ID   RNFG_CLOLD              Reviewed;         185 AA.
AC   D8GR68;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G {ECO:0000305};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000269|PubMed:23269825};
DE   AltName: Full=Rnf electron transport complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
GN   Name=rnfG {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000312|EMBL:ADK14206.1};
GN   OrderedLocusNames=CLJU_c11380 {ECO:0000312|EMBL:ADK14206.1};
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   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00479};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00479}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00479};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00479}.
CC   -!- SIMILARITY: Belongs to the RnfG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00479}.
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DR   EMBL; CP001666; ADK14206.1; -; Genomic_DNA.
DR   RefSeq; WP_013237803.1; NZ_LITS01000015.1.
DR   AlphaFoldDB; D8GR68; -.
DR   SMR; D8GR68; -.
DR   STRING; 748727.CLJU_c11380; -.
DR   EnsemblBacteria; ADK14206; ADK14206; CLJU_c11380.
DR   KEGG; clj:CLJU_c11380; -.
DR   PATRIC; fig|748727.19.peg.4234; -.
DR   eggNOG; COG4659; Bacteria.
DR   HOGENOM; CLU_077882_2_1_9; -.
DR   OMA; PYIEANQ; -.
DR   OrthoDB; 1381933at2; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   HAMAP; MF_00479; RsxG_RnfG; 1.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR010209; Ion_transpt_RnfG/RsxG.
DR   PANTHER; PTHR36118; PTHR36118; 1.
DR   Pfam; PF04205; FMN_bind; 1.
DR   PIRSF; PIRSF006091; E_trnsport_RnfG; 1.
DR   SMART; SM00900; FMN_bind; 1.
DR   TIGRFAMs; TIGR01947; rnfG; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Flavoprotein; FMN; Membrane; NAD;
KW   Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..185
FT                   /note="Proton-translocating ferredoxin:NAD(+)
FT                   oxidoreductase complex subunit G"
FT                   /id="PRO_0000443497"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
FT   MOD_RES         161
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
SQ   SEQUENCE   185 AA;  19810 MW;  6E70D7E1C0E04F21 CRC64;
     MAKDKDQNSI FAITKNLTIT CFISGIIIAA VYYITSPVAA QKQVQIQNDT MRVLVNDADK
     FNKVNGKKDW YAAQKGNKTI AYVVPAESKG YGGAIELLVA VTPDGKVIDF SIVSHNETPG
     LGANASKDSF RGQFKDKKAD ALTVVKDKSN TKNIQAMTGA TITSKAVTKG VKEAVEQVTT
     FTGGK