NFUA_ACIAD
ID NFUA_ACIAD Reviewed; 212 AA.
AC Q6FDB8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=ACIAD1052;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67940.1; -; Genomic_DNA.
DR RefSeq; WP_004921688.1; NC_005966.1.
DR AlphaFoldDB; Q6FDB8; -.
DR SMR; Q6FDB8; -.
DR STRING; 62977.ACIAD1052; -.
DR EnsemblBacteria; CAG67940; CAG67940; ACIAD1052.
DR GeneID; 45233494; -.
DR KEGG; aci:ACIAD1052; -.
DR eggNOG; COG0694; Bacteria.
DR HOGENOM; CLU_094569_0_0_6; -.
DR OMA; CLAYCRP; -.
DR OrthoDB; 2010888at2; -.
DR BioCyc; ASP62977:ACIAD_RS04845-MON; -.
DR Proteomes; UP000000430; 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..212
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_0000209470"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01637"
SQ SEQUENCE 212 AA; 22998 MW; 219058324914FC82 CRC64;
MSTENTSTAV AEEIPNLLIT PSAQEYLGDL LEKQNTPGIG VRIFVENPGT PRAECCMAYS
APDEVNPADY KQEYSDFPAY IDAPSIPYLL DAVIDYNKDR FGGQLTFRAP NSKVPRVGPD
ASIEERITYI LQSEINPGLA GHGGNCALVE VQDDPENGLT AVLKFGGGCQ GCSAIDVTLK
QGVETTLRQQ IPELQRVVDQ TDHTQAEGAY FK
