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 27-MAR-2024, entry version 127.
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 SMR; 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 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 Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
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; IPR049684; Ion_transpt_RnfC_Methano.
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 NCBIfam; TIGR01945; rnfC; 1.
DR NCBIfam; NF041837; rnfC_Methano; 1.
DR PANTHER; PTHR43034; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR PANTHER; PTHR43034:SF2; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF13375; RnfC_N; 1.
DR Pfam; PF10531; SLBB; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 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
//
