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Database: UniProt
Entry: A0A063Y1J9_9GAMM
LinkDB: A0A063Y1J9_9GAMM
Original site: A0A063Y1J9_9GAMM 
ID   A0A063Y1J9_9GAMM        Unreviewed;       565 AA.
AC   A0A063Y1J9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=ADINL_3106 {ECO:0000313|EMBL:KDE38651.1};
OS   Nitrincola lacisaponensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE38651.1, ECO:0000313|Proteomes:UP000027318};
RN   [1] {ECO:0000313|EMBL:KDE38651.1, ECO:0000313|Proteomes:UP000027318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4CA {ECO:0000313|EMBL:KDE38651.1,
RC   ECO:0000313|Proteomes:UP000027318};
RX   PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA   Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA   Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT   "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT   bacterium isolated from an alkaline, saline lake.";
RL   Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDE38651.1}.
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DR   EMBL; JMSZ01000042; KDE38651.1; -; Genomic_DNA.
DR   RefSeq; WP_036550094.1; NZ_JMSZ01000042.1.
DR   AlphaFoldDB; A0A063Y1J9; -.
DR   STRING; 267850.ADINL_3106; -.
DR   PATRIC; fig|267850.7.peg.3057; -.
DR   OrthoDB; 9767754at2; -.
DR   Proteomes; UP000027318; 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; 3.30.70.20; -; 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   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   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 {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:UP000027318};
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          362..391
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          401..430
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         371
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         374
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         377
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         381
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         410
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         413
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         416
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         420
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   565 AA;  61832 MW;  5A0BABF247511312 CRC64;
     MTRLYSFHGG VHPPENKRQS LGAPIRQAPL PARLILPLQQ HIGKPATPLV AVGDTVLKGQ
     KIAEPSGHVS AAIHAPSSGS ITYIGLQPVP HASGLESPCI VIETDGQEQW IERQPLTDYQ
     QLDKQALIRH IRNAGIAGLG GAGFPTDIKL NLGRDHIVNT LIINAAECEP YITADDALMR
     ERPDEILSGI EIIAHLLQPS HILIGIEDNK PNAIKALRDA IRARKLPIDL VVVPTRYPSG
     GEKQLIQLLT GIEVASGSIP ADVGIVCQNV GTAAAIYRAV ILGEPLISRI VTLTGFALGH
     RQNYEVLIGT PFSVLLESAE VDRSRMFRLV MGGPMMGISI EDDRIPVIKT TNCIIAATRE
     EMPPSPPAQP CIRCGMCEQV CPASLLPQQL FWFAKGREFD KARHHNLFDC IECGACAYVC
     PSNIPLVQHY RFAKSEIRNE EAEQLKAAQA RERFEARQAR LAREEQEKEQ RRKERAEAAA
     REQARKKAEA EQADAGEQDP EAELKKLKTA ASIARTKLKK ARDALKNAQE KGLDGTDKLE
     ATVLQLEQSA QAAEQAWQNA TGVQH
//
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