ID   NFUA_BUCAT              Reviewed;         192 AA.
AC   B8D868;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=BUAPTUC7_538;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(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; CP001158; ACL30333.1; -; Genomic_DNA.
DR   RefSeq; WP_010896157.1; NC_011834.1.
DR   AlphaFoldDB; B8D868; -.
DR   SMR; B8D868; -.
DR   KEGG; bau:BUAPTUC7_538; -.
DR   HOGENOM; CLU_094569_0_0_6; -.
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.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT   CHAIN           1..192
FT                   /note="Fe/S biogenesis protein NfuA"
FT                   /id="PRO_1000186740"
FT   BINDING         150
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
SQ   SEQUENCE   192 AA;  21439 MW;  979552D5FCFE8EA1 CRC64;
     MINISKKAQE HFTSLLSNEP ENTQIRVFIV NPGTPNAECG VAFCPENEIE LSDIQLKYDG
     FFVYVNKDTI SYLKNSVIDL VTDKIGSQLT LKAPYAKNNF SKKVSSSLEE KVKCFLNLEI
     NPQLSMHGGR VELIKIDKNG IAAIQFSGGC NGCSMIGSTL KETVEKKLLS SFSEIKKVYD
     ETHHLHGQHS FY