RNFB_METAC
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 03-AUG-2022, entry version 120.
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., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT 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 Methanosarcina
RT acetivorans involves a sodium-translocating Rnf 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 from the
RT 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 reductase.
CC Involved in heterodisulfide reduction during methanogenesis from
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_00463, ECO:0000305|PubMed:23066798}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00463,
CC ECO:0000269|PubMed:24836163}; Single-pass membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:24836163}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the rnf operon abolishes growth on
CC acetate and ferredoxin:heterodisulfide oxidoreductase-coupled Na(+)
CC transport. {ECO:0000269|PubMed:23066798}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
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DR EMBL; AE010299; AAM04106.1; -; Genomic_DNA.
DR RefSeq; WP_011020711.1; NC_003552.1.
DR AlphaFoldDB; Q8TSX9; -.
DR STRING; 188937.MA_0664; -.
DR TCDB; 3.D.6.1.3; the 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 HOGENOM; CLU_053470_0_0_2; -.
DR InParanoid; Q8TSX9; -.
DR OMA; MLPGANC; -.
DR OrthoDB; 111853at2157; -.
DR PhylomeDB; Q8TSX9; -.
DR BRENDA; 7.2.1.2; 7224.
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; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..264
FT /note="Ion-translocating oxidoreductase complex subunit B"
FT /id="PRO_0000443519"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 33..92
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 127..162
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 163..192
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 207..236
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 237..264
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 252
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="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
