ID   SUFE_PECAS              Reviewed;         138 AA.
AC   Q6D624;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=ECA1864;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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. {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; BX950851; CAG74767.1; -; Genomic_DNA.
DR   RefSeq; WP_011093434.1; NC_004547.2.
DR   AlphaFoldDB; Q6D624; -.
DR   SMR; Q6D624; -.
DR   STRING; 218491.ECA1864; -.
DR   EnsemblBacteria; CAG74767; CAG74767; ECA1864.
DR   GeneID; 57209429; -.
DR   KEGG; eca:ECA1864; -.
DR   PATRIC; fig|218491.5.peg.1893; -.
DR   eggNOG; COG2166; Bacteria.
DR   HOGENOM; CLU_124502_1_1_6; -.
DR   OMA; DWMQRYE; -.
DR   OrthoDB; 1996347at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000007966; 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; Reference proteome.
FT   CHAIN           1..138
FT                   /note="Cysteine desulfuration protein SufE"
FT                   /id="PRO_0000202128"
FT   ACT_SITE        51
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ   SEQUENCE   138 AA;  15480 MW;  83C92AC21E28DE47 CRC64;
     MASLPEPQKL ARNFARCNDW EEKYLYVIEL GERLDPLPDE WRNPENLISG CQSQVWIVTQ
     PDEQGVLILH GDSDAAIVKG LIAVVFSLYQ GLTAQEIVEL DVRPFFESLA LNQHLTPSRS
     QGLEAMLRAI RAHAAALL