ID   MGRB_ECOSE              Reviewed;          47 AA.
AC   B6IBQ3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=PhoP/PhoQ regulator MgrB {ECO:0000255|HAMAP-Rule:MF_01596};
GN   Name=mgrB {ECO:0000255|HAMAP-Rule:MF_01596}; OrderedLocusNames=ECSE_2000;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009240; BAG77524.1; -; Genomic_DNA.
DR   RefSeq; WP_000714550.1; NC_011415.1.
DR   AlphaFoldDB; B6IBQ3; -.
DR   SMR; B6IBQ3; -.
DR   EnsemblBacteria; BAG77524; BAG77524; ECSE_2000.
DR   GeneID; 66674285; -.
DR   KEGG; ecy:ECSE_2000; -.
DR   HOGENOM; CLU_208030_1_0_6; -.
DR   Proteomes; UP000008199; 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_1000201564"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01596"
SQ   SEQUENCE   47 AA;  5552 MW;  B1F03878D23CDDDE CRC64;
     MKKFRWVVLV VVVLACLLLW AQVFNMMCDQ DVQFFSGICA INQFIPW