NAPF_ECO57
ID NAPF_ECO57 Reviewed; 164 AA.
AC P0AAL2; P33939;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ferredoxin-type protein NapF {ECO:0000255|HAMAP-Rule:MF_02201};
GN Name=napF {ECO:0000255|HAMAP-Rule:MF_02201};
GN OrderedLocusNames=Z3465, ECs3097;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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. {ECO:0000255|HAMAP-Rule:MF_02201}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02201};
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02201}.
CC -!- SIMILARITY: Belongs to the NapF family. {ECO:0000255|HAMAP-
CC Rule:MF_02201}.
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DR EMBL; AE005174; AAG57343.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36520.1; -; Genomic_DNA.
DR PIR; A91016; A91016.
DR PIR; C85860; C85860.
DR RefSeq; NP_311124.1; NC_002695.1.
DR RefSeq; WP_000686723.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AAL2; -.
DR STRING; 155864.EDL933_3373; -.
DR PRIDE; P0AAL2; -.
DR EnsemblBacteria; AAG57343; AAG57343; Z3465.
DR EnsemblBacteria; BAB36520; BAB36520; ECs_3097.
DR GeneID; 66673897; -.
DR GeneID; 916803; -.
DR KEGG; ece:Z3465; -.
DR KEGG; ecs:ECs_3097; -.
DR PATRIC; fig|386585.9.peg.3231; -.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR HOGENOM; CLU_077329_2_1_6; -.
DR OMA; YQGIWCQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..164
FT /note="Ferredoxin-type protein NapF"
FT /id="PRO_0000159276"
FT DOMAIN 28..57
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201"
FT DOMAIN 58..89
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201"
FT DOMAIN 132..161
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02201"
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 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 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 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 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 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 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 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 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 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 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 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"
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
