NAPG_ECOLI
ID NAPG_ECOLI Reviewed; 231 AA.
AC P0AAL3; P33935; P33936; Q2MAN8;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferredoxin-type protein NapG {ECO:0000305};
DE AltName: Full=Ubiquinol--[NapC cytochrome c] reductase NapG subunit {ECO:0000305};
DE Flags: Precursor;
GN Name=napG; Synonyms=yojA, yojB; OrderedLocusNames=b2205, JW2193;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11967083; DOI=10.1046/j.1365-2958.2002.02875.x;
RA Brondijk T.H., Fiegen D., Richardson D.J., Cole J.A.;
RT "Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic
RT nitrate reductase, in ubiquinol oxidation.";
RL Mol. Microbiol. 44:245-255(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 11-ARG-ARG-12.
RX PubMed=14674886; DOI=10.1042/bj20031115;
RA Brondijk T.H., Nilavongse A., Filenko N., Richardson D.J., Cole J.A.;
RT "NapGH components of the periplasmic nitrate reductase of Escherichia coli
RT K-12: location, topology and physiological roles in quinol oxidation and
RT redox balancing.";
RL Biochem. J. 379:47-55(2004).
RN [6]
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: Required for electron transfer from ubiquinol, via NapC, to
CC the periplasmic nitrate reductase NapAB complex.
CC {ECO:0000269|PubMed:11967083, ECO:0000269|PubMed:14674886}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 4 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:14674886}.
CC -!- PTM: Exported by the Tat system (PubMed:17218314). The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000269|PubMed:17218314, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deletion of both napG and napH genes has little
CC effect on the overall rate of nitrate reduction during growth in the
CC glycerol/nitrate medium. However, during growth in the glucose/nitrate
CC medium, the double mutant shows a decreased rate of electron transfer
CC that correlates with decreased NapAB activity.
CC {ECO:0000269|PubMed:11967083}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16397.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA16398.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00008; AAA16398.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00008; AAA16397.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75265.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76668.1; -; Genomic_DNA.
DR PIR; C64990; C64990.
DR RefSeq; NP_416709.1; NC_000913.3.
DR RefSeq; WP_000091291.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0AAL3; -.
DR BioGRID; 4262222; 16.
DR IntAct; P0AAL3; 4.
DR STRING; 511145.b2205; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR PaxDb; P0AAL3; -.
DR PRIDE; P0AAL3; -.
DR EnsemblBacteria; AAC75265; AAC75265; b2205.
DR EnsemblBacteria; BAE76668; BAE76668; BAE76668.
DR GeneID; 67416641; -.
DR GeneID; 945544; -.
DR KEGG; ecj:JW2193; -.
DR KEGG; eco:b2205; -.
DR PATRIC; fig|1411691.4.peg.31; -.
DR EchoBASE; EB1993; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_077329_0_0_6; -.
DR InParanoid; P0AAL3; -.
DR OMA; LIDHETC; -.
DR PhylomeDB; P0AAL3; -.
DR BioCyc; EcoCyc:NAPG-MON; -.
DR BioCyc; MetaCyc:NAPG-MON; -.
DR PRO; PR:P0AAL3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004494; MauM_NapG.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF12800; Fer4_4; 2.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR00397; mauM_napG; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Periplasm;
KW Reference proteome; Repeat; Signal; Transport.
FT SIGNAL 1..41
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 42..231
FT /note="Ferredoxin-type protein NapG"
FT /id="PRO_0000159279"
FT DOMAIN 50..81
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 89..121
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 130..166
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 177..208
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT MUTAGEN 11..12
FT /note="RR->AA: Cannot complement a deletion mutant."
FT /evidence="ECO:0000269|PubMed:14674886"
SQ SEQUENCE 231 AA; 24925 MW; 9DA55774D6A68AD5 CRC64;
MSRSAKPQNG RRRFLRDVVR TAGGLAAVGV ALGLQQQTAR ASGVRLRPPG AINENAFASA
CVRCGQCVQA CPYDTLKLAT LASGLSAGTP YFVARDIPCE MCEDIPCAKV CPSGALDREI
ESIDDARMGL AVLVDQENCL NFQGLRCDVC YRECPKIDEA ITLELERNTR TGKHARFLPT
VHSDACTGCG KCEKVCVLEQ PAIKVLPLSL AKGELGHHYR FGWLEGNNGK S
