RNFG_METAC
ID RNFG_METAC Reviewed; 188 AA.
AC Q8TSY2;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
DE EC=7.2.1.- {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
DE AltName: Full=Rnf electron transport complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
GN Name=rnfG {ECO:0000255|HAMAP-Rule:MF_00479};
GN OrderedLocusNames=MA_0661 {ECO:0000312|EMBL:AAM04103.1};
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 SUBCELLULAR LOCATION, TOPOLOGY, PROSTHETIC GROUP AT THR-166, AND
RP MUTAGENESIS OF THR-166.
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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00479};
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_00479, ECO:0000305|PubMed:23066798}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00479,
CC ECO:0000269|PubMed:24836163}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00479}.
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 RnfG family. {ECO:0000255|HAMAP-
CC Rule:MF_00479}.
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DR EMBL; AE010299; AAM04103.1; -; Genomic_DNA.
DR RefSeq; WP_011020708.1; NC_003552.1.
DR AlphaFoldDB; Q8TSY2; -.
DR SMR; Q8TSY2; -.
DR STRING; 188937.MA_0661; -.
DR TCDB; 3.D.6.1.3; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR EnsemblBacteria; AAM04103; AAM04103; MA_0661.
DR GeneID; 1472553; -.
DR KEGG; mac:MA_0661; -.
DR HOGENOM; CLU_077882_2_2_2; -.
DR InParanoid; Q8TSY2; -.
DR OMA; PYIEANQ; -.
DR OrthoDB; 105359at2157; -.
DR PhylomeDB; Q8TSY2; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR HAMAP; MF_00479; RsxG_RnfG; 1.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR010209; Ion_transpt_RnfG/RsxG.
DR PANTHER; PTHR36118; PTHR36118; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR PIRSF; PIRSF006091; E_trnsport_RnfG; 1.
DR SMART; SM00900; FMN_bind; 1.
DR TIGRFAMs; TIGR01947; rnfG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Flavoprotein; FMN; Membrane;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..188
FT /note="Ion-translocating oxidoreductase complex subunit G"
FT /id="PRO_0000443498"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24836163"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
FT TOPO_DOM 31..188
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24836163"
FT MOD_RES 166
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479,
FT ECO:0000269|PubMed:24836163"
FT MUTAGEN 166
FT /note="T->G: Abolishes flavin binding."
FT /evidence="ECO:0000269|PubMed:24836163"
SQ SEQUENCE 188 AA; 19664 MW; 04F9FC3158A681D7 CRC64;
MSDSKEITKV IVTMVVISAV AAALLALTYT PTQAQLKLLQ AEQQKEAMKE ILPQAADFEP
VTGSEVDDDG NPVVLYYKGV DSSGNVVGYV VERNQVGAQG MIQLLAGISS DFSTITGFQV
MKHSETPGLG ALITTPEFQG QFVDLPVADT SLTKNGGQVD AISGATISSQ AVVDALHSAV
DYVSAQEG
