位置:首页 > 蛋白库 > RNFC_VIBC3
RNFC_VIBC3
ID   RNFC_VIBC3              Reviewed;         773 AA.
AC   A0A0H3AJC2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000305};
GN   Name=rnfC {ECO:0000255|HAMAP-Rule:MF_00461};
GN   OrderedLocusNames=VC0395_A0536 {ECO:0000312|EMBL:ABQ20645.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=25831459; DOI=10.1021/acs.biochem.5b00020;
RA   Hreha T.N., Mezic K.G., Herce H.D., Duffy E.B., Bourges A., Pryshchep S.,
RA   Juarez O., Barquera B.;
RT   "Complete topology of the RNF complex from Vibrio cholerae.";
RL   Biochemistry 54:2443-2455(2015).
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, ECO:0000269|PubMed:25831459}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000269|PubMed:25831459}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000627; ABQ20645.1; -; Genomic_DNA.
DR   RefSeq; WP_000949718.1; NZ_JAACZH010000005.1.
DR   AlphaFoldDB; A0A0H3AJC2; -.
DR   STRING; 345073.VC395_1030; -.
DR   EnsemblBacteria; ABQ20645; ABQ20645; VC0395_A0536.
DR   KEGG; vco:VC0395_A0536; -.
DR   eggNOG; COG4656; Bacteria.
DR   OMA; QQLYWYS; -.
DR   Proteomes; UP000000249; Chromosome 2.
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; 3.40.50.11540; -; 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   PANTHER; PTHR43034; PTHR43034; 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; SSF142019; SSF142019; 1.
DR   TIGRFAMs; TIGR01945; rnfC; 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..773
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_0000443488"
FT   DOMAIN          368..398
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   DOMAIN          408..437
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   REGION          460..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         378
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         381
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         384
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         388
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         417
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         420
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         423
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         427
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   773 AA;  83371 MW;  4BB7CB5D72F4A78F CRC64;
     MLSLIEQIKS GKLWDFPGGI HPFENKHQSN RQPIINASIP NELVLPLKQH IGKAGDLLVK
     VGDRVLKGQP LTQYTSTFML PIHAPTSGVI SAIEPRTVAH PSGLSELCIV LTPDQQEEWF
     ELQPQPDFQQ LTPETLLELI RQAGISGMGG AGFPTAKKLQ SGLSRTEILI INAAECEPYI
     TADDVLMRQY AHEIIQGIEI VEHILKPKLT IIGIEDNKPE AVAALQQAAQ DKPMVIRVIP
     TKYPSGGEKQ LIKILTNLEV PKGGIPADIG LMVQNVGSLQ AIARAIVHGE PLIRRVVTLT
     GDCFRKPRNV WALLGTPVQA LLNEFGYKAD KKLPRLIMGG PMMGFTLPHA QVPITKTANC
     ILAPTRNELT SSDNEMACIR CGQCAEACPV SLLPQQLQWH AKAEEFDKCE ELDLKDCIEC
     GACAYVCPSE IPLVQYYRQA KAEIRTRSLE AEAAERAKAR FEEKKARMER DKAERENRFK
     QAAEDRRKEM QQQGGSDAIA AAIERVKAQK AQLEPTDNSV KPAIAAAIAR AKAKQAEAAQ
     SGASEPDNSE MAKLREERKR QARERKAQKG EVTEASTSDG ADDKKSAVAA AIARAKARKA
     EQQETESAAQ PAQATPSSDD ADPKKAAVAA AIARAKARKA EQGTESTAQP AQATPSSDEA
     DPKKAAVAAA IARAKARKAE QQETESTAQP AQATPSSDDA DPKKAAVAAA IARAKARKAE
     QQETKSTAQP EQATPSSDDA DPKKAAVAAA IARAKARKAA QQSSSNLNAE EKD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024