NFUA_RUTMC
ID NFUA_RUTMC Reviewed; 192 AA.
AC A1AW72;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637};
GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; OrderedLocusNames=Rmag_0417;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000488; ABL02179.1; -; Genomic_DNA.
DR RefSeq; WP_011737804.1; NC_008610.1.
DR AlphaFoldDB; A1AW72; -.
DR SMR; A1AW72; -.
DR STRING; 413404.Rmag_0417; -.
DR EnsemblBacteria; ABL02179; ABL02179; Rmag_0417.
DR KEGG; rma:Rmag_0417; -.
DR eggNOG; COG0316; Bacteria.
DR eggNOG; COG0694; Bacteria.
DR HOGENOM; CLU_094569_0_0_6; -.
DR OMA; CLAYCRP; -.
DR OrthoDB; 2010888at2; -.
DR Proteomes; UP000002587; 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; IPR034904; FSCA_dom_sf.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
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; Reference proteome.
FT CHAIN 1..192
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_1000186769"
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; 21209 MW; 9F029E3D3367B1D3 CRC64;
MFDITDEAKV YVADLFAQQD EKDLGLKVDV EKAGTPAAVV TFNFCFPKEL SKTYKKFEYE
GFYAYIDELN FEYLKDSEVA LKDAGTGKKL TITAPNTKGK EPKEDAPLEE KIKYVIAANI
NPGLASHGGF VELVEITKHM DVILNFGGGC QGCSSVKSTL EQGVEAQLKM SFPEIKSVRD
VTDHSNTDNA YI