ID   SUFE_CROS8              Reviewed;         138 AA.
AC   A7MF58;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=ESA_02089;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77339.1; -; Genomic_DNA.
DR   RefSeq; WP_007783745.1; NC_009778.1.
DR   AlphaFoldDB; A7MF58; -.
DR   SMR; A7MF58; -.
DR   EnsemblBacteria; ABU77339; ABU77339; ESA_02089.
DR   GeneID; 45715819; -.
DR   GeneID; 56730853; -.
DR   KEGG; esa:ESA_02089; -.
DR   HOGENOM; CLU_124502_1_1_6; -.
DR   OMA; DWMQRYE; -.
DR   OrthoDB; 1996347at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000000260; 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_1000070442"
FT   ACT_SITE        51
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ   SEQUENCE   138 AA;  15617 MW;  AAF7B47EDC4F0D28 CRC64;
     MAGLPEKEKL LRNFNRCANW EEKYLYIIEL GQRLAPLDDA ERTPAHRIQG CQSQVWIVMN
     PGENGVIEMR GDSDAAIVKG LIAVVFALYQ QMTAQDIVNF DVRPWFEEMS LTQHLTPSRS
     QGLEAMIRAI RAKAADLS