ID   MGRB_ECOL6              Reviewed;          47 AA.
AC   Q8FGT7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=PhoP/PhoQ regulator MgrB {ECO:0000255|HAMAP-Rule:MF_01596};
GN   Name=mgrB {ECO:0000255|HAMAP-Rule:MF_01596}; OrderedLocusNames=c2234;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. Represses PhoP/PhoQ signaling,
CC       possibly by binding to the periplasmic domain of PhoQ, altering its
CC       activity and that of downstream effector PhoP. {ECO:0000255|HAMAP-
CC       Rule:MF_01596}.
CC   -!- SUBUNIT: May form homooligomers. Probably interacts with the
CC       periplasmic domain of PhoQ. {ECO:0000255|HAMAP-Rule:MF_01596}.
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; AE014075; AAN80693.1; -; Genomic_DNA.
DR   RefSeq; WP_000714544.1; NC_004431.1.
DR   AlphaFoldDB; Q8FGT7; -.
DR   STRING; 199310.c2234; -.
DR   EnsemblBacteria; AAN80693; AAN80693; c2234.
DR   KEGG; ecc:c2234; -.
DR   eggNOG; ENOG50333DF; Bacteria.
DR   HOGENOM; CLU_208030_1_0_6; -.
DR   BioCyc; ECOL199310:C2234-MON; -.
DR   Proteomes; UP000001410; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..47
FT                   /note="PhoP/PhoQ regulator MgrB"
FT                   /id="PRO_0000330672"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01596"
SQ   SEQUENCE   47 AA;  5524 MW;  337A0378D23CDDC0 CRC64;
     MKKFRWVALV VVVLACLLLW AQVFNMMCDQ DVQFFSGICA INQFIPW