ID   NASB_BACSU              Reviewed;         771 AA.
AC   P42433;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Assimilatory nitrate reductase electron transfer subunit;
GN   Name=nasB; Synonyms=nasBA; OrderedLocusNames=BSU03320;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=7868621; DOI=10.1128/jb.177.5.1409-1413.1995;
RA   Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P.,
RA   Nakano M.M.;
RT   "The nasB operon and nasA gene are required for nitrate/nitrite
RT   assimilation in Bacillus subtilis.";
RL   J. Bacteriol. 177:1409-1413(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
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   SEQUENCE REVISION TO 363-364 AND 716.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   INDUCTION BY TNRA.
RC   STRAIN=168;
RX   PubMed=10864496; DOI=10.1006/jmbi.2000.3846;
RA   Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
RT   "Purification and in vitro activities of the Bacillus subtilis TnrA
RT   transcription factor.";
RL   J. Mol. Biol. 300:29-40(2000).
RN   [6]
RP   INDUCTION BY TNRA.
RX   PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA   Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT   "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT   associated with a TnrA box.";
RL   Mol. Microbiol. 49:157-165(2003).
CC   -!- FUNCTION: Required for nitrate assimilation.
CC       {ECO:0000269|PubMed:7868621}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC       conditions. {ECO:0000269|PubMed:10864496, ECO:0000269|PubMed:12823818}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D30689; BAA06352.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08966.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12126.2; -; Genomic_DNA.
DR   PIR; I40027; I40027.
DR   RefSeq; NP_388214.2; NC_000964.3.
DR   RefSeq; WP_003246389.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; P42433; -.
DR   SMR; P42433; -.
DR   STRING; 224308.BSU03320; -.
DR   PaxDb; P42433; -.
DR   PRIDE; P42433; -.
DR   EnsemblBacteria; CAB12126; CAB12126; BSU_03320.
DR   GeneID; 938328; -.
DR   KEGG; bsu:BSU03320; -.
DR   PATRIC; fig|224308.179.peg.346; -.
DR   eggNOG; COG1251; Bacteria.
DR   InParanoid; P42433; -.
DR   OMA; ETICQCN; -.
DR   PhylomeDB; P42433; -.
DR   BioCyc; BSUB:BSU03320-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1100; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.30.413.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   Pfam; PF04324; Fer2_BFD; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   SUPFAM; SSF56014; SSF56014; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; FAD; Flavoprotein; NADP; Nitrate assimilation;
KW   Reference proteome; Transport.
FT   CHAIN           1..771
FT                   /note="Assimilatory nitrate reductase electron transfer
FT                   subunit"
FT                   /id="PRO_0000096736"
FT   BINDING         43..79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        363..364
FT                   /note="AG -> R (in Ref. 1; BAA06352 and 2; BAA08966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        716
FT                   /note="A -> D (in Ref. 1; BAA06352 and 2; BAA08966)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   771 AA;  84682 MW;  559C372EFD00AD32 CRC64;
     MKKQRLVLAG NGMAGIRCIE EVLKLNRHMF EIVIFGSEPH PNYNRILLSS VLQGEASLDD
     ITLNSKDWYD KHGITLYTGE TVIQIDTDQQ QVITDRKRTL SYDKLIVATG SSPHILPIPG
     ADKKGVYGFR TIEDCQALMN MAQHFQKAAV IGAGLLGLEA AVGLQHLGMD VSVIHHSAGI
     MQKQLDQTAA RLLQTELEQK GLTFLLEKDT VSISGATKAD RIHFKDGSSL KADLIVMAAG
     VKPNIELAVS AGIKVNRGII VNDFMQTSEP NIYAVGECAE HNGTVYGLVA PLYEQGKALA
     SHICGVPCEE YQGSAPSAAL KIAGIDVWSA GKIQEDERTT SIKIYDEQAG VYKKALFVDD
     KLAGVILFGD TRDKQRLLDS LLKQRDISIA KKQIIEPETS GPLFESMPSS ETICQCNTVT
     KGAIEDAVHT NSLTTVEEVK HCTKATGSCG GCKPLVEDLL RYMTNSEYTK PASTPSFCSC
     TDFTEDDIIA ELQRRPFTNP AEVMNQLDWK TKNGCSTCVP AIQYYLEMLY PGFVQPEPAT
     EETCILIPQM YGGRTNAEQL RTIANIIEAY SIPDVSITHG QRLKLSGIKP ADLPNMKKDL
     KMPVYTNEHR HALQSIKACT CGQNRSIQQL AAQIERQLEM LPLPAPISIS LSCETDCTEA
     ALQDVGAIRT QAGWDIHIGG VRGTHARSGA LFCVTENEDS TAGMIKGLIQ YYRETAHYLE
     GVHQWIDRLG IVHIREVLFE EDLRAQLLES LQTDLSLIQN PTVETGAYKK G