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Database: UniProt
Entry: Q8TSY4
LinkDB: Q8TSY4
Original site: Q8TSY4 
ID   RNFC_METAC              Reviewed;         447 AA.
AC   Q8TSY4;
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 C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE            EC=7.2.1.- {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
GN   Name=rnfC {ECO:0000255|HAMAP-Rule:MF_00461};
GN   OrderedLocusNames=MA_0659 {ECO:0000312|EMBL:AAM04101.1};
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).
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_00461};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00461};
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_00461, ECO:0000305|PubMed:23066798}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00461}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00461}.
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       RnfC subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
DR   EMBL; AE010299; AAM04101.1; -; Genomic_DNA.
DR   RefSeq; WP_011020706.1; NC_003552.1.
DR   ProteinModelPortal; Q8TSY4; -.
DR   TCDB; 3.D.6.1.3; the putative ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   EnsemblBacteria; AAM04101; AAM04101; MA_0659.
DR   GeneID; 1472551; -.
DR   KEGG; mac:MA_0659; -.
DR   eggNOG; arCOG06548; Archaea.
DR   eggNOG; COG4656; LUCA.
DR   InParanoid; Q8TSY4; -.
DR   KO; K03615; -.
DR   OMA; FGGPMMG; -.
DR   OrthoDB; 13364at2157; -.
DR   PhylomeDB; Q8TSY4; -.
DR   BioCyc; MACE188937:G1FZT-701-MONOMER; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   HAMAP; MF_00461; RsxC_RnfC; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR010208; Ion_transpt_RnfC/RsxC.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR026902; RnfC_N.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   PANTHER; PTHR43034; PTHR43034; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF13375; RnfC_N; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SUPFAM; SSF142019; SSF142019; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR01945; rnfC; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Transport.
FT   CHAIN         1    447       Ion-translocating oxidoreductase complex
FT                                subunit C.
FT                                /FTId=PRO_0000443489.
FT   DOMAIN      359    389       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   DOMAIN      399    430       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       369    369       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       372    372       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       375    375       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       379    379       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       408    408       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       411    411       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       414    414       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       418    418       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
SQ   SEQUENCE   447 AA;  48477 MW;  78FEBC0065765656 CRC64;
     MKRSLHSKEV ANLSDVIKID KLPEKAIIPM RQHDGIACAP LVKKGAEVIV GQKLGECEGS
     DLAYVHSPFC GTVNSIELMP NPSGKRILSV VLTPSECAQT VDFVPEKDAP PSRLIEIIKE
     AGIVEYYEKP TYLALKPGKR IDTLLMNATF PLITHAYLSS LDKVLEGFKL MLEASGISRG
     VIVLRADDKE SIKAFKNAKV DGKPLTVAPI VGMRHADYYL EDVEDQIIVV AAGKITYTPT
     MMNLLSANVM GRKLPLGYEP PDVHVVVCGV KSAKAVYDAI NEGKPYLESA VTVTGAVNNP
     KTVIVKFGTP IKDVIEACGG YKGEPGKVIV NGSMGGVAVY TDEAPVVKNT VGIVVQTEAE
     VLRDEATVCI HCARCVDVCP MNLLPGRIAA MADMGMFDRC REYFALNCIE CGECAVVCPA
     KRHLVQLIRY SKLQIMNQKN ETVEATE
//
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