MGTS_ECOLI
ID MGTS_ECOLI Reviewed; 31 AA.
AC A5A616;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Small protein MgtS {ECO:0000305};
GN Name=mgtS {ECO:0000303|PubMed:28512220}; Synonyms=yneM;
GN OrderedLocusNames=b4599, JW1527.1;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19121005; DOI=10.1111/j.1365-2958.2008.06495.x;
RA Hemm M.R., Paul B.J., Schneider T.D., Storz G., Rudd K.E.;
RT "Small membrane proteins found by comparative genomics and ribosome binding
RT site models.";
RL Mol. Microbiol. 70:1487-1501(2008).
RN [4]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19734316; DOI=10.1128/jb.00872-09;
RA Hemm M.R., Paul B.J., Miranda-Rios J., Zhang A., Soltanzad N., Storz G.;
RT "Small stress response proteins in Escherichia coli: proteins missed by
RT classical proteomic studies.";
RL J. Bacteriol. 192:46-58(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [6]
RP FUNCTION, INTERACTION WITH MGTA, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLY-19; LEU-21; SER-26; TRP-29; ASP-30 AND ASP-31.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28512220; DOI=10.1073/pnas.1703415114;
RA Wang H., Yin X., Wu Orr M., Dambach M., Curtis R., Storz G.;
RT "Increasing intracellular magnesium levels with the 31-amino acid MgtS
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:5689-5694(2017).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30837344; DOI=10.1128/mbio.02819-18;
RA Weaver J., Mohammad F., Buskirk A.R., Storz G.;
RT "Identifying small proteins by ribosome profiling with stalled initiation
RT complexes.";
RL MBio 10:0-0(2019).
RN [8] {ECO:0007744|PDB:5OQT, ECO:0007744|PDB:6F34}
RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS).
RX PubMed=29416041; DOI=10.1038/s41467-018-03066-6;
RA Jungnickel K.E.J., Parker J.L., Newstead S.;
RT "Structural basis for amino acid transport by the CAT family of SLC7
RT transporters.";
RL Nat. Commun. 9:550-550(2018).
CC -!- FUNCTION: Modulates intracellular Mg(2+) levels to maintain cellular
CC integrity upon Mg(2+) limitation. Acts by binding and stabilizing the
CC Mg(2+) transporter MgtA, thereby leading to increased intracellular
CC level of Mg(2+). May inhibit FtsH proteolysis of MgtA.
CC {ECO:0000269|PubMed:28512220}.
CC -!- SUBUNIT: Interacts with MgtA. {ECO:0000269|PubMed:28512220}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21778229,
CC ECO:0000305|PubMed:19121005}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21778229}.
CC -!- INDUCTION: Induced by very low Mg(2+) via the PhoQ/PhoP two-component
CC regulatory system (PubMed:28512220). Induced by SDS/EDTA (envelope
CC stress), at 45 degrees Celsius, repressed in minimal glucose or
CC glycerol medium and by the thiol oxidant diamide (at protein level)
CC (PubMed:19734316). Expressed in both exponential and stationary phase
CC in rich medium; expression is higher in exponential phase (at protein
CC level) (PubMed:30837344). {ECO:0000269|PubMed:19734316,
CC ECO:0000269|PubMed:28512220, ECO:0000269|PubMed:30837344}.
CC -!- DISRUPTION PHENOTYPE: Upon Mg(2+) depletion, deletion mutants have
CC lower intracellular Mg(2+) levels than wild-type cells.
CC {ECO:0000269|PubMed:28512220}.
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DR EMBL; U00096; ABP93445.1; -; Genomic_DNA.
DR EMBL; AP009048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000901367.1; NZ_STEB01000003.1.
DR RefSeq; YP_001165319.1; NC_000913.3.
DR PDB; 5OQT; X-ray; 2.86 A; C=1-31.
DR PDB; 6F34; X-ray; 3.13 A; C=1-27.
DR PDBsum; 5OQT; -.
DR PDBsum; 6F34; -.
DR AlphaFoldDB; A5A616; -.
DR SMR; A5A616; -.
DR STRING; 511145.b4599; -.
DR PaxDb; A5A616; -.
DR EnsemblBacteria; ABP93445; ABP93445; b4599.
DR GeneID; 5061497; -.
DR GeneID; 67372775; -.
DR KEGG; eco:b4599; -.
DR PATRIC; fig|511145.12.peg.1604; -.
DR eggNOG; ENOG5033MGC; Bacteria.
DR BioCyc; EcoCyc:MON0-766; -.
DR PRO; PR:A5A616; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0010350; P:cellular response to magnesium starvation; IEP:EcoCyc.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..31
FT /note="Small protein MgtS"
FT /id="PRO_0000311788"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21778229"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21778229"
FT MUTAGEN 19
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT MUTAGEN 21
FT /note="L->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT MUTAGEN 26
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT MUTAGEN 29
FT /note="W->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT MUTAGEN 30
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT MUTAGEN 31
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28512220"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:5OQT"
SQ SEQUENCE 31 AA; 3509 MW; 97E32C3AD73DD3B0 CRC64;
MLGNMNVFMA VLGIILFSGF LAAYFSHKWD D
