NIRC_ECOLI
ID NIRC_ECOLI Reviewed; 268 AA.
AC P0AC26; P11097; P78112; Q2M733;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nitrite transporter NirC;
GN Name=nirC; OrderedLocusNames=b3367, JW3330;
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;
RX PubMed=2543955; DOI=10.1093/nar/17.10.3865;
RA Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.;
RT "Cloning of binding sequences for the Escherichia coli transcription
RT activators, FNR and CRP: location of bases involved in discrimination
RT between FNR and CRP.";
RL Nucleic Acids Res. 17:3865-3874(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2200672; DOI=10.1111/j.1432-1033.1990.tb19125.x;
RA Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N.,
RA Wootton J., Nicolson R., Cole J.A.;
RT "Nucleotide sequence, organisation and structural analysis of the products
RT of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome.";
RL Eur. J. Biochem. 191:315-323(1990).
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 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 [6]
RP FUNCTION.
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 [7]
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 [8]
RP FUNCTION.
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 nitrite uptake and nitrite export across the
CC cytoplasmic membrane. Is up to 10-fold more active than NarK or NarU in
CC nitrite uptake for subsequent reduction in the cytoplasm by the
CC NirB/NirD nitrite reductase. {ECO:0000269|PubMed:11967075,
CC ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:18691156}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the FNT transporter (TC 2.A.44) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58164.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA32418.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X14202; CAA32418.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA58164.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76392.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77923.1; -; Genomic_DNA.
DR PIR; B65131; B65131.
DR RefSeq; WP_000493556.1; NZ_STEB01000004.1.
DR RefSeq; YP_026212.2; NC_000913.3.
DR AlphaFoldDB; P0AC26; -.
DR SMR; P0AC26; -.
DR BioGRID; 4262477; 13.
DR STRING; 511145.b3367; -.
DR TCDB; 1.A.16.3.1; the formate-nitrite transporter (fnt) family.
DR PaxDb; P0AC26; -.
DR PRIDE; P0AC26; -.
DR EnsemblBacteria; AAC76392; AAC76392; b3367.
DR EnsemblBacteria; BAE77923; BAE77923; BAE77923.
DR GeneID; 2847757; -.
DR GeneID; 66672752; -.
DR KEGG; ecj:JW3330; -.
DR KEGG; eco:b3367; -.
DR PATRIC; fig|1411691.4.peg.3362; -.
DR EchoBASE; EB0648; -.
DR eggNOG; COG2116; Bacteria.
DR HOGENOM; CLU_036896_2_1_6; -.
DR InParanoid; P0AC26; -.
DR OMA; SIRPLVM; -.
DR PhylomeDB; P0AC26; -.
DR BioCyc; EcoCyc:NIRC-MON; -.
DR BioCyc; MetaCyc:NIRC-MON; -.
DR PHI-base; PHI:3597; -.
DR PRO; PR:P0AC26; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015499; F:formate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015724; P:formate transport; IBA:GO_Central.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000292; For/NO2_transpt.
DR InterPro; IPR024002; For/NO2_transpt_CS.
DR PANTHER; PTHR30520; PTHR30520; 1.
DR Pfam; PF01226; Form_Nir_trans; 1.
DR TIGRFAMs; TIGR00790; fnt; 1.
DR PROSITE; PS01005; FORMATE_NITRITE_TP_1; 1.
DR PROSITE; PS01006; FORMATE_NITRITE_TP_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Nitrate assimilation;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..268
FT /note="Nitrite transporter NirC"
FT /id="PRO_0000094724"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..151
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..225
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 268 AA; 28563 MW; 6E01788EA8FB8F31 CRC64;
MFTDTINKCA ANAARIARLS ANNPLGFWVS SAMAGAYVGL GIILIFTLGN LLDPSVRPLV
MGATFGIALT LVIIAGSELF TGHTMFLTFG VKAGSISHGQ MWAILPQTWL GNLVGSVFVA
MLYSWGGGSL LPVDTSIVHS VALAKTTAPA MVLFFKGALC NWLVCLAIWM ALRTEGAAKF
IAIWWCLLAF IASGYEHSIA NMTLFALSWF GNHSEAYTLA GIGHNLLWVT LGNTLSGAVF
MGLGYWYATP KANRPVADKF NQTETAAG
