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Database: UniProt
Entry: RNFC_YERP3
LinkDB: RNFC_YERP3
Original site: RNFC_YERP3 
ID   RNFC_YERP3              Reviewed;         698 AA.
AC   A7FHZ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00461};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
GN   Name=rnfC {ECO:0000255|HAMAP-Rule:MF_00461};
GN   OrderedLocusNames=YpsIP31758_1896;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_00461}.
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: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00461}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00461}.
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; CP000720; ABS46946.1; -; Genomic_DNA.
DR   RefSeq; WP_012105096.1; NC_009708.1.
DR   AlphaFoldDB; A7FHZ3; -.
DR   SMR; A7FHZ3; -.
DR   KEGG; ypi:YpsIP31758_1896; -.
DR   HOGENOM; CLU_010808_2_1_6; -.
DR   Proteomes; UP000002412; Chromosome.
DR   GO; GO:0005886; C:plasma 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   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 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   NCBIfam; TIGR01945; rnfC; 1.
DR   PANTHER; PTHR43034; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR   PANTHER; PTHR43034:SF2; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF13375; RnfC_N; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Repeat; Translocase; Transport.
FT   CHAIN           1..698
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_1000060341"
FT   DOMAIN          366..397
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   DOMAIN          407..436
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         377
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         380
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         383
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="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   BINDING         416
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         419
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         422
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="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
SQ   SEQUENCE   698 AA;  75018 MW;  B51965764DEE8A4D CRC64;
     MFKLFTARQH DKIWDFDGGI HPPEMKLQSS TVPMRIAPLP DQLIIPLQQH LGPEGELRVR
     AGEQVLKGQP LTVGRGRTVP VHAPTSGMIT AIAPHTTAHP SGLAELCVHI TPDGEDRWRE
     QQPWADYRQR DKMALLDRIH QAGIAGLGGA GFPTASKLQG GLNGIITLII NAAECEPYIT
     ADDRLMQEHA DEVITGIHIL RHLLQPQQVL IGIEDNKPEA IAALQRALRG QDDIHLRVVP
     TKYPSGGAKQ LTKILTGKEV PFGKHSSSIG VLMQNVGTVV AIKRAVIDDE PLIERVVTLT
     GDALSSPGNF WARIGTPVLY LLKLAGFKPQ NPPMVIMGGP LMGFTLPSLD VPIVKISNCI
     LAPAETEMGL SEPEQSCIRC GLCVDACPAG LLPQQLYWFS RGEEHEKARN HNLFDCIECG
     ACAYVCPSNI PLVQYYRQEK AEIRALDQES ARAAEAKARF EAKQARLARE KLARELRHKQ
     AAVKLTDADQ QTVDAAVSRL TRQSDGSESV INIPAGQMPD NSAVIAAREA RKAQARARQA
     EKQQARSTEE TTDVVDPRQA AVAAAIARVK AKKAAQVQHV TTDVAEAGSE AIAEDPRKAA
     VAAAIARVKA KKAAQAQHVT TDVAEAGSEA MAEDPRKAAV AAAIARVKAK KAAQAQHVTT
     DVAEAGSEAI AEDPRKAAVA AAIARVKAKK AAQAINPD
//
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