ID   SUFE_ECOK1              Reviewed;         138 AA.
AC   A1ABL7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=Ecok1_15630;
GN   ORFNames=APECO1_756;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01057.1; -; Genomic_DNA.
DR   RefSeq; WP_001196521.1; NC_008563.1.
DR   AlphaFoldDB; A1ABL7; -.
DR   SMR; A1ABL7; -.
DR   EnsemblBacteria; ABJ01057; ABJ01057; APECO1_756.
DR   KEGG; ecv:APECO1_756; -.
DR   HOGENOM; CLU_124502_1_1_6; -.
DR   OMA; DWMQRYE; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000008216; 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_1000070438"
FT   ACT_SITE        51
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ   SEQUENCE   138 AA;  15781 MW;  8912AFE53F950355 CRC64;
     MALLPDKEKL LRNFLRCANW EEKYLYIIEL GQRLPELRDE DKSPQNSIQG CQSQVWIVMR
     QNAQGIIELH GDSDAAIVKG LIAVVFILYD QMTPQDIVNF DVRPWFEKMA LTQHLTPSRS
     QGLEAMIRAI RAKAAALS