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Database: UniProt
Entry: P42176
LinkDB: P42176
Original site: P42176 
ID   NARH_BACSU              Reviewed;         487 AA.
AC   P42176;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   10-APR-2019, entry version 133.
DE   RecName: Full=Nitrate reductase beta chain;
DE            EC=1.7.5.1;
GN   Name=narH; OrderedLocusNames=BSU37270;
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.,
RA   Glaser P.;
RT   "Anaerobic transcription activation in Bacillus subtilis:
RT   identification of distinct FNR-dependent and -independent regulatory
RT   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.,
RA   Villani G., 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 [GENOMIC DNA].
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
RT   encoding the respiratory nitrate reductase system.";
RL   FEMS Microbiol. Lett. 131:219-225(1995).
RN   [4]
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
CC   -!- FUNCTION: The beta chain is an electron transfer unit containing
CC       four cysteine clusters involved in the formation of iron-sulfur
CC       centers. Electrons are transferred from the gamma chain to the
CC       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;
CC         EC=1.7.5.1;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P11349};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:P11349};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250|UniProtKB:P11349};
CC       Note=Binds 1 [3Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P11349};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
DR   EMBL; Z49884; CAA90046.1; -; Genomic_DNA.
DR   EMBL; X91819; CAA62927.1; -; Genomic_DNA.
DR   EMBL; X85014; CAA59372.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15755.1; -; Genomic_DNA.
DR   PIR; S60086; S60573.
DR   RefSeq; NP_391608.1; NC_000964.3.
DR   RefSeq; WP_003244173.1; NZ_JNCM01000034.1.
DR   ProteinModelPortal; P42176; -.
DR   SMR; P42176; -.
DR   STRING; 224308.BSU37270; -.
DR   jPOST; P42176; -.
DR   PaxDb; P42176; -.
DR   PRIDE; P42176; -.
DR   EnsemblBacteria; CAB15755; CAB15755; BSU37270.
DR   GeneID; 937047; -.
DR   KEGG; bsu:BSU37270; -.
DR   PATRIC; fig|224308.179.peg.4038; -.
DR   eggNOG; ENOG4108IUE; Bacteria.
DR   eggNOG; COG1140; LUCA.
DR   HOGENOM; HOG000237353; -.
DR   InParanoid; P42176; -.
DR   KO; K00371; -.
DR   OMA; VYFNWQT; -.
DR   PhylomeDB; P42176; -.
DR   BioCyc; BSUB:BSU37270-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd10557; NarH_beta-like; 1.
DR   Gene3D; 1.10.3650.10; -; 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   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF14711; Nitr_red_bet_C; 1.
DR   TIGRFAMs; TIGR01660; narH; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome; Electron transport;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Nitrate assimilation;
KW   Oxidoreductase; Reference proteome; Repeat; Transport.
FT   CHAIN         1    487       Nitrate reductase beta chain.
FT                                /FTId=PRO_0000096719.
FT   DOMAIN        7     36       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      172    203       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      205    234       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        16     16       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL        22     22       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL        26     26       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       181    181       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       184    184       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       189    189       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       193    193       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       214    214       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       220    220       Iron-sulfur 4 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       224    224       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       241    241       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       244    244       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       256    256       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   METAL       260    260       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P11349}.
FT   CONFLICT     21     21       T -> A (in Ref. 3; CAA62927/CAA59372).
FT                                {ECO:0000305}.
FT   CONFLICT    174    174       M -> I (in Ref. 3; CAA62927/CAA59372).
FT                                {ECO:0000305}.
SQ   SEQUENCE   487 AA;  55472 MW;  7BCE6F32CC4F4283 CRC64;
     MKIKAQIGMV MNLDKCIGCH TCSVTCKNTW TNRSGAEYMY FNNVETKPGI GYPKQWEDQD
     KYKGGWTLKK GKLELKSGSK TNRLAGLFYN PNQPSIDDYY EPWNYDYETL TNSPQKKHQP
     VARPKSSLTG DFMNIEWGPN WEDDLAGGHI TGLEDPNVQK MEESIKTEFD DVFMMYLPRI
     CEHCINPACV SSCPSGAMYK REEDGIVLVD QNACRSWRYC VSSCPYKKVY FNWQTNKAEK
     CTLCFPRLEA GLPTICSETC VGRIRYLGVM LYDADKVEEA ASVENEKDLY HSQLDVFLDP
     NDPEVAKLAK EQGIPAEWIE AAQQSPIYKM IIDWKIALPL HPEYRTLPMV WYIPPLSPIM
     NLFEGKGSRQ TAEDIFPAID QMRIPIDYLA QLLTAGDTDH IRSTLKKMSV MRQYMRAVQT
     NKSIDPELIS SVGLTEQQIE DMYRLLAIAK YDDRFVIPSS HREEVSDLYA EQGSCGLSFS
     GGPGSCF
//
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