NAPF_ECOLI
ID NAPF_ECOLI Reviewed; 164 AA.
AC P0AAL0; P33939;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ferredoxin-type protein NapF {ECO:0000255|HAMAP-Rule:MF_02201, ECO:0000305};
GN Name=napF {ECO:0000255|HAMAP-Rule:MF_02201}; Synonyms=yojG;
GN OrderedLocusNames=b2208, JW2196;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [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 PROTEIN SEQUENCE OF 1-5, FUNCTION, INTERACTION WITH NAPA, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 7-ARG-ARG-8; PRO-24; PRO-25 AND TRP-26.
RC STRAIN=K12;
RX PubMed=17074894; DOI=10.1099/mic.0.29157-0;
RA Nilavongse A., Brondijk T.H., Overton T.W., Richardson D.J., Leach E.R.,
RA Cole J.A.;
RT "The NapF protein of the Escherichia coli periplasmic nitrate reductase
RT system: demonstration of a cytoplasmic location and interaction with the
RT catalytic subunit, NapA.";
RL Microbiology 152:3227-3237(2006).
RN [6]
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).
CC -!- FUNCTION: Could be involved in the maturation of NapA, the catalytic
CC subunit of the periplasmic nitrate reductase, before its export into
CC the periplasm (PubMed:17074894). Is not involved in the electron
CC transfer from menaquinol or ubiquinol to the periplasmic nitrate
CC reductase (PubMed:11967083). {ECO:0000269|PubMed:11967083,
CC ECO:0000269|PubMed:17074894}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02201,
CC ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 3 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- SUBUNIT: Interacts with the cytoplasmic NapA precursor.
CC {ECO:0000255|HAMAP-Rule:MF_02201, ECO:0000269|PubMed:17074894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17074894}.
CC Note=Loosely attached to the inner side of the membrane.
CC {ECO:0000269|PubMed:17074894}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not decrease the rate
CC of electron transfer from physiological substrates to the Nap complex,
CC but it has a significant effect on cell energetics.
CC {ECO:0000269|PubMed:11967083}.
CC -!- SIMILARITY: Belongs to the NapF family. {ECO:0000255|HAMAP-
CC Rule:MF_02201, ECO:0000305}.
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DR EMBL; U00008; AAA16401.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75268.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15991.1; -; Genomic_DNA.
DR PIR; F64990; F64990.
DR RefSeq; NP_416712.1; NC_000913.3.
DR RefSeq; WP_000686723.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P0AAL0; -.
DR BioGRID; 4262219; 35.
DR STRING; 511145.b2208; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR PaxDb; P0AAL0; -.
DR PRIDE; P0AAL0; -.
DR EnsemblBacteria; AAC75268; AAC75268; b2208.
DR EnsemblBacteria; BAA15991; BAA15991; BAA15991.
DR GeneID; 66673897; -.
DR GeneID; 946813; -.
DR KEGG; ecj:JW2196; -.
DR KEGG; eco:b2208; -.
DR PATRIC; fig|1411691.4.peg.28; -.
DR EchoBASE; EB1995; -.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR HOGENOM; CLU_077329_2_1_6; -.
DR InParanoid; P0AAL0; -.
DR OMA; YQGIWCQ; -.
DR PhylomeDB; P0AAL0; -.
DR BioCyc; EcoCyc:NAPF-MON; -.
DR PRO; PR:P0AAL0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR CDD; cd10564; NapF_like; 1.
DR HAMAP; MF_02201; NapF; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004496; NapF.
DR PANTHER; PTHR24960:SF46; PTHR24960:SF46; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR TIGRFAMs; TIGR00402; napF; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..164
FT /note="Ferredoxin-type protein NapF"
FT /id="PRO_0000159275"
FT DOMAIN 28..57
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 58..89
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 132..161
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT 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|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT MUTAGEN 7..8
FT /note="RR->AA: No change in activity."
FT /evidence="ECO:0000269|PubMed:17074894"
FT MUTAGEN 24
FT /note="P->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:17074894"
FT MUTAGEN 25
FT /note="P->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:17074894"
FT MUTAGEN 26
FT /note="W->Y: No change in activity."
FT /evidence="ECO:0000269|PubMed:17074894"
SQ SEQUENCE 164 AA; 18047 MW; 3832B3D78805FAC1 CRC64;
MKIDASRRGI LTGRWRKASN GIRPPWSGDE SHFLTHCTRC DACINACENN ILQRGAGGYP
SVNFKNNECS FCYACAQACP ESLFSPRHTR AWDLQFTIGD ACLAYQSVEC RRCQDSCEPM
AIIFRPTLSG IYQPQLNSQL CNGCGACAAS CPVSAITAEY LHAH
