RNFG_RHOCA
ID RNFG_RHOCA Reviewed; 217 AA.
AC P97054; Q52714;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305};
DE AltName: Full=Nitrogen fixation protein RnfG {ECO:0000305};
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:0000303|PubMed:9492268};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=B10S;
RX PubMed=8264535; DOI=10.1007/bf00279903;
RA Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA Schuppler M., Marxer M., Oelze J., Klipp W.;
RT "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT capsulatus: a putative membrane complex involved in electron transport to
RT nitrogenase.";
RL Mol. Gen. Genet. 241:602-615(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9492268; DOI=10.1046/j.1432-1327.1998.2510054.x;
RA Jouanneau Y., Jeong H.-S., Hugo N., Meyer C., Willison J.C.;
RT "Overexpression in Escherichia coli of the rnf genes from Rhodobacter
RT capsulatus -- characterization of two membrane-bound iron-sulfur
RT proteins.";
RL Eur. J. Biochem. 251:54-64(1998).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane (By
CC similarity). Required for nitrogen fixation. Involved in electron
CC transfer to nitrogenase (PubMed:8264535). {ECO:0000255|HAMAP-
CC Rule:MF_00479, ECO:0000269|PubMed:8264535}.
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 ECO:0000305|PubMed:9492268}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000255|HAMAP-Rule:MF_00479, ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00479}.
CC -!- INDUCTION: Expression is reduced under iron-limiting conditions.
CC {ECO:0000269|PubMed:9492268}.
CC -!- SIMILARITY: Belongs to the RnfG family. {ECO:0000255|HAMAP-
CC Rule:MF_00479}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51397.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X72888; CAA51397.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Y11913; CAA72665.1; -; Genomic_DNA.
DR RefSeq; WP_013068987.1; NZ_VIBE01000016.1.
DR AlphaFoldDB; P97054; -.
DR SMR; P97054; -.
DR TCDB; 3.D.6.1.1; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR GeneID; 31492071; -.
DR OMA; YSGAIHL; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Electron transport; Flavoprotein; FMN; Membrane; Nitrogen fixation;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..217
FT /note="Ion-translocating oxidoreductase complex subunit G"
FT /id="PRO_0000214639"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
FT MOD_RES 185
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00479"
FT CONFLICT 50..52
FT /note="ARG -> PR (in Ref. 1; CAA51397)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="T -> P (in Ref. 1; CAA51397)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="V -> G (in Ref. 1; CAA51397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 22847 MW; 5E5FDD74CCC7E342 CRC64;
MTDTPPPEKP KLPWFKASPL AHGIMLAMFA LVTAVLLAVA NDSTSAPIAA RGAEDLAASL
EQVIPHDLHD NDLAAAMRPV SDAEEGTIKV YVATKAGAVT GLAYELSGPG YSGQIRVLLG
IAPDGTLLGV RVLSHTETPG LGDKIEVAKD DWILGFAGKS LADPEPGHWK VKRDGGVFDQ
FSGATITPRA VVKTIYRGLM FFDRNKAALT APLPPKS
