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Database: UniProt
Entry: D5ARZ0
LinkDB: D5ARZ0
Original site: D5ARZ0 
ID   RNFB_RHOCB              Reviewed;         187 AA.
AC   D5ARZ0; O08056; Q07394;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 47.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
DE   AltName: Full=Nitrogen fixation protein RnfB {ECO:0000305};
DE   AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
GN   Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463,
GN   ECO:0000303|PubMed:9154934}; OrderedLocusNames=RCAP_rcc03288;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=8199774;
RA   Saeki K., Tokuda K., Fujiwara T., Matsubara H.;
RT   "Nucleotide sequence and genetic analysis of the region essential for
RT   functional expression of the gene for ferredoxin I, fdxN, in
RT   Rhodobacter capsulatus: sharing of one upstream activator sequence in
RT   opposite directions by two operons related to nitrogen fixation.";
RL   Plant Cell Physiol. 34:185-199(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur
RT   bacterium Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=9154934; DOI=10.1021/bi970014q;
RA   Kumagai H., Fujiwara T., Matsubara H., Saeki K.;
RT   "Membrane localization, topology, and mutual stabilization of the
RT   rnfABC gene products in Rhodobacter capsulatus and implications for a
RT   new family of energy-coupling NADH oxidoreductases.";
RL   Biochemistry 36:5509-5521(1997).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane (By
CC       similarity). Required for nitrogen fixation. Stabilizes RnfC
CC       (PubMed:9154934). {ECO:0000255|HAMAP-Rule:MF_00463,
CC       ECO:0000269|PubMed:9154934}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00463};
CC       Note=Binds 3 [4Fe-4S] clusters. {ECO:0000255|HAMAP-Rule:MF_00463};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB,
CC       RnfC, RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00463}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000269|PubMed:9154934};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00463,
CC       ECO:0000269|PubMed:9154934}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_00463, ECO:0000269|PubMed:9154934}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC       RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
DR   EMBL; D13625; BAA02787.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE87012.1; -; Genomic_DNA.
DR   RefSeq; WP_013068984.1; NC_014034.1.
DR   ProteinModelPortal; D5ARZ0; -.
DR   SMR; D5ARZ0; -.
DR   STRING; 272942.RCAP_rcc03288; -.
DR   EnsemblBacteria; ADE87012; ADE87012; RCAP_rcc03288.
DR   GeneID; 31492068; -.
DR   KEGG; rcp:RCAP_rcc03288; -.
DR   eggNOG; ENOG4108R3D; Bacteria.
DR   eggNOG; COG2878; LUCA.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; RCAP272942:G1GUE-3272-MONOMER; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.20; -; 1.
DR   HAMAP; MF_00463; RsxB_RnfB; 1.
DR   InterPro; IPR007202; 4Fe-4S_dom.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB.
DR   InterPro; IPR016463; RnfB/RsxB_Proteobac.
DR   PANTHER; PTHR42859:SF3; PTHR42859:SF3; 1.
DR   Pfam; PF04060; FeS; 1.
DR   PIRSF; PIRSF005784; Elect_transpt_RnfB; 1.
DR   TIGRFAMs; TIGR01944; rnfB; 1.
DR   PROSITE; PS51656; 4FE4S; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Nitrogen fixation; Reference proteome;
KW   Repeat; Translocase; Transport.
FT   CHAIN         1    187       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_0000410701.
FT   DOMAIN       29     88       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      103    132       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      133    162       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   REGION        1     23       Hydrophobic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   METAL        46     46       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        54     54       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        71     71       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       112    112       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       115    115       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       118    118       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       122    122       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       142    142       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       145    145       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       148    148       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       152    152       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
SQ   SEQUENCE   187 AA;  19090 MW;  93965D368FC63D3F CRC64;
     MIAAAASMSA LGLGLGYLLG AAARKFHVET PPIVEEIAKI LPGTNCGACG FPGCNGLAEA
     MAEGNAPVTA CTPGGRDVAL ALAEIVTVEA GADAGPIAEI EPMVAFVFED HCTGCQKCFK
     RCPTDAIVGG AKQIHTVVMD ACIGCDACIE VCPTEAIVSR VKPKTLKTWY WDKPQPGLVA
     ASAETAA
//
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