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RNFC_RHOCA
ID   RNFC_RHOCA              Reviewed;         519 AA.
AC   Q52716; O08057; Q52712;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=Nitrogen fixation protein RnfC {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, ECO:0000303|PubMed:8264535};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RC   STRAIN=B10S;
RX   PubMed=8264535; DOI=10.1007/bf00279903;
RA   Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA   Schuppler M., Marxer M., Oelze J., Klipp W.;
RT   "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT   capsulatus: a putative membrane complex involved in electron transport to
RT   nitrogenase.";
RL   Mol. Gen. Genet. 241:602-615(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=9492268; DOI=10.1046/j.1432-1327.1998.2510054.x;
RA   Jouanneau Y., Jeong H.-S., Hugo N., Meyer C., Willison J.C.;
RT   "Overexpression in Escherichia coli of the rnf genes from Rhodobacter
RT   capsulatus -- characterization of two membrane-bound iron-sulfur
RT   proteins.";
RL   Eur. J. Biochem. 251:54-64(1998).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane (By
CC       similarity). Required for nitrogen fixation. Involved in electron
CC       transfer to nitrogenase (PubMed:8264535). {ECO:0000255|HAMAP-
CC       Rule:MF_00461, ECO:0000269|PubMed:8264535}.
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       ECO:0000305|PubMed:9492268}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00461, ECO:0000269|PubMed:9492268};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00461,
CC       ECO:0000269|PubMed:9492268}.
CC   -!- INDUCTION: Expression is reduced under iron-limiting conditions.
CC       {ECO:0000269|PubMed:9492268}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
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DR   EMBL; X72888; CAA51399.1; -; Genomic_DNA.
DR   EMBL; Y11913; CAA72670.1; -; Genomic_DNA.
DR   PIR; S39893; S39893.
DR   RefSeq; WP_013068985.1; NZ_VIBE01000016.1.
DR   AlphaFoldDB; Q52716; -.
DR   SMR; Q52716; -.
DR   TCDB; 3.D.6.1.1; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   GeneID; 31492069; -.
DR   OMA; YPMGSEK; -.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore 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   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
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; PF13237; Fer4_10; 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   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Nitrogen fixation; Repeat; Translocase; Transport.
FT   CHAIN           1..519
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_0000073211"
FT   DOMAIN          372..401
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   DOMAIN          411..440
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT   REGION          494..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         387
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         391
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         426
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         430
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   519 AA;  55588 MW;  E5451EB2A3FA6026 CRC64;
     MRLPSIATLF HPLQSFSIRG GIHPETHKHL TSECEIETMP MPALIRLPLQ QHIGAEAEPI
     VKRDDLVLKG QLIAKARGPL SANIHAPTSG RVIAVGHFVA PHASGLPVPT ITIRPDGEDK
     WGPHLPRLRP ENAAPEEIAA QVAAAGIVGM GGATFPSAVK LNLRAKYDLT TLIINGAECE
     PYLTCDDRLM RERAEEIADG IGIMARALGV KQVFVAIESN KPQAIEAMTR YNRALGYTFK
     IHVVPTQYPM GSEKHLVKMI TGQETPARAL TADLGVVVHN IATAHAVHLA VRYGEPLIAR
     TVTVSGHGIR RPANLRVLIG TPVSEIIAHC GGFTEEPDRL LLGGPMMGMP IQNPRVPVVK
     GTNGILALTA AETPEAKTMP CIRCGRCVQG CPVGLTPFEL NARIHAGDLE GAAKVGLMDC
     LACGCCSYNC PANLPLVQSF QFAKGKLSER QSRKHQQEET KRLAAARKAR EEAIAEAKKQ
     MMLKRKAEMA AKKKAEEAAA AAAMPPPATA TAIQGEATP
 
 
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