ID   NFUA_YERPG              Reviewed;         191 AA.
AC   A9R4D2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN   Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN   OrderedLocusNames=YpAngola_A3750;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX88167.1; -; Genomic_DNA.
DR   RefSeq; WP_002208924.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R4D2; -.
DR   SMR; A9R4D2; -.
DR   GeneID; 66843803; -.
DR   KEGG; ypg:YpAngola_A3750; -.
DR   PATRIC; fig|349746.12.peg.457; -.
DR   OMA; CLAYCRP; -.
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_1000186796"
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;  21004 MW;  87BD6C71D938FE84 CRC64;
     MITITDAAQS HFAKLLANQE EGTQIRVFVI NPGTPTAECG VSYCPPDAVE ATDTELKFEQ
     LSAYVDELSV PYLQDAEIDF VTDQLGSQLT LKAPNAKMRK VDDSAPLMER VEYVLQSQIN
     PQLAGHGGRV TLMEITPEGL AILQFGGGCN GCSMVDVTLK EGIEKELLQK FPELKGVRDL
     TEHQRGEHSY Y