SUFE_ECOLI
ID SUFE_ECOLI Reviewed; 138 AA.
AC P76194; Q2MB56;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cysteine desulfuration protein SufE;
GN Name=sufE; Synonyms=ynhA; OrderedLocusNames=b1679, JW1669;
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 GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10322040; DOI=10.1128/jb.181.10.3307-3309.1999;
RA Patzer S.I., Hantke K.;
RT "SufS is a NifS-like protein, and SufD is necessary for stability of the
RT 2Fe-2S FhuF protein in Escherichia coli.";
RL J. Bacteriol. 181:3307-3309(1999).
RN [4]
RP FUNCTION, INTERACTION WITH SUFS, AND MUTAGENESIS OF CYS-51.
RC STRAIN=K12 / TG1;
RX PubMed=12876288; DOI=10.1074/jbc.m305953200;
RA Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.;
RT "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form
RT a new type of cysteine desulfurase.";
RL J. Biol. Chem. 278:38352-38359(2003).
RN [5]
RP FUNCTION, INTERACTION WITH SUFS, AND MUTAGENESIS OF CYS-51.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12941942; DOI=10.1074/jbc.m308004200;
RA Outten F.W., Wood M.J., Munoz F.M., Storz G.;
RT "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase
RT activity as part of a sulfur transfer pathway for Fe-S cluster assembly in
RT Escherichia coli.";
RL J. Biol. Chem. 278:45713-45719(2003).
RN [6]
RP FUNCTION, INTERACTION WITH SUFS, AND MUTAGENESIS OF CYS-51.
RX PubMed=14644425; DOI=10.1016/s0014-5793(03)01244-4;
RA Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E.,
RA Fontecave M.;
RT "Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for
RT sulfur transfer from SufS to SufE.";
RL FEBS Lett. 555:263-267(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=15522304; DOI=10.1016/j.jmb.2004.08.074;
RA Goldsmith-Fischman S., Kuzin A., Edstrom W.C., Benach J., Shastry R.,
RA Xiao R., Acton T.B., Honig B., Montelione G.T., Hunt J.F.;
RT "The SufE sulfur-acceptor protein contains a conserved core structure that
RT mediates interdomain interactions in a variety of redox protein
RT complexes.";
RL J. Mol. Biol. 344:549-565(2004).
CC -!- FUNCTION: Participates in cysteine desulfuration mediated by SufS.
CC Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-
CC alanine and constitutes an essential step in sulfur metabolism for
CC biosynthesis of a variety of sulfur-containing biomolecules. Functions
CC as a sulfur acceptor for SufS, by mediating the direct transfer of the
CC sulfur atom from the S-sulfanylcysteine of SufS, an intermediate
CC product of cysteine desulfuration process. Together with the SufBCD
CC complex, it thereby enhances up to 50-fold, the cysteine desulfurase
CC activity of SufS. Component of the suf operon, which is activated and
CC required under specific conditions such as oxidative stress and iron
CC limitation. Does not affect the selenocysteine lyase activity of SufS.
CC {ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942,
CC ECO:0000269|PubMed:14644425}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Homodimer. Interacts with SufS. {ECO:0000269|PubMed:12876288,
CC ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:14644425}.
CC -!- INTERACTION:
CC P76194; P77444: sufS; NbExp=3; IntAct=EBI-1124973, EBI-1124981;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Suf operon is under both the Fe-dependent Fur repressor and
CC the oxidative stress dependent OxyR activator.
CC -!- SIMILARITY: Belongs to the SufE family. {ECO:0000305}.
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DR EMBL; U00096; AAC74749.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76500.1; -; Genomic_DNA.
DR PIR; G64925; G64925.
DR RefSeq; NP_416194.1; NC_000913.3.
DR RefSeq; WP_001196530.1; NZ_STEB01000003.1.
DR PDB; 1MZG; X-ray; 2.00 A; A/B=1-138.
DR PDBsum; 1MZG; -.
DR AlphaFoldDB; P76194; -.
DR SMR; P76194; -.
DR BioGRID; 4260278; 38.
DR ComplexPortal; CPX-2125; SufE complex.
DR DIP; DIP-10941N; -.
DR IntAct; P76194; 9.
DR STRING; 511145.b1679; -.
DR jPOST; P76194; -.
DR PaxDb; P76194; -.
DR PRIDE; P76194; -.
DR EnsemblBacteria; AAC74749; AAC74749; b1679.
DR EnsemblBacteria; BAE76500; BAE76500; BAE76500.
DR GeneID; 66674428; -.
DR GeneID; 946173; -.
DR KEGG; ecj:JW1669; -.
DR KEGG; eco:b1679; -.
DR PATRIC; fig|1411691.4.peg.579; -.
DR EchoBASE; EB3719; -.
DR eggNOG; COG2166; Bacteria.
DR HOGENOM; CLU_124502_1_1_6; -.
DR InParanoid; P76194; -.
DR OMA; DWMQRYE; -.
DR PhylomeDB; P76194; -.
DR BioCyc; EcoCyc:G6905-MON; -.
DR BioCyc; MetaCyc:G6905-MON; -.
DR UniPathway; UPA00266; -.
DR EvolutionaryTrace; P76194; -.
DR PRO; PR:P76194; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990228; C:sulfurtransferase complex; IPI:ComplexPortal.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0097163; F:sulfur carrier activity; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0031162; P:sulfur incorporation into metallo-sulfur cluster; IDA:ComplexPortal.
DR HAMAP; MF_01832; SufE; 1.
DR InterPro; IPR023939; Cysteine_desulfuration_SufE.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR PANTHER; PTHR43597; PTHR43597; 1.
DR Pfam; PF02657; SufE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..138
FT /note="Cysteine desulfuration protein SufE"
FT /id="PRO_0000202124"
FT ACT_SITE 51
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 51
FT /note="C->S: Abolishes cysteine desulfurase activity."
FT /evidence="ECO:0000269|PubMed:12876288,
FT ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:14644425"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1MZG"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1MZG"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1MZG"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1MZG"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1MZG"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1MZG"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1MZG"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:1MZG"
SQ SEQUENCE 138 AA; 15800 MW; AD7B89A74C946772 CRC64;
MALLPDKEKL LRNFLRCANW EEKYLYIIEL GQRLPELRDE DRSPQNSIQG CQSQVWIVMR
QNAQGIIELQ GDSDAAIVKG LIAVVFILYD QMTPQDIVNF DVRPWFEKMA LTQHLTPSRS
QGLEAMIRAI RAKAAALS
