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RNFC_VIBCH
ID   RNFC_VIBCH              Reviewed;         774 AA.
AC   Q9KT88;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00461};
DE   AltName: Full=Rnf electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
GN   Name=rnfC {ECO:0000255|HAMAP-Rule:MF_00461}; OrderedLocusNames=VC_1015;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00461}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF94176.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF94176.1; ALT_INIT; Genomic_DNA.
DR   PIR; E82252; E82252.
DR   RefSeq; NP_230661.1; NC_002505.1.
DR   RefSeq; WP_000949723.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KT88; -.
DR   STRING; 243277.VC_1015; -.
DR   PRIDE; Q9KT88; -.
DR   DNASU; 2614286; -.
DR   EnsemblBacteria; AAF94176; AAF94176; VC_1015.
DR   GeneID; 57739699; -.
DR   KEGG; vch:VC_1015; -.
DR   PATRIC; fig|243277.26.peg.969; -.
DR   eggNOG; COG4656; Bacteria.
DR   HOGENOM; CLU_010808_2_1_6; -.
DR   OMA; QQLYWYS; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; Reference proteome; Repeat;
KW   Translocase; Transport.
FT   CHAIN           1..774
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_0000073213"
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          459..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..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        724..739
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   774 AA;  83500 MW;  44EB13EC304E3A4E 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 EQQETESTAQ PAQATPSSDD
     ADPKKAAVAA AIARAKARKA EKQETESAAQ PTQATPSSDD ADPKKAAVAA AIARAKARKA
     EQQETESAAQ PTQATPSSDD ADPKKAAVAA AIARAKARKA AQQSSSNLNA EEKD
 
 
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