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MGRB_SALT1
ID   MGRB_SALT1              Reviewed;          47 AA.
AC   D0ZK39;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=PhoP/PhoQ regulator MgrB {ECO:0000255|HAMAP-Rule:MF_01596};
GN   Name=yobG; Synonyms=mgrB; OrderedLocusNames=STM14_2226;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   FUNCTION.
RC   STRAIN=14028s / SGSC 2262;
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).
CC   -!- FUNCTION: PhoP-regulated transcription is redox-sensitive, being
CC       activated when the periplasm becomes more reducing. MgrB acts between
CC       DsbA/DsbB and PhoP/PhoQ in this pathway (Probable). Represses PhoP/PhoQ
CC       signaling, possibly by binding to the periplasmic domain of PhoQ,
CC       altering its activity and that of downstream effector PhoP.
CC       {ECO:0000255|HAMAP-Rule:MF_01596, ECO:0000269|PubMed:20041203,
CC       ECO:0000305}.
CC   -!- SUBUNIT: May form homooligomers. Probably interacts with the
CC       periplasmic domain of PhoQ (Probable). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01596}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01596}.
CC   -!- SIMILARITY: Belongs to the MgrB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01596}.
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DR   EMBL; CP001363; ACY88689.1; -; Genomic_DNA.
DR   RefSeq; WP_000714547.1; NZ_CP043402.1.
DR   AlphaFoldDB; D0ZK39; -.
DR   EnsemblBacteria; ACY88689; ACY88689; STM14_2226.
DR   GeneID; 66756315; -.
DR   KEGG; seo:STM14_2226; -.
DR   PATRIC; fig|588858.6.peg.2089; -.
DR   HOGENOM; CLU_208030_1_0_6; -.
DR   BioCyc; SENT588858:STM14_RS10095-MON; -.
DR   Proteomes; UP000002695; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070298; P:negative regulation of phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01596; MgrB; 1.
DR   InterPro; IPR020907; MgrB.
DR   Pfam; PF13998; MgrB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Repressor; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..47
FT                   /note="PhoP/PhoQ regulator MgrB"
FT                   /id="PRO_0000424531"
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:0000255"
SQ   SEQUENCE   47 AA;  5520 MW;  5A0469233478913F CRC64;
     MKKFRWVVLG IVVVVCLLLW AQVFNIMCDQ DVQFFSGICA INKFIPW
 
 
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