ID   NARV_ECOLI              Reviewed;         226 AA.
AC   P0AF32; P19316;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Respiratory nitrate reductase 2 gamma chain;
DE            EC=1.7.5.1;
GN   Name=narV; OrderedLocusNames=b1465, JW1460;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [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   TOPOLOGY [LARGE SCALE ANALYSIS].
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).
CC   -!- FUNCTION: This is a second nitrate reductase enzyme which can
CC       substitute for the NRA enzyme and allows E.coli to use nitrate as an
CC       electron acceptor during anaerobic growth. The gamma chain is a
CC       membrane-embedded heme-iron unit resembling cytochrome b, which
CC       transfers electrons from quinones to the beta subunit.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC         Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC         ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 2 heme groups per subunit. Heme 1 is located at the
CC       cytoplasmic interface, heme 2 is located at the periplasmic interface.
CC       Electrons are transferred from the periplasmic to the cytoplasmic heme.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta and a
CC       gamma chain. Alpha and beta are catalytic chains; gamma chains are
CC       involved in binding the enzyme complex to the cytoplasmic membrane.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR   EMBL; X17110; CAA34967.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74547.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15102.1; -; Genomic_DNA.
DR   PIR; S11430; S11430.
DR   RefSeq; NP_415982.1; NC_000913.3.
DR   RefSeq; WP_000617115.1; NZ_STEB01000053.1.
DR   AlphaFoldDB; P0AF32; -.
DR   SMR; P0AF32; -.
DR   BioGRID; 4263337; 14.
DR   ComplexPortal; CPX-5581; Nitrate reductase Z complex.
DR   STRING; 511145.b1465; -.
DR   TCDB; 5.A.3.1.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P0AF32; -.
DR   PaxDb; 511145-b1465; -.
DR   EnsemblBacteria; AAC74547; AAC74547; b1465.
DR   GeneID; 75203169; -.
DR   GeneID; 946029; -.
DR   KEGG; ecj:JW1460; -.
DR   KEGG; eco:b1465; -.
DR   PATRIC; fig|1411691.4.peg.803; -.
DR   EchoBASE; EB0638; -.
DR   eggNOG; COG2181; Bacteria.
DR   HOGENOM; CLU_092378_1_0_6; -.
DR   InParanoid; P0AF32; -.
DR   OMA; FLPMSQK; -.
DR   OrthoDB; 9788113at2; -.
DR   PhylomeDB; P0AF32; -.
DR   BioCyc; EcoCyc:NARV-MONOMER; -.
DR   BioCyc; MetaCyc:NARV-MONOMER; -.
DR   PHI-base; PHI:10519; -.
DR   PRO; PR:P0AF32; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0009325; C:nitrate reductase complex; IPI:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; ISM:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IDA:EcoCyc.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IDA:EcoCyc.
DR   GO; GO:0009061; P:anaerobic respiration; IDA:EcoCyc.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0042126; P:nitrate metabolic process; NAS:ComplexPortal.
DR   Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR   InterPro; IPR023234; NarG-like_domain.
DR   InterPro; IPR036197; NarG-like_sf.
DR   InterPro; IPR003816; Nitrate_red_gam.
DR   NCBIfam; TIGR00351; narI; 1.
DR   PANTHER; PTHR30598; NITRATE REDUCTASE PRIVATE CHAPERONE, REDOX ENZYME MATURATION PROTEIN REMP FAMILY; 1.
DR   PANTHER; PTHR30598:SF4; RESPIRATORY NITRATE REDUCTASE 2 GAMMA CHAIN; 1.
DR   Pfam; PF02665; Nitrate_red_gam; 1.
DR   SUPFAM; SSF103501; Respiratory nitrate reductase 1 gamma chain; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..226
FT                   /note="Respiratory nitrate reductase 2 gamma chain"
FT                   /id="PRO_0000096731"
FT   TOPO_DOM        1..4
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        5..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        31..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..71
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        72..83
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        84..113
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        114..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        126..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        150..183
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        184..199
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        200..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  26018 MW;  1D5FAC307F3D5B84 CRC64;
     MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV IWSNLFHIGI
     LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV LTLIGGAGLL WRRLTNQRVR
     ATSTTPDIII MSILLIQCLL GLSTIPFSAQ YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG
     VAFVFRLHLV LGMTIFLLFP FTRLVHVWSA PFEYFTRRYQ IVRSRR
//