ID   NFUA_SHIDS              Reviewed;         191 AA.
AC   Q32AM7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN   Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; Synonyms=yhgI;
GN   OrderedLocusNames=SDY_3662;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63628.1; -; Genomic_DNA.
DR   RefSeq; WP_000619389.1; NC_007606.1.
DR   RefSeq; YP_405119.1; NC_007606.1.
DR   AlphaFoldDB; Q32AM7; -.
DR   SMR; Q32AM7; -.
DR   STRING; 300267.SDY_3662; -.
DR   PRIDE; Q32AM7; -.
DR   EnsemblBacteria; ABB63628; ABB63628; SDY_3662.
DR   GeneID; 67417042; -.
DR   KEGG; sdy:SDY_3662; -.
DR   PATRIC; fig|300267.13.peg.4344; -.
DR   HOGENOM; CLU_094569_0_0_6; -.
DR   OMA; CLAYCRP; -.
DR   Proteomes; UP000002716; 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; Reference proteome.
FT   CHAIN           1..191
FT                   /note="Fe/S biogenesis protein NfuA"
FT                   /id="PRO_0000268244"
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