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Database: UniProt
Entry: B2VEQ2
LinkDB: B2VEQ2
Original site: B2VEQ2 
ID   RNFB_ERWT9              Reviewed;         191 AA.
AC   B2VEQ2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   16-JAN-2019, entry version 69.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00463};
DE   AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
GN   Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463};
GN   OrderedLocusNames=ETA_17750;
OS   Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CIP 109463 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_00463}.
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: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00463}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC       RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
DR   EMBL; CU468135; CAO96821.1; -; Genomic_DNA.
DR   RefSeq; WP_012441510.1; NC_010694.1.
DR   SMR; B2VEQ2; -.
DR   STRING; 465817.ETA_17750; -.
DR   EnsemblBacteria; CAO96821; CAO96821; ETA_17750.
DR   KEGG; eta:ETA_17750; -.
DR   eggNOG; ENOG4108R3D; Bacteria.
DR   eggNOG; COG2878; LUCA.
DR   HOGENOM; HOG000262938; -.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   OrthoDB; 1619561at2; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005886; C:plasma 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   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; 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; Cell inner membrane; Cell membrane; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN         1    191       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_1000194473.
FT   DOMAIN       32     91       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      107    136       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      137    166       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   REGION        1     26       Hydrophobic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        52     52       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        57     57       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        74     74       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       116    116       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       119    119       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       122    122       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       126    126       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       146    146       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       149    149       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       152    152       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       156    156       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
SQ   SEQUENCE   191 AA;  20399 MW;  5EE1EFEC0D7F27D6 CRC64;
     MSAIWIAIAV LSALSLVFGG LLGYASRRFA VEEDPIVEQI DAILPQSQCG QCGYPGCRPY
     ADAVGNNGEM INKCAPGGEQ TMLKLAALLN VEPQPLGAEE AREPERKVAW IDEANCIGCT
     KCIQACPVDA IVGATRAMHT VLSDICTGCD LCVAPCPTDC IEMRPVATTT ANWKWDLHTI
     PVRVITVESH A
//
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