ID   NARI_BACSU              Reviewed;         223 AA.
AC   P42177;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Nitrate reductase gamma chain;
DE            EC=1.7.5.1;
GN   Name=narI; OrderedLocusNames=BSU37250;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8846791; DOI=10.1002/j.1460-2075.1995.tb00287.x;
RA   Cruz Ramos H., Boursier L., Moszer I., Kunst F., Danchin A., Glaser P.;
RT   "Anaerobic transcription activation in Bacillus subtilis: identification of
RT   distinct FNR-dependent and -independent regulatory mechanisms.";
RL   EMBO J. 14:5984-5994(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA   Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA   Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA   Kunst F., Danchin A., Glaser P.;
RT   "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT   degrees).";
RL   Microbiology 143:3313-3328(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
RC   STRAIN=168 / JH642;
RX   PubMed=7557333; DOI=10.1111/j.1574-6968.1995.tb07780.x;
RA   Hoffmann T., Troup B., Szabo A., Hungerer C., Jahn D.;
RT   "The anaerobic life of Bacillus subtilis: cloning of the genes encoding the
RT   respiratory nitrate reductase system.";
RL   FEMS Microbiol. Lett. 131:219-225(1995).
CC   -!- FUNCTION: The gamma chain is a membrane-embedded heme-iron unit
CC       resembling cytochrome b, which transfers electrons from quinones to the
CC       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;
CC         Evidence={ECO:0000250|UniProtKB:P11350};
CC       Note=Binds 2 heme groups per subunit. Heme 1, called the proximal or
CC       heme Bp in, is located at the cytoplasmic interface, heme 2, called the
CC       distal or heme Bd, is located at the periplasmic interface. Electrons
CC       are transferred from the periplasmic to the cytoplasmic heme.
CC       {ECO:0000250|UniProtKB:P11350};
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR   EMBL; Z49884; CAA90048.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15753.1; -; Genomic_DNA.
DR   EMBL; X85014; CAA59374.1; -; Genomic_DNA.
DR   EMBL; X91819; CAA62929.1; -; Genomic_DNA.
DR   PIR; S60088; S60088.
DR   RefSeq; NP_391606.1; NC_000964.3.
DR   RefSeq; WP_003242665.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P42177; -.
DR   SMR; P42177; -.
DR   STRING; 224308.BSU37250; -.
DR   PaxDb; 224308-BSU37250; -.
DR   EnsemblBacteria; CAB15753; CAB15753; BSU_37250.
DR   GeneID; 938454; -.
DR   KEGG; bsu:BSU37250; -.
DR   PATRIC; fig|224308.179.peg.4036; -.
DR   eggNOG; COG2181; Bacteria.
DR   InParanoid; P42177; -.
DR   OrthoDB; 9788113at2; -.
DR   PhylomeDB; P42177; -.
DR   BioCyc; BSUB:BSU37250-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IBA:GO_Central.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IBA:GO_Central.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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:SF3; RESPIRATORY NITRATE REDUCTASE 1 GAMMA CHAIN; 1.
DR   Pfam; PF02665; Nitrate_red_gam; 1.
DR   SUPFAM; SSF103501; Respiratory nitrate reductase 1 gamma chain; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..223
FT                   /note="Nitrate reductase gamma chain"
FT                   /id="PRO_0000096722"
FT   TRANSMEM        2..27
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        28..45
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        46..68
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        69..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        82..111
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        112..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        124..147
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        148..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        181..196
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        197..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
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|UniProtKB:P11350"
FT   BINDING         64
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|UniProtKB:P11350"
FT   BINDING         185
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|UniProtKB:P11350"
FT   BINDING         203
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|UniProtKB:P11350"
SQ   SEQUENCE   223 AA;  25296 MW;  9C4379C5DF780000 CRC64;
     MSGQILWGIM PYIVLTIFIG GHIYRYQHDQ FGWTAKSSEL LEKKKLAAGS TLFHWGLLCV
     VGGHVMGILI PEGVYASLGI SEHMYHKMAI GAGLPAGIAA CTGLVILTYR RLFDKRIRKT
     SSPSDILTLL LLLFMMLSGV AATFLNIDSK GFDYRTTVGP WFREIVLFRP DASLMESVPL
     WFKFHIVIGY VVFILWPFTR LVHVFSLPLK YLTRSYVVYR KRS
//