ID   SUFE_PHOLL              Reviewed;         138 AA.
AC   Q7N3U6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN   Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=plu2617;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571867; CAE14991.1; -; Genomic_DNA.
DR   RefSeq; WP_011146839.1; NC_005126.1.
DR   AlphaFoldDB; Q7N3U6; -.
DR   SMR; Q7N3U6; -.
DR   STRING; 243265.plu2617; -.
DR   EnsemblBacteria; CAE14991; CAE14991; plu2617.
DR   GeneID; 24166042; -.
DR   KEGG; plu:plu2617; -.
DR   eggNOG; COG2166; Bacteria.
DR   HOGENOM; CLU_124502_1_1_6; -.
DR   OMA; DWMQRYE; -.
DR   OrthoDB; 1996347at2; -.
DR   BioCyc; PLUM243265:PLU_RS12965-MON; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000002514; 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_0000202129"
FT   ACT_SITE        51
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ   SEQUENCE   138 AA;  15868 MW;  6A310C76FD555832 CRC64;
     MASLPDTNKL LRNFSRCRNW EERYLYMIEL GAKLPPLTDE QRQPENLIAG CQSQVWILLR
     MNHQNKVEFI GDSDAAIVKG LVAIVFILFQ GKTTQEILDL DVTEYFGKLS LEQHLTPSRT
     QGLHAMIHAI RNRTSKMV