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RNFC_RHOCB
ID   RNFC_RHOCB              Reviewed;         519 AA.
AC   D5ARZ1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE   AltName: Full=Nitrogen fixation protein RnfC {ECO:0000305};
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:0000303|PubMed:9154934};
GN   OrderedLocusNames=RCAP_rcc03289;
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 [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   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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. Stabilizes RnfB
CC       (PubMed:9154934). {ECO:0000255|HAMAP-Rule:MF_00461,
CC       ECO:0000269|PubMed:9154934}.
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: Cellular chromatophore membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000269|PubMed:9154934};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00461,
CC       ECO:0000269|PubMed:9154934}.
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; CP001312; ADE87013.1; -; Genomic_DNA.
DR   RefSeq; WP_013068985.1; NC_014034.1.
DR   AlphaFoldDB; D5ARZ1; -.
DR   SMR; D5ARZ1; -.
DR   STRING; 272942.RCAP_rcc03289; -.
DR   PRIDE; D5ARZ1; -.
DR   EnsemblBacteria; ADE87013; ADE87013; RCAP_rcc03289.
DR   GeneID; 31492069; -.
DR   KEGG; rcp:RCAP_rcc03289; -.
DR   eggNOG; COG4656; Bacteria.
DR   HOGENOM; CLU_010808_6_2_5; -.
DR   OMA; YPMGSEK; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore 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   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Nitrogen fixation; Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..519
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_0000410721"
FT   DOMAIN          372..401
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   DOMAIN          411..440
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   REGION          494..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         381
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         384
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         387
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         391
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         420
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         423
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         426
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         430
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   519 AA;  55588 MW;  E5451EB2A3FA6026 CRC64;
     MRLPSIATLF HPLQSFSIRG GIHPETHKHL TSECEIETMP MPALIRLPLQ QHIGAEAEPI
     VKRDDLVLKG QLIAKARGPL SANIHAPTSG RVIAVGHFVA PHASGLPVPT ITIRPDGEDK
     WGPHLPRLRP ENAAPEEIAA QVAAAGIVGM GGATFPSAVK LNLRAKYDLT TLIINGAECE
     PYLTCDDRLM RERAEEIADG IGIMARALGV KQVFVAIESN KPQAIEAMTR YNRALGYTFK
     IHVVPTQYPM GSEKHLVKMI TGQETPARAL TADLGVVVHN IATAHAVHLA VRYGEPLIAR
     TVTVSGHGIR RPANLRVLIG TPVSEIIAHC GGFTEEPDRL LLGGPMMGMP IQNPRVPVVK
     GTNGILALTA AETPEAKTMP CIRCGRCVQG CPVGLTPFEL NARIHAGDLE GAAKVGLMDC
     LACGCCSYNC PANLPLVQSF QFAKGKLSER QSRKHQQEET KRLAAARKAR EEAIAEAKKQ
     MMLKRKAEMA AKKKAEEAAA AAAMPPPATA TAIQGEATP
 
 
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