ID   NFUA_ACTP7              Reviewed;         199 AA.
AC   B3GZZ1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN   Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=APP7_0151;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE60803.1; -; Genomic_DNA.
DR   RefSeq; WP_005600176.1; NC_010939.1.
DR   AlphaFoldDB; B3GZZ1; -.
DR   SMR; B3GZZ1; -.
DR   EnsemblBacteria; ACE60803; ACE60803; APP7_0151.
DR   KEGG; apa:APP7_0151; -.
DR   HOGENOM; CLU_094569_0_0_6; -.
DR   OMA; CLAYCRP; -.
DR   BioCyc; APLE537457:APP7_RS00775-MON; -.
DR   Proteomes; UP000001226; 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..199
FT                   /note="Fe/S biogenesis protein NfuA"
FT                   /id="PRO_1000186733"
FT   BINDING         156
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
FT   BINDING         159
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
SQ   SEQUENCE   199 AA;  22250 MW;  01CC212B195E89DC CRC64;
     MEQQETIHIS ISEAAQTHFR RLLEQQEENT NIRIFVVNPG TPNAECGVSY CPPNAVEETD
     TQFEYNGFSA FVDEISLPFL DEAEIDYVTD PMGSQLTLKA PNAKMRKVAD DAPFIERLDY
     VIQTQVNPQL ASHGGRVTLI EVTEDKYAIL QFGGGCNGCS MVDVTLKEGI EKQLLAMFPD
     ELAGVKDVTE HQRGEHSYY