NFUA_ACIBS
ID NFUA_ACIBS Reviewed; 212 AA.
AC B0VSR5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=ABSDF2422;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP01733.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VSR5; -.
DR SMR; B0VSR5; -.
DR EnsemblBacteria; CAP01733; CAP01733; ABSDF2422.
DR KEGG; abm:ABSDF2422; -.
DR HOGENOM; CLU_094569_0_0_6; -.
DR OMA; CLAYCRP; -.
DR Proteomes; UP000001741; 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..212
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_1000186730"
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; 23116 MW; CB3C5832048A7490 CRC64;
MSTENTNTAV AEEIPNLLIT PSAQEYLHEL LAKQNTPGIG VRIFVEHPGT PRAECCMAYS
APEEVVPTDY KQDYPDFPAY IDAPSIPYLL DAVIDYNKDR FGGQLTFRAP NSKVPRVGPD
ASIEERITYV LQAEINPGLA GHGGNCSLVE VQDDPEHGLT AVLKFGGGCQ GCSAIDVTLK
QGVETTLKEH ILELQRVVDQ TDHTQAEGAY FK
