ID   SUFE_ECOSM              Reviewed;         138 AA.
AC   B1LE57;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   OrderedLocusNames=EcSMS35_1517;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01832}.
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01832}.
CC   -!- SUBUNIT: Homodimer. Interacts with SufS. {ECO:0000255|HAMAP-
CC       Rule:MF_01832}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01832}.
CC   -!- SIMILARITY: Belongs to the SufE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01832}.
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DR   EMBL; CP000970; ACB16404.1; -; Genomic_DNA.
DR   RefSeq; WP_001196530.1; NC_010498.1.
DR   AlphaFoldDB; B1LE57; -.
DR   SMR; B1LE57; -.
DR   EnsemblBacteria; ACB16404; ACB16404; EcSMS35_1517.
DR   GeneID; 66674428; -.
DR   KEGG; ecm:EcSMS35_1517; -.
DR   HOGENOM; CLU_124502_1_1_6; -.
DR   OMA; DWMQRYE; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm.
FT   CHAIN           1..138
FT                   /note="Cysteine desulfuration protein SufE"
FT                   /id="PRO_1000188327"
FT   ACT_SITE        51
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ   SEQUENCE   138 AA;  15800 MW;  AD7B89A74C946772 CRC64;
     MALLPDKEKL LRNFLRCANW EEKYLYIIEL GQRLPELRDE DRSPQNSIQG CQSQVWIVMR
     QNAQGIIELQ GDSDAAIVKG LIAVVFILYD QMTPQDIVNF DVRPWFEKMA LTQHLTPSRS
     QGLEAMIRAI RAKAAALS