..206
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..287
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..344
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..432
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 87
FT /note="R->F,H,K,L,N,P,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15667293,
FT ECO:0000269|PubMed:18691156"
FT MUTAGEN 99
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 99
FT /note="G->T: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 113
FT /note="P->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 113
FT /note="P->C,L: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 139
FT /note="G->E,I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 145
FT /note="F->E,W: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 162
FT /note="G->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 172
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 172
FT /note="G->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 175
FT /note="G->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 261
FT /note="Y->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 266
FT /note="G->A,P,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 303
FT /note="R->C,D,K,L,N,P,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15667293,
FT ECO:0000269|PubMed:18691156"
FT MUTAGEN 307
FT /note="G->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 311
FT /note="D->G,K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 405
FT /note="G->A,L,V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT MUTAGEN 414
FT /note="G->L: No change in activity."
FT /evidence="ECO:0000269|PubMed:18691156"
FT CONFLICT 290
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="F -> FR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 29..50
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:4IU9"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4IU9"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 259..265
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:4IU8"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4IU9"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 345..374
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 396..409
FT /evidence="ECO:0007829|PDB:4IU9"
FT TURN 410..413
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 414..428
FT /evidence="ECO:0007829|PDB:4IU9"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:4IU9"
FT HELIX 433..452
FT /evidence="ECO:0007829|PDB:4IU9"
SQ SEQUENCE 462 AA; 49890 MW; 33FBE3C140FBC4DF CRC64;
MALQNEKNSR YLLRDWKPEN PAFWENKGKH IARRNLWISV SCLLLAFCVW MLFSAVTVNL
NKIGFNFTTD QLFLLTALPS VSGALLRVPY SFMVPIFGGR RWTVFSTAIL IIPCVWLGIA
VQNPNTPFGI FIVIALLCGF AGANFASSMG NISFFFPKAK QGSALGINGG LGNLGVSVMQ
LVAPLVIFVP VFAFLGVNGV PQADGSVMSL ANAAWIWVPL LAIATIAAWS GMNDIASSRA
SIADQLPVLQ RLHLWLLSLL YLATFGSFIG FSAGFAMLAK TQFPDVNILR LAFFGPFIGA
IARSVGGAIS DKFGGVRVTL INFIFMAIFS ALLFLTLPGT GSGNFIAFYA VFMGLFLTAG
LGSGSTFQMI AVIFRQITIY RVKMKGGSDE QAHKEAVTET AAALGFISAI GAVGGFFIPQ
AFGMSLNMTG SPVGAMKVFL IFYIVCVLLT WLVYGRRKFS QK
