ID NRFC_ECOLI Reviewed; 223 AA.
AC P0AAK7; P32708; Q2M6N2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Protein NrfC;
DE Flags: Precursor;
GN Name=nrfC; Synonyms=yjcJ; OrderedLocusNames=b4072, JW4033;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8057835; DOI=10.1111/j.1365-2958.1994.tb01004.x;
RA Hussain H.A., Grove J., Griffiths L., Busby S., Cole J.;
RT "A seven-gene operon essential for formate-dependent nitrite reduction to
RT ammonia by enteric bacteria.";
RL Mol. Microbiol. 12:153-163(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 65-66.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP EXPORT VIA THE TAT-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
CC -!- FUNCTION: Probably involved in the transfer of electrons from the
CC quinone pool to the type-c cytochromes.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
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DR EMBL; X72298; CAA51043.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43166.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77042.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78074.1; -; Genomic_DNA.
DR PIR; C57987; C57987.
DR RefSeq; NP_418496.1; NC_000913.3.
DR RefSeq; WP_000220281.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P0AAK7; -.
DR SMR; P0AAK7; -.
DR BioGRID; 4263519; 39.
DR IntAct; P0AAK7; 3.
DR STRING; 511145.b4072; -.
DR TCDB; 5.A.3.5.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P0AAK7; -.
DR PaxDb; 511145-b4072; -.
DR EnsemblBacteria; AAC77042; AAC77042; b4072.
DR GeneID; 75169595; -.
DR GeneID; 948581; -.
DR KEGG; ecj:JW4033; -.
DR KEGG; eco:b4072; -.
DR PATRIC; fig|1411691.4.peg.2632; -.
DR EchoBASE; EB1889; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_1_3_6; -.
DR InParanoid; P0AAK7; -.
DR OMA; CVDRIYN; -.
DR OrthoDB; 9779457at2; -.
DR PhylomeDB; P0AAK7; -.
DR BioCyc; EcoCyc:NRFC-MONOMER; -.
DR PHI-base; PHI:10999; -.
DR PRO; PR:P0AAK7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IMP:EcoCyc.
DR CDD; cd10551; PsrB; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR017567; Cyt_c_NO2Rdtase_NrfC.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR03149; cyt_nit_nrfC; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43177; PROTEIN NRFC; 1.
DR PANTHER; PTHR43177:SF9; PROTEIN NRFC; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Signal; Transport.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 28..223
FT /note="Protein NrfC"
FT /id="PRO_0000042276"
FT DOMAIN 37..65
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 83..114
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 116..145
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 65..66
FT /note="GV -> AS (in Ref. 2; AAC43166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24567 MW; 676C3264D341FC8E CRC64;
MTWSRRQFLT GVGVLAAVSG TAGRVVAKTL NINGVRYGMV HDESLCIGCT ACMDACREVN
KVPEGVSRLT IIRSEPQGEF PDVKYRFFRK SCQHCDHAPC VDVCPTGASF RDAASGIVDV
NPDLCVGCQY CIAACPYRVR FIHPVTKTAD KCDFCRKTNL QAGKLPACVE ACPTKALTFG
NLDDPNSEIS QLLRQKPTYR YKLALGTKPK LYRVPFKYGE VSQ
//
