ID NFUA_ACTP2 Reviewed; 199 AA.
AC A3MYM1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=APL_0149;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(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; CP000569; ABN73257.1; -; Genomic_DNA.
DR RefSeq; WP_005600176.1; NC_009053.1.
DR AlphaFoldDB; A3MYM1; -.
DR SMR; A3MYM1; -.
DR STRING; 416269.APL_0149; -.
DR EnsemblBacteria; ABN73257; ABN73257; APL_0149.
DR GeneID; 69417316; -.
DR KEGG; apl:APL_0149; -.
DR eggNOG; COG0316; Bacteria.
DR eggNOG; COG0694; Bacteria.
DR HOGENOM; CLU_094569_0_0_6; -.
DR Proteomes; UP000001432; 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; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR Gene3D; 2.60.300.12; HesB-like domain; 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 NCBIfam; TIGR03341; YhgI_GntY; 1.
DR PANTHER; PTHR11178; IRON-SULFUR CLUSTER SCAFFOLD PROTEIN NFU-RELATED; 1.
DR PANTHER; PTHR11178:SF1; NFU1 IRON-SULFUR CLUSTER SCAFFOLD HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR Pfam; PF01106; NifU; 1.
DR SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR SUPFAM; SSF89360; HesB-like domain; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..199
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_0000292086"
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
//
