ID F9UE33_9GAMM Unreviewed; 508 AA.
AC F9UE33;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
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 ORFNames=ThimaDRAFT_3135 {ECO:0000313|EMBL:EGV17590.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV17590.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV17590.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV17590.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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; AFWV01000010; EGV17590.1; -; Genomic_DNA.
DR RefSeq; WP_007194007.1; NZ_AFWV01000010.1.
DR AlphaFoldDB; F9UE33; -.
DR STRING; 768671.ThimaDRAFT_3135; -.
DR PATRIC; fig|768671.3.peg.3316; -.
DR eggNOG; COG4656; Bacteria.
DR OrthoDB; 9767754at2; -.
DR Proteomes; UP000005459; Unassembled WGS sequence.
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; 3.30.70.3270; -; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000005459};
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 360..389
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 399..428
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 463..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
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 372
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 375
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 379
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 408
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 411
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 414
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="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ SEQUENCE 508 AA; 53590 MW; 6CEAB217DF576968 CRC64;
MKLFKIRGGV HPHDNKHLAA GQAIEDLPMP ALLHIPLQQH IGAPAKPAVR RGQQVAKGDL
LAFSQGVISA PVHAPTSGRV MGVGSYPAHH ASGLSVRTVT LKPDGEDRWS DEIQGVSDPF
ALTPEEIATR VAAAGIVGMG GATFPSAVKL NLRTRYRLHT LVINGAECEP YLTCDDRLMR
EHAEEVIDGV RIMAHALGVE RIIVAIENNK PEAQAAVALA ASVDPRIRVA RLPTRYPMGS
EKHLVQALTG RETPARGLTA DIGVVVHNGA TAFAVHEALR FGRPLVSRIV TVSGGAVSRP
RNLRVPIGAR VQDLLEYCGG FTEQPAQLIS GGPMMGQPLP STRVPMVKGS NGVLALTGAE
AAGHEPMPCI RCATCVQACP CGLVPLDMAA HTRAGDLDGA VSLGLMDCIG CGSCAYVCPA
HIPLVQYFNY AKGEMAARGR AKQKMTETKR LAEQRTARME AIKQAKREAM AKRKREAAAK
KAAETAAADA ATMTSGAAAE PTATTAEA
//
