NAPF_ECOL6
ID NAPF_ECOL6 Reviewed; 164 AA.
AC P0AAL1; P33939;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ferredoxin-type protein NapF {ECO:0000255|HAMAP-Rule:MF_02201};
GN Name=napF {ECO:0000255|HAMAP-Rule:MF_02201}; OrderedLocusNames=c2747;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN81201.1; -; Genomic_DNA.
DR RefSeq; WP_000686723.1; NC_004431.1.
DR AlphaFoldDB; P0AAL1; -.
DR STRING; 199310.c2747; -.
DR EnsemblBacteria; AAN81201; AAN81201; c2747.
DR GeneID; 66673897; -.
DR KEGG; ecc:c2747; -.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR HOGENOM; CLU_077329_2_1_6; -.
DR OMA; YQGIWCQ; -.
DR BioCyc; ECOL199310:C2747-MON; -.
DR Proteomes; UP000001410; 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; Repeat.
FT CHAIN 1..164
FT /note="Ferredoxin-type protein NapF"
FT /id="PRO_0000159277"
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
