RNFC_CLOLD
ID RNFC_CLOLD Reviewed; 457 AA.
AC D8GR66;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C {ECO:0000305};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000269|PubMed:23269825};
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, ECO:0000312|EMBL:ADK14204.1};
GN OrderedLocusNames=CLJU_c11360 {ECO:0000312|EMBL:ADK14204.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=23269825; DOI=10.1128/mbio.00406-12;
RA Tremblay P.L., Zhang T., Dar S.A., Leang C., Lovley D.R.;
RT "The Rnf complex of Clostridium ljungdahlii is a proton-translocating
RT ferredoxin:NAD+ oxidoreductase essential for autotrophic growth.";
RL MBio 4:E00406-E00412(2012).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane. Couples
CC electron transfer from reduced ferredoxin to NAD(+) with translocation
CC of H(+) out of the cell. Essential for energy conservation during
CC autotrophic growth. Contributes to ATP synthesis during heterotrophic
CC growth. {ECO:0000269|PubMed:23269825}.
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 complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00461}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00461};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00461}.
CC -!- INDUCTION: Up-regulated when grown on H(2)-CO(2).
CC {ECO:0000269|PubMed:23269825}.
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; CP001666; ADK14204.1; -; Genomic_DNA.
DR RefSeq; WP_013237801.1; NZ_LITS01000015.1.
DR AlphaFoldDB; D8GR66; -.
DR SMR; D8GR66; -.
DR STRING; 748727.CLJU_c11360; -.
DR EnsemblBacteria; ADK14204; ADK14204; CLJU_c11360.
DR KEGG; clj:CLJU_c11360; -.
DR PATRIC; fig|748727.19.peg.4236; -.
DR eggNOG; COG4656; Bacteria.
DR HOGENOM; CLU_010808_6_0_9; -.
DR OMA; QQLYWYS; -.
DR OrthoDB; 688908at2; -.
DR BRENDA; 7.1.1.11; 12866.
DR Proteomes; UP000001656; 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; 3.40.50.11540; -; 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 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 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Repeat; Translocase; Transport.
FT CHAIN 1..457
FT /note="Proton-translocating ferredoxin:NAD(+)
FT oxidoreductase complex subunit C"
FT /id="PRO_0000443487"
FT DOMAIN 353..386
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT DOMAIN 396..427
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT REGION 433..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365
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 368
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 371
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="2"
FT /evidence="ECO:0000255|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: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 415
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 457 AA; 49459 MW; 608CD7C3DD4974AB CRC64;
MLKSFRGGVH PDDSKKYTAN KPIEIAPIPD KVFIPVRQHI GAPTSPVVQK GDEVKKGQLI
AKSDAFVSAN IYASTSGKVV DIGDYPHPGF GKCQAIVIEK DGKDEWVEGI PTSRNWKELS
VKEMLGIIRE AGIVGMGGAT FPVHVKLAPP PDKKVDVFIL NGAECEPYLT ADYRSMLENS
DKVVAGVQII MKILNVEKAF VGIEDNKPKA IEAMKKAFEG TKVQVVGLPT KYPQGAEKML
INVLTGREVP SGGLPADVGA VVQNVGTCIA ISDAVERGIP LIQRVTTISG GAIKEPKNIL
VRIGTTFKDA IDFCGGFKEE PVKIISGGPM MGFAQSNLDI PIMKGSSGIL GLTKNDVNDG
KESSCIRCGR CLKACPMHLN PSMLSILGQK DLYQEAKEEY NLLDCVECGS CVYTCPAKRK
IVQYIRYLKS ENRAAGEREK AKAAKAKEKK EKEEVLK
