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Database: UniProt
Entry: A4Y6I8_SHEPC
LinkDB: A4Y6I8_SHEPC
Original site: A4Y6I8_SHEPC 
ID   A4Y6I8_SHEPC            Unreviewed;       793 AA.
AC   A4Y6I8;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
DE            EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00461};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
GN   Name=rnfC {ECO:0000256|HAMAP-Rule:MF_00461};
GN   OrderedLocusNames=Sputcn32_1848 {ECO:0000313|EMBL:ABP75571.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP75571.1};
RN   [1] {ECO:0000313|EMBL:ABP75571.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP75571.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00461};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00461};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00461}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00461}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00461}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00461}.
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DR   EMBL; CP000681; ABP75571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y6I8; -.
DR   STRING; 319224.Sputcn32_1848; -.
DR   KEGG; spc:Sputcn32_1848; -.
DR   eggNOG; COG4656; Bacteria.
DR   HOGENOM; CLU_010808_2_1_6; -.
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; PF13237; Fer4_10; 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; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_00461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00461}; Membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00461};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00461};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00461};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00461}.
FT   DOMAIN          368..397
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          409..438
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          643..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          438..487
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        647..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..771
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         379
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         382
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         385
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         389
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         418
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         421
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         424
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         428
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ   SEQUENCE   793 AA;  84283 MW;  3542B1361EDAF039 CRC64;
     MLTLLDQLDK GTLWRSHGGI HPPEVKFLSN GTPIATLPLA KTYLVPIPQV GENCTLAVKL
     GDKVLKGTPL TQGPSIWHLP VHAPTSGTIV AIEPRASNHA SALPVNTCVI EADGKDTWCE
     LASNDLDSLS HQQIIDKIHQ AGVAGMGGAA FPSHIKLNPA SEIDLVIING VECEPYISSD
     DRLMREYSQD ILAGIAIIYR LLTPKRIVIA IEDNKPEAIK AMQMAVTQSA LPTGSIRVTV
     IPTKYPSGGE KQLIQIITGR EVPSGAIPAK LGIVVHNVGT AFAIHQAVVQ DKPLVERVVT
     VTGKNVGKPG NYWLPIGTPV EHVLMQTEFK PESEQKIIVG GPMMGHALPT INVPILKGTN
     CILVPSNQEI GVTPEEKACI RCGECANVCP ALLLPQQLFW HAKAEEYDKA ASFNLKDCIE
     CGCCSYVCPS DIPLVEYYRI AKSALKQTAD EKQQAERAKH RFEARLARLE EEKLAREAKA
     KEAAERRQAT MTGTDKNAVA EAMARIAAKK AAATQAPSET AIAPTAVVEV PREKAAVAAA
     IARAKAKKAA AATVSQVTDD EPDSSMEIEQ AEPLSQKDKV AAAIARAKAK KATMKAGSDV
     NEDIDAAEVD AEKRVTGSAA STEVDDKKAK IAAAVARAKA KKAIQQSGIV SEDQTPAVQA
     PEDQATKTPV VNTPVAERES STVTPSPEDD KKARVAAAIA RAKAKKAAAQ ADSSEVAEVQ
     PKLEAESAQP SDTPLKPEPI TELRSELSSE LSSEPSHQLS PEDEKKAKIA AAVARAKAKK
     AARAVDATSD SNE
//
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