ID   NARY_ECOLI              Reviewed;         514 AA.
AC   P19318; P78267;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Respiratory nitrate reductase 2 beta chain;
DE            EC=1.7.5.1;
GN   Name=narY; OrderedLocusNames=b1467, JW1462;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
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).
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 beta chain is an
CC       electron transfer unit containing four cysteine clusters involved in
CC       the formation of iron-sulfur centers. Electrons are transferred from
CC       the gamma chain to the molybdenum cofactor of the alpha 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster per subunit. {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   -!- INTERACTION:
CC       P19318; P42593: fadH; NbExp=3; IntAct=EBI-555059, EBI-561933;
CC       P19318; P09152: narG; NbExp=5; IntAct=EBI-555059, EBI-547248;
CC       P19318; P11349: narH; NbExp=3; IntAct=EBI-555059, EBI-555067;
CC       P19318; P19317: narW; NbExp=4; IntAct=EBI-555059, EBI-555088;
CC       P19318; P04825: pepN; NbExp=3; IntAct=EBI-555059, EBI-545385;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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DR   EMBL; X17110; CAA34965.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74549.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15104.1; -; Genomic_DNA.
DR   PIR; F64899; F64899.
DR   RefSeq; NP_415984.1; NC_000913.3.
DR   RefSeq; WP_000702535.1; NZ_SSZK01000038.1.
DR   AlphaFoldDB; P19318; -.
DR   SMR; P19318; -.
DR   BioGRID; 4262894; 13.
DR   BioGRID; 850395; 5.
DR   ComplexPortal; CPX-5581; Nitrate reductase Z complex.
DR   DIP; DIP-10323N; -.
DR   IntAct; P19318; 14.
DR   STRING; 511145.b1467; -.
DR   TCDB; 5.A.3.1.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P19318; -.
DR   PaxDb; 511145-b1467; -.
DR   EnsemblBacteria; AAC74549; AAC74549; b1467.
DR   GeneID; 946034; -.
DR   KEGG; ecj:JW1462; -.
DR   KEGG; eco:b1467; -.
DR   PATRIC; fig|1411691.4.peg.801; -.
DR   EchoBASE; EB0641; -.
DR   eggNOG; COG1140; Bacteria.
DR   HOGENOM; CLU_043374_5_2_6; -.
DR   InParanoid; P19318; -.
DR   OMA; MAMRVYM; -.
DR   OrthoDB; 9779457at2; -.
DR   PhylomeDB; P19318; -.
DR   BioCyc; EcoCyc:NARY-MONOMER; -.
DR   BioCyc; MetaCyc:NARY-MONOMER; -.
DR   PHI-base; PHI:10517; -.
DR   PRO; PR:P19318; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0009325; C:nitrate reductase complex; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; ISM:EcoCyc.
DR   GO; GO:0051536; F:iron-sulfur cluster 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:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0042126; P:nitrate metabolic process; NAS:ComplexPortal.
DR   CDD; cd10557; NarH_beta-like; 1.
DR   Gene3D; 3.30.70.20; -; 3.
DR   Gene3D; 1.10.3650.10; nitrate reductase domain like; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR029263; Nitr_red_bet_C.
DR   InterPro; IPR038262; Nitr_red_bet_C_sf.
DR   InterPro; IPR006547; NO3_Rdtase_bsu.
DR   NCBIfam; TIGR01660; narH; 1.
DR   PANTHER; PTHR43518; NITRATE REDUCTASE BETA SUBUNIT; 1.
DR   PANTHER; PTHR43518:SF3; RESPIRATORY NITRATE REDUCTASE 2 BETA CHAIN; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF14711; Nitr_red_bet_C; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..514
FT                   /note="Respiratory nitrate reductase 2 beta chain"
FT                   /id="PRO_0000096734"
FT   DOMAIN          7..35
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          174..205
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          207..236
FT                   /note="4Fe-4S ferredoxin-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         16
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        325..326
FT                   /note="QR -> HG (in Ref. 1; CAA34965)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  58558 MW;  82D997DB093CD818 CRC64;
     MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TGREGMEYAW FNNVETKPGI GYPKNWEDQE
     EWQGGWVRDV NGKIRPRLGN KMGVITKIFA NPVVPQIDDY YEPFTFDYEH LHSAPEGKHI
     PTARPRSLID GKRMDKVIWG PNWEELLGGE FEKRARDRNF EAMQKEMYGQ FENTFMMYLP
     RLCEHCLNPS CVATCPSGAI YKREEDGIVL IDQDKCRGWR LCISGCPYKK IYFNWKSGKS
     EKCIFCYPRI ESGQPTVCSE TCVGRIRYLG VLLYDADRIE EAASTEREVD LYERQCEVFL
     DPHDPSVIEE ALKQGIPQNV IDAAQRSPVY KMAMDWKLAL PLHPEYRTLP MVWYVPPLSP
     IQSYADAGGL PKSEGVLPAI ESLRIPVQYL ANMLSAGDTG PVLRALKRMM AMRHYMRSQT
     VEGVTDTRAI DEVGLSVAQV EEMYRYLAIA NYEDRFVIPT SHREMAGDAF AERNGCGFTF
     GDGCHGSDSK FNLFNSSRID AINITEVRDK AEGE
//