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RNFC_METAC
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   03-AUG-2022, entry version 121.
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., 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).
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_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. {ECO:0000255|HAMAP-
CC       Rule:MF_00461, ECO:0000305|PubMed:23066798}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00461};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00461}.
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. RnfC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
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DR   EMBL; AE010299; AAM04101.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TSY4; -.
DR   STRING; 188937.MA_0659; -.
DR   TCDB; 3.D.6.1.3; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   EnsemblBacteria; AAM04101; AAM04101; MA_0659.
DR   KEGG; mac:MA_0659; -.
DR   HOGENOM; CLU_010808_6_0_2; -.
DR   InParanoid; Q8TSY4; -.
DR   OMA; YPMGSEK; -.
DR   OrthoDB; 13364at2157; -.
DR   PhylomeDB; Q8TSY4; -.
DR   BRENDA; 7.2.1.2; 7224.
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   HAMAP; MF_00461; RsxC_RnfC; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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   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; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..447
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_0000443489"
FT   DOMAIN          359..389
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   DOMAIN          399..430
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         369
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         372
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         375
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         379
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         408
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         411
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         414
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         418
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="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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