ID   NFUA_ECO81              Reviewed;         191 AA.
AC   B7N147;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN   Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=ECED1_4075;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S
CC       cluster, can transfer this cluster to apoproteins, and thereby
CC       intervenes in the maturation of Fe/S proteins. Could also act as a
CC       scaffold/chaperone for damaged Fe/S proteins. {ECO:0000255|HAMAP-
CC       Rule:MF_01637}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01637};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably
CC       bound at the interface of two monomers. {ECO:0000255|HAMAP-
CC       Rule:MF_01637};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01637}.
CC   -!- SIMILARITY: Belongs to the NfuA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01637}.
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DR   EMBL; CU928162; CAR10065.1; -; Genomic_DNA.
DR   RefSeq; WP_000619389.1; NC_011745.1.
DR   AlphaFoldDB; B7N147; -.
DR   SMR; B7N147; -.
DR   EnsemblBacteria; CAR10065; CAR10065; ECED1_4075.
DR   GeneID; 67417042; -.
DR   KEGG; ecq:ECED1_4075; -.
DR   HOGENOM; CLU_094569_0_0_6; -.
DR   OMA; CLAYCRP; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0051604; P:protein maturation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.300.12; -; 1.
DR   Gene3D; 3.30.300.130; -; 1.
DR   HAMAP; MF_01637; Fe_S_biogen_NfuA; 1.
DR   InterPro; IPR017726; Fe/S_biogenesis_protein_NfuA.
DR   InterPro; IPR000361; FeS_biogenesis.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR035903; HesB-like_dom_sf.
DR   InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR   Pfam; PF01521; Fe-S_biosyn; 1.
DR   Pfam; PF01106; NifU; 1.
DR   SUPFAM; SSF117916; SSF117916; 1.
DR   SUPFAM; SSF89360; SSF89360; 1.
DR   TIGRFAMs; TIGR03341; YhgI_GntY; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT   CHAIN           1..191
FT                   /note="Fe/S biogenesis protein NfuA"
FT                   /id="PRO_1000186747"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
FT   BINDING         152
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
SQ   SEQUENCE   191 AA;  20998 MW;  06874546ADA5A971 CRC64;
     MIRISDAAQA HFAKLLANQE EGTQIRVFVI NPGTPNAECG VSYCPPDAVE ATDTALKFDL
     LTAYVDELSA PYLEDAEIDF VTDQLGSQLT LKAPNAKMRK VADDAPLMER VEYMLQSQIN
     PQLAGHGGRV SLMEITEDGY AILQFGGGCN GCSMVDVTLK EGIEKQLLNE FPELKGVRDL
     TEHQRGEHSY Y