NFUA_ECOLI
ID NFUA_ECOLI Reviewed; 191 AA.
AC P63020; P46847; Q2M779;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fe/S biogenesis protein NfuA;
GN Name=nfuA; Synonyms=gntY {ECO:0000303|PubMed:9871335}, yhgI;
GN OrderedLocusNames=b3414, JW3377;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PRELIMINARY FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9871335;
RX DOI=10.1002/(sici)1521-4028(199811)38:5/6<395::aid-jobm395>3.0.co;2-7;
RA Porco A., Alonso G., Isturiz T.;
RT "The gluconate high affinity transport of GntI in Escherichia coli involves
RT a multicomponent complex system.";
RL J. Basic Microbiol. 38:395-404(1998).
RN [4]
RP INDUCTION BY HEAT-SHOCK AND MISFOLDED PROTEINS.
RX PubMed=11917152; DOI=10.1093/protein/15.2.153;
RA Lesley S.A., Graziano J., Cho C.Y., Knuth M.W., Klock H.E.;
RT "Gene expression response to misfolded protein as a screen for soluble
RT recombinant protein.";
RL Protein Eng. 15:153-160(2002).
RN [5]
RP INDUCTION BY IRON DEPLETION CONDITIONS.
RX PubMed=12746439; DOI=10.1074/jbc.m303381200;
RA McHugh J.P., Rodriguez-Quinones F., Abdul-Tehrani H., Svistunenko D.A.,
RA Poole R.K., Cooper C.E., Andrews S.C.;
RT "Global iron-dependent gene regulation in Escherichia coli. A new mechanism
RT for iron homeostasis.";
RL J. Biol. Chem. 278:29478-29486(2003).
RN [6]
RP DISRUPTION PHENOTYPE, AND ROLE IN THE USE OF DNA AS A NUTRIENT.
RC STRAIN=K12 / W3110 / ZK126;
RX PubMed=16707682; DOI=10.1128/jb.01974-05;
RA Palchevskiy V., Finkel S.E.;
RT "Escherichia coli competence gene homologs are essential for competitive
RT fitness and the use of DNA as a nutrient.";
RL J. Bacteriol. 188:3902-3910(2006).
RN [7]
RP FUNCTION IN FE/S BIOGENESIS, IRON-SULFUR CLUSTER BINDING, SUBUNIT,
RP INDUCTION BY OXIDATIVE STRESS AND IRON STARVATION, DOMAIN, AND MUTAGENESIS
RP OF CYS-39; CYS-44; CYS-149 AND CYS-152.
RX PubMed=18339628; DOI=10.1074/jbc.m709405200;
RA Angelini S., Gerez C., Ollagnier-de Choudens S., Sanakis Y., Fontecave M.,
RA Barras F., Py B.;
RT "NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli
RT under oxidative stress and iron starvation conditions.";
RL J. Biol. Chem. 283:14084-14091(2008).
CC -!- FUNCTION: Involved in iron-sulfur cluster biogenesis under severe
CC conditions such as iron starvation or oxidative stress. 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. Required for E.coli to
CC sustain oxidative stress and iron starvation. Also necessary for the
CC use of extracellular DNA as the sole source of carbon and energy.
CC {ECO:0000269|PubMed:16707682, ECO:0000269|PubMed:18339628}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably
CC bound at the interface of two monomers.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18339628}.
CC -!- INDUCTION: Up-regulated under conditions of iron depletion or oxidative
CC stress, via IscR. Is also induced by heat shock or the presence of
CC misfolded proteins. {ECO:0000269|PubMed:11917152,
CC ECO:0000269|PubMed:12746439, ECO:0000269|PubMed:18339628}.
CC -!- DOMAIN: Consits of two domains, an N-terminal domain that resembles the
CC so-called Fe/S A-type scaffold, and a C-terminal domain that shares
CC sequence identity with Nfu-type scaffold proteins. Both domains are
CC important for NfuA to fulfill its function in vivo. The N-terminal
CC domain does not possess the three conserved cysteine residues thought
CC to act as Fe/S cluster ligands in A-type scaffold proteins, but may
CC keep the ability to interact with apoproteins.
CC {ECO:0000269|PubMed:18339628}.
CC -!- DISRUPTION PHENOTYPE: Cells express the stationary phase-specific
CC competition-defective (SPCD) phenotype and are unable to catabolize
CC dsDNA. {ECO:0000269|PubMed:16707682}.
CC -!- SIMILARITY: Belongs to the NfuA family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in gluconate metabolism
CC and was referred to as GntY. {ECO:0000305|PubMed:9871335}.
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DR EMBL; U18997; AAA58212.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76439.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77877.1; -; Genomic_DNA.
DR PIR; A65137; A65137.
DR RefSeq; NP_417873.1; NC_000913.3.
DR RefSeq; WP_000619389.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P63020; -.
DR SMR; P63020; -.
DR BioGRID; 4261219; 424.
DR BioGRID; 852234; 1.
DR DIP; DIP-48001N; -.
DR IntAct; P63020; 13.
DR STRING; 511145.b3414; -.
DR SWISS-2DPAGE; P63020; -.
DR jPOST; P63020; -.
DR PaxDb; P63020; -.
DR PRIDE; P63020; -.
DR EnsemblBacteria; AAC76439; AAC76439; b3414.
DR EnsemblBacteria; BAE77877; BAE77877; BAE77877.
DR GeneID; 67417042; -.
DR GeneID; 947925; -.
DR KEGG; ecj:JW3377; -.
DR KEGG; eco:b3414; -.
DR PATRIC; fig|1411691.4.peg.3314; -.
DR EchoBASE; EB2771; -.
DR eggNOG; COG0316; Bacteria.
DR eggNOG; COG0694; Bacteria.
DR HOGENOM; CLU_094569_0_0_6; -.
DR InParanoid; P63020; -.
DR OMA; CLAYCRP; -.
DR PhylomeDB; P63020; -.
DR BioCyc; EcoCyc:G7748-MON; -.
DR BioCyc; MetaCyc:G7748-MON; -.
DR PRO; PR:P63020; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0140132; F:iron-sulfur cluster carrier activity; IDA:EcoCyc.
DR GO; GO:0015976; P:carbon utilization; IMP:EcoCyc.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoliWiki.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IDA:EcoCyc.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..191
FT /note="Fe/S biogenesis protein NfuA"
FT /id="PRO_0000209464"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="C->S: No effect on activity in vivo. Still able to
FT bind a Fe/S cluster in vitro."
FT /evidence="ECO:0000269|PubMed:18339628"
FT MUTAGEN 44
FT /note="C->S: No effect on activity in vivo."
FT /evidence="ECO:0000269|PubMed:18339628"
FT MUTAGEN 149
FT /note="C->S: Loss of activity in vivo. Still able to bind a
FT Fe/S cluster in vitro."
FT /evidence="ECO:0000269|PubMed:18339628"
FT MUTAGEN 152
FT /note="C->S: Loss of activity in vivo. Still able to bind a
FT Fe/S cluster in vitro."
FT /evidence="ECO:0000269|PubMed:18339628"
SQ SEQUENCE 191 AA; 20998 MW; 06874546ADA5A971 CRC64;
MIRISDAAQA HFAKLLANQE EGTQIRVFVI NPGTPNAECG VSYCPPDAVE ATDTALKFDL
LTAYVDELSA PYLEDAEIDF VTDQLGSQLT LKAPNAKMRK VADDAPLMER VEYMLQSQIN
PQLAGHGGRV SLMEITEDGY AILQFGGGCN GCSMVDVTLK EGIEKQLLNE FPELKGVRDL
TEHQRGEHSY Y
