RNFE_CLOLD
ID RNFE_CLOLD Reviewed; 213 AA.
AC D8GR69;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E {ECO:0000305};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000269|PubMed:23269825};
DE AltName: Full=Rnf electron transport complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000305};
GN Name=rnfE {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000312|EMBL:ADK14207.1};
GN OrderedLocusNames=CLJU_c11390 {ECO:0000312|EMBL:ADK14207.1};
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.
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 -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00478}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00478};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00478}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00478}.
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DR EMBL; CP001666; ADK14207.1; -; Genomic_DNA.
DR RefSeq; WP_013237804.1; NZ_LITS01000015.1.
DR AlphaFoldDB; D8GR69; -.
DR SMR; D8GR69; -.
DR STRING; 748727.CLJU_c11390; -.
DR EnsemblBacteria; ADK14207; ADK14207; CLJU_c11390.
DR KEGG; clj:CLJU_c11390; -.
DR PATRIC; fig|748727.19.peg.4233; -.
DR eggNOG; COG4660; Bacteria.
DR HOGENOM; CLU_046659_1_1_9; -.
DR OMA; DGFMMGL; -.
DR OrthoDB; 1782047at2; -.
DR BRENDA; 7.1.1.11; 12866.
DR Proteomes; UP000001656; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00478; RsxE_RnfE; 1.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR InterPro; IPR010968; RnfE.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01948; rnfE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Membrane; NAD; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..213
FT /note="Proton-translocating ferredoxin:NAD(+)
FT oxidoreductase complex subunit E"
FT /id="PRO_0000443494"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
SQ SEQUENCE 213 AA; 22910 MW; 21FCE2D0A405A463 CRC64;
MKNLWNIFKK GLIAENPIFV LALSLCPALA TTSTAVNGFT MGICVLFVIT CNNTVVSIIK
NVVNPKVRVP VYITCIATIV TVVELVMQAY APLLYKQLGI YLALVVVFAI ILARAETFAS
KNPVVPSFFD GLGMGCGFTL ALTIIGMIRE LFGSGAIFGV NVFGASYNPA LIMILPPGGF
ILIGYLVAIV KVYNQHMEKI KMQKLEKANG GEA