MZRA_ECOLI
ID MZRA_ECOLI Reviewed; 127 AA.
AC P42615; Q2M9B0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Modulator protein MzrA {ECO:0000255|HAMAP-Rule:MF_00904};
GN Name=mzrA {ECO:0000255|HAMAP-Rule:MF_00904}; Synonyms=ecfM, yqjB;
GN OrderedLocusNames=b3096, JW3067;
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;
RX PubMed=16861804; DOI=10.1271/bbb.60024;
RA Yamamoto K., Ishihama A.;
RT "Characterization of copper-inducible promoters regulated by CpxA/CpxR in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 70:1688-1695(2006).
RN [4]
RP FUNCTION, INTERACTION WITH ENVZ, SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION,
RP AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19432797; DOI=10.1111/j.1365-2958.2009.06728.x;
RA Gerken H., Charlson E.S., Cicirelli E.M., Kenney L.J., Misra R.;
RT "MzrA: a novel modulator of the EnvZ/OmpR two-component regulon.";
RL Mol. Microbiol. 72:1408-1422(2009).
RN [5]
RP FUNCTION, INTERACTION WITH ENVZ, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF ASP-51; LYS-67; ASP-74 AND ILE-78.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20889743; DOI=10.1128/jb.00855-10;
RA Gerken H., Misra R.;
RT "MzrA-EnvZ interactions in the periplasm influence the EnvZ/OmpR two-
RT component regulon.";
RL J. Bacteriol. 192:6271-6278(2010).
RN [6]
RP INTERACTION WITH ENVZ, AND SUBUNIT.
RX PubMed=29953503; DOI=10.1371/journal.pone.0199782;
RA Motz M., Jung K.;
RT "The role of polyproline motifs in the histidine kinase EnvZ.";
RL PLoS ONE 13:E0199782-E0199782(2018).
CC -!- FUNCTION: Modulates the activity of the EnvZ/OmpR two-component
CC regulatory system, probably by directly modulating EnvZ enzymatic
CC activity and increasing stability of phosphorylated OmpR. Links the
CC two-component systems CpxA/CpxR and EnvZ/OmpR. {ECO:0000255|HAMAP-
CC Rule:MF_00904, ECO:0000269|PubMed:19432797,
CC ECO:0000269|PubMed:20889743}.
CC -!- SUBUNIT: Interacts with EnvZ. {ECO:0000255|HAMAP-Rule:MF_00904,
CC ECO:0000269|PubMed:19432797, ECO:0000269|PubMed:20889743,
CC ECO:0000269|PubMed:29953503}.
CC -!- INTERACTION:
CC P42615; P0AEJ4: envZ; NbExp=3; IntAct=EBI-6412632, EBI-1121750;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00904, ECO:0000269|PubMed:19432797,
CC ECO:0000269|PubMed:20889743}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00904, ECO:0000269|PubMed:19432797,
CC ECO:0000269|PubMed:20889743}.
CC -!- INDUCTION: Regulated by the CpxA/CpxR two-component system. Negatively
CC regulated by EnvZ/OmpR. {ECO:0000269|PubMed:16861804,
CC ECO:0000269|PubMed:19432797}.
CC -!- DOMAIN: Interacts with EnvZ through its soluble periplasmic region.
CC {ECO:0000269|PubMed:20889743}.
CC -!- SIMILARITY: Belongs to the MzrA family. {ECO:0000255|HAMAP-
CC Rule:MF_00904}.
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DR EMBL; U18997; AAA57900.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76131.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77146.1; -; Genomic_DNA.
DR PIR; E65098; E65098.
DR RefSeq; NP_417567.1; NC_000913.3.
DR RefSeq; WP_001166760.1; NZ_SSZK01000007.1.
DR AlphaFoldDB; P42615; -.
DR SMR; P42615; -.
DR BioGRID; 4259422; 9.
DR IntAct; P42615; 1.
DR STRING; 511145.b3096; -.
DR PaxDb; P42615; -.
DR PRIDE; P42615; -.
DR EnsemblBacteria; AAC76131; AAC76131; b3096.
DR EnsemblBacteria; BAE77146; BAE77146; BAE77146.
DR GeneID; 947619; -.
DR KEGG; ecj:JW3067; -.
DR KEGG; eco:b3096; -.
DR PATRIC; fig|1411691.4.peg.3632; -.
DR EchoBASE; EB2597; -.
DR eggNOG; ENOG50333DY; Bacteria.
DR HOGENOM; CLU_153761_0_0_6; -.
DR OMA; WHHLDAN; -.
DR PhylomeDB; P42615; -.
DR BioCyc; EcoCyc:G7610-MON; -.
DR PRO; PR:P42615; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019901; F:protein kinase binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEP:EcoCyc.
DR HAMAP; MF_00904; Modulator_MzrA; 1.
DR InterPro; IPR026574; Modulator_MzrA.
DR InterPro; IPR027398; SecD-TM.
DR Pfam; PF13721; SecD-TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..127
FT /note="Modulator protein MzrA"
FT /id="PRO_0000169427"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00904"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00904"
FT TOPO_DOM 32..127
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00904"
FT MUTAGEN 51
FT /note="D->A: Loss of activity. Decreases interaction with
FT EnvZ."
FT /evidence="ECO:0000269|PubMed:20889743"
FT MUTAGEN 67
FT /note="K->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20889743"
FT MUTAGEN 74
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20889743"
FT MUTAGEN 78
FT /note="I->F: Loss of activity. Decreases interaction with
FT EnvZ."
FT /evidence="ECO:0000269|PubMed:20889743"
SQ SEQUENCE 127 AA; 14172 MW; 814A6F43756E7E86 CRC64;
MQIPRMSLRQ LAWSGAVLLL VGTLLLAWSA VRQQESTLAI RAVHQGTTMP DGFSIWHHLD
AHGIPFKSIT PKNDTLLITF DSSDQSAAAK AVLDRTLPHG YIIAQQDNNS QAMQWLTRLR
DNSHRFG
