RNFA_RHOCB
ID RNFA_RHOCB Reviewed; 193 AA.
AC D5ARY9; Q07396;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit A {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
DE AltName: Full=Nitrogen fixation protein RnfA {ECO:0000305};
DE AltName: Full=Rnf electron transport complex subunit A {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
GN Name=rnfA {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000303|PubMed:9154934};
GN OrderedLocusNames=RCAP_rcc03287;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8199774;
RA Saeki K., Tokuda K., Fujiwara T., Matsubara H.;
RT "Nucleotide sequence and genetic analysis of the region essential for
RT functional expression of the gene for ferredoxin I, fdxN, in Rhodobacter
RT capsulatus: sharing of one upstream activator sequence in opposite
RT directions by two operons related to nitrogen fixation.";
RL Plant Cell Physiol. 34:185-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9154934; DOI=10.1021/bi970014q;
RA Kumagai H., Fujiwara T., Matsubara H., Saeki K.;
RT "Membrane localization, topology, and mutual stabilization of the rnfABC
RT gene products in Rhodobacter capsulatus and implications for a new family
RT of energy-coupling NADH oxidoreductases.";
RL Biochemistry 36:5509-5521(1997).
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. Necessary for stable
CC existence of both RnfB and RnfC (PubMed:9154934). {ECO:0000255|HAMAP-
CC Rule:MF_00459, ECO:0000269|PubMed:9154934}.
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00459}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000269|PubMed:9154934}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00459,
CC ECO:0000269|PubMed:9154934}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00459}.
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DR EMBL; D13625; BAA02788.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE87011.1; -; Genomic_DNA.
DR RefSeq; WP_013068983.1; NC_014034.1.
DR AlphaFoldDB; D5ARY9; -.
DR SMR; D5ARY9; -.
DR STRING; 272942.RCAP_rcc03287; -.
DR EnsemblBacteria; ADE87011; ADE87011; RCAP_rcc03287.
DR GeneID; 31492067; -.
DR KEGG; rcp:RCAP_rcc03287; -.
DR eggNOG; COG4657; Bacteria.
DR HOGENOM; CLU_095255_1_0_5; -.
DR OMA; CPFFGVS; -.
DR OrthoDB; 1814639at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00459; RsxA_RnfA; 1.
DR InterPro; IPR011293; Ion_transpt_RnfA/RsxA.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01943; rnfA; 1.
PE 1: Evidence at protein level;
KW Electron transport; Membrane; Nitrogen fixation; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..193
FT /note="Ion-translocating oxidoreductase complex subunit A"
FT /id="PRO_0000410700"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 25..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 60..70
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 92..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 123..133
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 155..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9154934"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT TOPO_DOM 192..193
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9154934"
SQ SEQUENCE 193 AA; 20424 MW; 2C4FE33A66290C3D CRC64;
MQDFLLVLLS TALVNNVVLV KFLGLCPFMG VSRKTDAAIG MGLATTFVIT VASAACWLVE
ALILEPLDLK FLRILSMILV IAAIVQFIET VMRKVTPDLH KALGIYLPLI TTNCAVLGLP
LMYIQGHLSL AMSTLSGFGA SVGFTLVLVI FAGMRERLAQ LSVPAAFAGT PIAFVSAGLL
GLAFMGFAGL VHV
