ID   FETP_SALTY              Reviewed;          91 AA.
AC   P67617; Q8XFV6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable Fe(2+)-trafficking protein;
GN   Name=yggX; OrderedLocusNames=STM3111;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=LT2;
RX   PubMed=11416172; DOI=10.1073/pnas.151243198;
RA   Gralnick J.A., Downs D.M.;
RT   "Protection from superoxide damage associated with an increased level of
RT   the YggX protein in Salmonella enterica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8030-8035(2001).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF CYS-7.
RC   STRAIN=LT2;
RX   PubMed=12670952; DOI=10.1074/jbc.m301577200;
RA   Gralnick J.A., Downs D.M.;
RT   "The YggX protein of Salmonella enterica is involved in Fe(II) trafficking
RT   and minimizes the DNA damage caused by hydroxyl radicals: residue Cys-7 is
RT   essential for YggX function.";
RL   J. Biol. Chem. 278:20708-20715(2003).
RN   [4]
RP   FUNCTION.
RC   STRAIN=LT2;
RX   PubMed=15516576; DOI=10.1128/jb.186.22.7626-7634.2004;
RA   Skovran E., Lauhon C.T., Downs D.M.;
RT   "Lack of YggX results in chronic oxidative stress and uncovers subtle
RT   defects in Fe-S cluster metabolism in Salmonella enterica.";
RL   J. Bacteriol. 186:7626-7634(2004).
CC   -!- FUNCTION: Could be a mediator in iron transactions between iron
CC       acquisition and iron-requiring processes, such as synthesis and/or
CC       repair of Fe-S clusters in biosynthetic enzymes. Necessary to maintain
CC       high levels of aconitase under oxidative stress.
CC       {ECO:0000269|PubMed:11416172, ECO:0000269|PubMed:12670952,
CC       ECO:0000269|PubMed:15516576}.
CC   -!- SIMILARITY: Belongs to the Fe(2+)-trafficking protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL21986.1; -; Genomic_DNA.
DR   RefSeq; NP_462027.1; NC_003197.2.
DR   RefSeq; WP_000091706.1; NC_003197.2.
DR   PDB; 1XS8; NMR; -; A=1-91.
DR   PDBsum; 1XS8; -.
DR   AlphaFoldDB; P67617; -.
DR   SMR; P67617; -.
DR   STRING; 99287.STM3111; -.
DR   PaxDb; P67617; -.
DR   EnsemblBacteria; AAL21986; AAL21986; STM3111.
DR   GeneID; 1254634; -.
DR   GeneID; 66757416; -.
DR   KEGG; stm:STM3111; -.
DR   PATRIC; fig|99287.12.peg.3297; -.
DR   HOGENOM; CLU_170994_0_0_6; -.
DR   OMA; SKQTMLI; -.
DR   PhylomeDB; P67617; -.
DR   BioCyc; SENT99287:STM3111-MON; -.
DR   EvolutionaryTrace; P67617; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   Gene3D; 1.10.3880.10; -; 1.
DR   HAMAP; MF_00686; Fe_traffic_YggX; 1.
DR   InterPro; IPR007457; Fe_traffick_prot_YggX.
DR   InterPro; IPR036766; Fe_traffick_prot_YggX_sf.
DR   PANTHER; PTHR36965; PTHR36965; 1.
DR   Pfam; PF04362; Iron_traffic; 1.
DR   PIRSF; PIRSF029827; Fe_traffic_YggX; 1.
DR   SUPFAM; SSF111148; SSF111148; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..91
FT                   /note="Probable Fe(2+)-trafficking protein"
FT                   /id="PRO_0000214505"
FT   MUTAGEN         7
FT                   /note="C->S: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:12670952"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1XS8"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:1XS8"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:1XS8"
FT   HELIX           25..31
FT                   /evidence="ECO:0007829|PDB:1XS8"
FT   HELIX           36..53
FT                   /evidence="ECO:0007829|PDB:1XS8"
FT   HELIX           60..74
FT                   /evidence="ECO:0007829|PDB:1XS8"
SQ   SEQUENCE   91 AA;  10899 MW;  7A46E8736B81C375 CRC64;
     MSRTIFCTYL QRDAEGQDFQ LYPGELGKRI YNEISKDAWA QWQHKQTMLI NEKKLNMMNA
     EHRKLLEQEM VSFLFEGKDV HIEGYTPEDK K