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Database: UniProt
Entry: A0A430KQ08_9GAMM
LinkDB: A0A430KQ08_9GAMM
Original site: A0A430KQ08_9GAMM 
ID   A0A430KQ08_9GAMM        Unreviewed;       988 AA.
AC   A0A430KQ08;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=rsxC {ECO:0000313|EMBL:RTE65545.1};
GN   Synonyms=rnfC {ECO:0000256|HAMAP-Rule:MF_00461};
GN   ORFNames=EH243_11430 {ECO:0000313|EMBL:RTE65545.1};
OS   Amphritea opalescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=2490544 {ECO:0000313|EMBL:RTE65545.1, ECO:0000313|Proteomes:UP000283087};
RN   [1] {ECO:0000313|EMBL:RTE65545.1, ECO:0000313|Proteomes:UP000283087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANRC-JH13 {ECO:0000313|EMBL:RTE65545.1,
RC   ECO:0000313|Proteomes:UP000283087};
RA   Fang Z., Zhang Y., Han X.;
RT   "The draft genome sequence of Amphritea opalescens ANRC-JH13T.";
RL   Submitted (NOV-2018) 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}.
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:RTE65545.1}.
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DR   EMBL; RQXW01000009; RTE65545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430KQ08; -.
DR   OrthoDB; 9767754at2; -.
DR   Proteomes; UP000283087; 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; 1.20.58.60; -; 1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000283087};
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          365..394
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          404..433
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          454..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          513..711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          752..779
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          820..982
FT                   /evidence="ECO:0000256|SAM:Coils"
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         380
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         384
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         419
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         423
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   988 AA;  105670 MW;  26E80A655C1A180B CRC64;
     MKNTIRVHQF HGGIHPPENK KQSTGAPISL APLPSRIILP LQQHIGLPAD PIVKVGDRVL
     KGQRVAEAIG RISANIHASI SGTVVDIGPH PVPHVSGMDA DCLVIESDGQ DEWIEHQGLP
     DYTQLAKPEL IEYIRQAGVA GMGGAGFPTD VKLHLGDDHI VNTLIINAAE CEPYITADDM
     LMRERADEIL GGIEIIAHLL KPLHIMVGIE DNKPQAIRAL HDALDKSHLN LDIVITPTKY
     PSGGEKQLIK LLTGVEVPSG KIPADVGIVC QNVGTTTAVY RAVILGEPLI SRIMTVTGES
     ANHKQNYEVR IGTPIADLLN HSGVDRAQMQ RLIIGGPMMG ITVTNEQIPV IKTTNCLIAA
     SIHEMPPQPP AQACIRCGMC EQVCPAELLP QQLYWFAKGK EFDKARHHNL FDCIECGACS
     YVCPSNIPLV QYYRFAKAEI RKEDDEQRKA DHARLRFEAR LARLERDKIE KEERRKQRAI
     EAAAAQAAKK DAAFNKAASP ATNNPTDAGV PDLKQLKSNA AIARTKLRKA EKALANAQDK
     GLDGIETLQA TLKQLQLKSE LAEKAYTEAQ QAPAKSAAAP ETDLKQLKSN AAIARTKLKK
     AEKQLAAAEA GGEGDIDALK AQVVALQAKS ADAEKAYQAA DSGTVSPVAI DTSALEAEIA
     TLQGKVDKAE NAWKAAVESG SPAAEKMAAG VEKLKEKLTG LQAELTQARS AVQPAATVDT
     SALDTEIATL QGKVDKAENA WKAAVESGSP AAEKMAAGVE KLKEKLTGLQ AELTQARSAV
     QPAATVDTSA LDAEITTLQG KVDKAENAWK AAVESGSPAA DKMAAGVEKL KEKLKGLQAE
     LTQAKGHLET NAEGKAEEAP AIDLKALKQQ VSIMRTKLKK AEKQLAELPE GEDNASLMAE
     IEALRARHDA AKASFDAAEA DKIAAAASEG IDLKQLKIDA ALARAAVTKA ERALSKAEQE
     SKQSLETELL SIRAKADKLN ATLERFSD
//
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