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Database: UniProt
Entry: R6U770_9FIRM
LinkDB: R6U770_9FIRM
Original site: R6U770_9FIRM 
ID   R6U770_9FIRM            Unreviewed;       434 AA.
AC   R6U770;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
DE            EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00461};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
GN   Name=rnfC {ECO:0000256|HAMAP-Rule:MF_00461};
GN   ORFNames=BN714_02028 {ECO:0000313|EMBL:CDC66652.1};
OS   Ruminococcus sp. CAG:57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262962 {ECO:0000313|EMBL:CDC66652.1, ECO:0000313|Proteomes:UP000018131};
RN   [1] {ECO:0000313|EMBL:CDC66652.1, ECO:0000313|Proteomes:UP000018131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:57 {ECO:0000313|Proteomes:UP000018131};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00461};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00461};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDC66652.1}.
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DR   EMBL; CBFS010000155; CDC66652.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6U770; -.
DR   Proteomes; UP000018131; Unassembled WGS sequence.
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; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 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; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR026902; RnfC_N.
DR   NCBIfam; TIGR01945; rnfC; 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   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_00461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00461}; Membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00461}; Reference proteome {ECO:0000313|Proteomes:UP000018131};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00461}.
FT   DOMAIN          357..386
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          396..426
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         366
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         376
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         405
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         415
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ   SEQUENCE   434 AA;  46883 MW;  F0DD89DFC2530897 CRC64;
     MKLNSIFLSH KKGTENSETI AMPLPARVKI SMSQHMGAPC EPTVAKGDRV LVGQVIGESN
     AFMSCPVHSS VSGTVAAISE LLTAGGKVCK MVEIDTDGEQ EVSPDVKPPV ITDKASLCEA
     VRQSGCCGMG GAGFPTHIKL NFDENKYKVD TLVINAAECE PYITSDYREM MENADDVMCG
     IKLVRDMLGL KKVVIGIEDN KPQAIKLMRE KSADDESIEV KVLKSCYPQG AEKVIIFNTT
     GRAVGEGQLP SDQGVIVMNV TTAGFIGEYS KTGMPLISKR ITVDGDVVST PCNVKVPIGT
     SAEDILKFGD CDKEKVRKAL FGGPMMGMCL YELDTPVTKT TNAILAFGEK ADKKKGIEDR
     CAQTNCIKCG RCISACPLNL MPTELEKAYD RRDKEALMKL KVGLCMNCGS CSYVCPAKRD
     LAEKNQLAKA FIRT
//
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