NARI_BACSU
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 03-AUG-2022, entry version 130.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8846791;
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; P42177; -.
DR PRIDE; P42177; -.
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 OMA; MVSGGFF; -.
DR PhylomeDB; P42177; -.
DR BioCyc; BSUB:BSU37250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR InterPro; IPR003816; Nitrate_red_gam.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
DR TIGRFAMs; TIGR00351; narI; 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
