MGRB_ECOLI
ID MGRB_ECOLI Reviewed; 47 AA.
AC P64512; P76267; Q2MB17;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=PhoP/PhoQ regulator MgrB {ECO:0000255|HAMAP-Rule:MF_01596};
GN Name=mgrB {ECO:0000255|HAMAP-Rule:MF_01596}; Synonyms=yobG;
GN OrderedLocusNames=b1826, JW1815;
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 INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10464230; DOI=10.1128/jb.181.17.5516-5520.1999;
RA Kato A., Tanabe H., Utsumi R.;
RT "Molecular characterization of the PhoP-PhoQ two-component system in
RT Escherichia coli K-12: identification of extracellular Mg2+-responsive
RT promoters.";
RL J. Bacteriol. 181:5516-5520(1999).
RN [4]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA Mori H., Ishihama A., Utsumi R.;
RT "Identification and molecular characterization of the Mg2+ stimulon of
RT Escherichia coli.";
RL J. Bacteriol. 185:3696-3702(2003).
RN [5]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17909183; DOI=10.1073/pnas.0700025104;
RA Miyashiro T., Goulian M.;
RT "Stimulus-dependent differential regulation in the Escherichia coli PhoQ-
RT PhoP system.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16305-16310(2007).
RN [6]
RP INDUCTION.
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 [7]
RP FUNCTION, PROBABLE INTERACTION WITH PHOQ, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20041203; DOI=10.1371/journal.pgen.1000788;
RA Lippa A.M., Goulian M.;
RT "Feedback inhibition in the PhoQ/PhoP signaling system by a membrane
RT peptide.";
RL PLoS Genet. 5:E1000788-E1000788(2009).
RN [8]
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 [9]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF CYS-16; CYS-28 AND CYS-39.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22267510; DOI=10.1128/jb.06055-11;
RA Lippa A.M., Goulian M.;
RT "Perturbation of the oxidizing environment of the periplasm stimulates the
RT PhoQ/PhoP system in Escherichia coli.";
RL J. Bacteriol. 194:1457-1463(2012).
CC -!- FUNCTION: Represses PhoP/PhoQ signaling, possibly by binding to the
CC periplasmic domain of PhoQ, altering its activity and that of
CC downstream effector PhoP. PhoP-regulated transcription is redox-
CC sensitive, being activated when the periplasm becomes more reducing
CC (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts
CC between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys
CC residues of MgrB are required for its action on PhoQ, and thus PhoP.
CC {ECO:0000269|PubMed:20041203, ECO:0000269|PubMed:22267510}.
CC -!- SUBUNIT: May form homooligomers. Probably interacts with the
CC periplasmic domain of PhoQ. {ECO:0000255|HAMAP-Rule:MF_01596,
CC ECO:0000269|PubMed:20041203}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20041203}; Single-pass membrane protein
CC {ECO:0000305|PubMed:20041203}.
CC -!- INDUCTION: Induced by low extracellular levels of Mg(2+) via the
CC PhoP/PhoQ two-component regulatory system (PubMed:10464230) (Probable).
CC In exponential phase (at protein level) (PubMed:19121005). By
CC dithiothreitol (PubMed:22267510). {ECO:0000269|PubMed:10464230,
CC ECO:0000269|PubMed:12813061, ECO:0000269|PubMed:17909183,
CC ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:19734316,
CC ECO:0000269|PubMed:22267510, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Induction of genes regulated by PhoP, not
CC suppressed by a dsbA deletion or 50 uM CuSO(4).
CC {ECO:0000269|PubMed:20041203}.
CC -!- SIMILARITY: Belongs to the MgrB family. {ECO:0000255|HAMAP-
CC Rule:MF_01596}.
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DR EMBL; U00096; AAC74896.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76539.1; -; Genomic_DNA.
DR PIR; B64944; B64944.
DR RefSeq; NP_416340.1; NC_000913.3.
DR RefSeq; WP_000714550.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P64512; -.
DR SMR; P64512; -.
DR BioGRID; 4261732; 6.
DR STRING; 511145.b1826; -.
DR PaxDb; P64512; -.
DR EnsemblBacteria; AAC74896; AAC74896; b1826.
DR EnsemblBacteria; BAE76539; BAE76539; BAE76539.
DR GeneID; 66674285; -.
DR GeneID; 946351; -.
DR KEGG; ecj:JW1815; -.
DR KEGG; eco:b1826; -.
DR PATRIC; fig|511145.12.peg.1903; -.
DR EchoBASE; EB4126; -.
DR eggNOG; ENOG50333DF; Bacteria.
DR HOGENOM; CLU_208030_1_0_6; -.
DR PhylomeDB; P64512; -.
DR BioCyc; EcoCyc:G7002-MON; -.
DR PRO; PR:P64512; -.
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:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; IMP:EcoCyc.
DR GO; GO:0044092; P:negative regulation of molecular function; IMP:EcoCyc.
DR GO; GO:0070298; P:negative regulation of phosphorelay signal transduction system; IDA:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR HAMAP; MF_01596; MgrB; 1.
DR InterPro; IPR020907; MgrB.
DR Pfam; PF13998; MgrB; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..47
FT /note="PhoP/PhoQ regulator MgrB"
FT /id="PRO_0000169066"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01596"
FT TOPO_DOM 27..47
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:20041203"
FT MUTAGEN 16
FT /note="C->A: Still represses PhoP-regulated transcription."
FT /evidence="ECO:0000269|PubMed:22267510"
FT MUTAGEN 28
FT /note="C->A: No longer represses PhoP-regulated
FT transcription."
FT /evidence="ECO:0000269|PubMed:22267510"
FT MUTAGEN 39
FT /note="C->A: No longer represses PhoP-regulated
FT transcription."
FT /evidence="ECO:0000269|PubMed:22267510"
SQ SEQUENCE 47 AA; 5552 MW; B1F03878D23CDDDE CRC64;
MKKFRWVVLV VVVLACLLLW AQVFNMMCDQ DVQFFSGICA INQFIPW
