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Database: UniProt
Entry: Q8TSX9
LinkDB: Q8TSX9
Original site: Q8TSX9 
ID   RNFB_METAC              Reviewed;         264 AA.
AC   Q8TSX9;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
DE            EC=7.2.1.- {ECO:0000255|HAMAP-Rule:MF_00463, 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   OrderedLocusNames=MA_0664 {ECO:0000312|EMBL:AAM04106.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=23066798; DOI=10.1111/febs.12031;
RA   Schlegel K., Welte C., Deppenmeier U., Mueller V.;
RT   "Electron transport during aceticlastic methanogenesis by
RT   Methanosarcina acetivorans involves a sodium-translocating Rnf
RT   complex.";
RL   FEBS J. 279:4444-4452(2012).
RN   [3]
RP   COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=24836163; DOI=10.1371/journal.pone.0097966;
RA   Suharti S., Wang M., de Vries S., Ferry J.G.;
RT   "Characterization of the RnfB and RnfG subunits of the Rnf complex
RT   from the archaeon Methanosarcina acetivorans.";
RL   PLoS ONE 9:E97966-E97966(2014).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane. Catalyzes
CC       Na(+) transport, most probably coupled to electron transfer from
CC       reduced ferredoxin to methanophenazine and heterodisulfide
CC       reductase. Involved in heterodisulfide reduction during
CC       methanogenesis from acetate. {ECO:0000269|PubMed:23066798}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00463,
CC         ECO:0000305|PubMed:24836163};
CC       Note=Binds 5 [4Fe-4S] clusters. {ECO:0000305};
CC   -!- SUBUNIT: The Rnf complex is probably composed of eight subunits,
CC       including RnfA, RnfB, RnfC, RnfD, RnfE and RnfG.
CC       {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305|PubMed:23066798}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00463, ECO:0000269|PubMed:24836163}; Single-pass membrane
CC       protein {ECO:0000255, ECO:0000269|PubMed:24836163}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the rnf operon abolishes growth
CC       on acetate and ferredoxin:heterodisulfide oxidoreductase-coupled
CC       Na(+) transport. {ECO:0000269|PubMed:23066798}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC       RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
DR   EMBL; AE010299; AAM04106.1; -; Genomic_DNA.
DR   RefSeq; WP_011020711.1; NC_003552.1.
DR   ProteinModelPortal; Q8TSX9; -.
DR   SMR; Q8TSX9; -.
DR   TCDB; 3.D.6.1.3; the putative ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   EnsemblBacteria; AAM04106; AAM04106; MA_0664.
DR   GeneID; 1472556; -.
DR   KEGG; mac:MA_0664; -.
DR   eggNOG; arCOG02186; Archaea.
DR   eggNOG; COG2878; LUCA.
DR   InParanoid; Q8TSX9; -.
DR   KO; K03616; -.
DR   OMA; MLPGANC; -.
DR   OrthoDB; 111853at2157; -.
DR   PhylomeDB; Q8TSX9; -.
DR   BioCyc; MACE188937:G1FZT-706-MONOMER; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF04060; FeS; 1.
DR   TIGRFAMs; TIGR01944; rnfB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51656; 4FE4S; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    264       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_0000443519.
FT   TRANSMEM      5     25       Helical. {ECO:0000255}.
FT   DOMAIN       33     92       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      127    162       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      163    192       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      207    236       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      237    264       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        50     50       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        53     53       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        75     75       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       138    138       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       142    142       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       148    148       Iron-sulfur 2 (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       172    172       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       175    175       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       178    178       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       182    182       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       217    217       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       220    220       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       223    223       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       227    227       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       246    246       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       249    249       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       252    252       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       256    256       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   264 AA;  27352 MW;  693976388A3BEEDD CRC64;
     MSSVLINSIA VLAGLGFAVG VMLVIASKVF KIDSNPLIDD VASLLPGANC GGCGFAGCAA
     CAEAIVEQGA PVNSCPVGGF EVAKQIGALL GQEVTESEKE FPFVRCQGGN QHCTTLYDYH
     GVENCKVALM LCDSRKGCTY GCLGLGTCVQ ACQFGALSMG EDGFPVVNKA LCTSCGNCIA
     ACPNGVLTFA RDSEKVHVLC RSHDKGKDVK AVCEVGCIGC KKCEKECPAG AIRVTEFLAE
     IDQEKCTACG ACVAICPQKA IELR
//
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