PHOQ_ECOLI
ID PHOQ_ECOLI Reviewed; 486 AA.
AC P23837;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Sensor protein PhoQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
DE AltName: Full=Sensor histidine protein kinase/phosphatase PhoQ;
GN Name=phoQ; OrderedLocusNames=b1129, JW1115;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1729240; DOI=10.1128/jb.174.2.492-498.1992;
RA Kasahara M., Nakata A., Shinagawa H.;
RT "Molecular analysis of the Escherichia coli phoP-phoQ operon.";
RL J. Bacteriol. 174:492-498(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC STRAIN=K12;
RX PubMed=1530848; DOI=10.1128/jb.174.2.486-491.1992;
RA Groisman E.A., Heffron F., Solomon F.;
RT "Molecular genetic analysis of the Escherichia coli phoP locus.";
RL J. Bacteriol. 174:486-491(1992).
RN [6]
RP PROTEIN SEQUENCE OF 43-190, SECONDARY STRUCTURE OF SENSOR DOMAIN, AND
RP MUTAGENESIS OF 148-GLU--GLU-154.
RC STRAIN=BL21-DE3, and K12 / CSH26;
RX PubMed=8900137; DOI=10.1074/jbc.271.43.26630;
RA Waldburger C.D., Sauer R.T.;
RT "Signal detection by the PhoQ sensor-transmitter. Characterization of the
RT sensor domain and a response-impaired mutant that identifies ligand-binding
RT determinants.";
RL J. Biol. Chem. 271:26630-26636(1996).
RN [7]
RP FUNCTION, AND INDUCTION BY LOW MG(2+).
RC STRAIN=K12 / MC4100 / JA176;
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 [8]
RP MUTAGENESIS OF SENSOR PERIPLASMIC DOMAIN, AND MUTAGENESIS OF THR-48.
RC STRAIN=K12 / CSH26;
RX PubMed=12218035; DOI=10.1128/jb.184.19.5468-5478.2002;
RA Regelmann A.G., Lesley J.A., Mott C., Stokes L., Waldburger C.D.;
RT "Mutational analysis of the Escherichia coli PhoQ sensor kinase:
RT differences with the Salmonella enterica serovar Typhimurium PhoQ protein
RT and in the mechanism of Mg2+ and Ca2+ sensing.";
RL J. Bacteriol. 184:5468-5478(2002).
RN [9]
RP ACTIVITY REGULATION, AND KINETIC PARAMETERS.
RC STRAIN=K12 / CSH26;
RX PubMed=12670981; DOI=10.1128/jb.185.8.2563-2570.2003;
RA Lesley J.A., Waldburger C.D.;
RT "Repression of Escherichia coli PhoP-PhoQ signaling by acetate reveals a
RT regulatory role for acetyl coenzyme A.";
RL J. Bacteriol. 185:2563-2570(2003).
RN [10]
RP GENOME-WIDE ANALYSIS, AND REGULATION BY MG(2+).
RC STRAIN=K12 / MC4100 / JA176;
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 [11]
RP GENOME-WIDE ANALYSIS.
RC STRAIN=K12 / ST001;
RX PubMed=13129944; DOI=10.1128/jb.185.19.5735-5746.2003;
RA Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
RA Mizuno T.;
RT "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB
RT phosphorelay system in Escherichia coli.";
RL J. Bacteriol. 185:5735-5746(2003).
RN [12]
RP INTERACTION WITH EVGA/EVGS.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=15126461; DOI=10.1128/jb.186.10.3006-3014.2004;
RA Eguchi Y., Okada T., Minagawa S., Oshima T., Mori H., Yamamoto K.,
RA Ishihama A., Utsumi R.;
RT "Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component
RT systems of Escherichia coli.";
RL J. Bacteriol. 186:3006-3014(2004).
RN [13]
RP MUTAGENESIS OF THR-47; ASN-68; ASP-90; ASP-149; ASP-150; ASP-151; ASP-152
RP AND ASP-179.
RC STRAIN=BL21-DE3, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16041131; DOI=10.1271/bbb.69.1281;
RA Minagawa S., Okura R., Tsuchitani H., Hirao K., Yamamoto K., Utsumi R.;
RT "Isolation and molecular characterization of the locked-on mutant of Mg(2+)
RT sensor PhoQ in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 69:1281-1287(2005).
RN [14]
RP REGULATION OF ACID RESISTANCE GENES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15703297; DOI=10.1073/pnas.0408238102;
RA Zwir I., Shin D., Kato A., Nishino K., Latifi T., Solomon F., Hare J.M.,
RA Huang H., Groisman E.A.;
RT "Dissecting the PhoP regulatory network of Escherichia coli and Salmonella
RT enterica.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2862-2867(2005).
RN [15]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [16]
RP ACTIVITY REGULATION, AND PROBABLE INTERACTION WITH MGRB.
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 [17]
RP ACTIVITY REGULATION, AND INDUCTION.
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).
RN [18]
RP MUTAGENESIS OF VAL-27; LEU-30; LEU-199; ASN-202; LEU-203 AND LEU-205, AND
RP ROLE OF ASN-202 IN SIGNALING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20404199; DOI=10.1073/pnas.1003166107;
RA Goldberg S.D., Clinthorne G.D., Goulian M., DeGrado W.F.;
RT "Transmembrane polar interactions are required for signaling in the
RT Escherichia coli sensor kinase PhoQ.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8141-8146(2010).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 335-486 IN COMPLEX WITH ATP
RP ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, MG(2+)-BINDING, AND MUTAGENESIS OF
RP LYS-392; ARG-434 AND ARG-439.
RC STRAIN=BL21;
RX PubMed=11493605; DOI=10.1074/jbc.m106080200;
RA Marina A., Mott C., Auyzenberg A., Hendrickson W.A., Waldburger C.D.;
RT "Structural and mutational analysis of the PhoQ histidine kinase catalytic
RT domain. Insight into the reaction mechanism.";
RL J. Biol. Chem. 276:41182-41190(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-190 OF WILD-TYPE IN COMPLEX
RP WITH NICKEL IONS AND MUTANT 148-GLN-ASN-ASN-ASN-ASN-ALA-GLN-154, SUBUNIT,
RP PERIPLASMIC SENSOR DOMAIN, AND MUTAGENESIS OF ARG-50; GLY-54 AND ASP-179.
RC STRAIN=K12 / CSH26;
RX PubMed=18348979; DOI=10.1074/jbc.m710592200;
RA Cheung J., Bingman C.A., Reyngold M., Hendrickson W.A., Waldburger C.D.;
RT "Crystal structure of a functional dimer of the PhoQ sensor domain.";
RL J. Biol. Chem. 283:13762-13770(2008).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ
CC involved in adaptation to low Mg(2+) environments and the control of
CC acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a
CC membrane-associated protein kinase that undergoes autophosphorylation
CC and subsequently transfers the phosphate to PhoP, resulting in the
CC expression of PhoP-activated genes (PAG) and repression of PhoP-
CC repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein
CC phosphatase that dephosphorylates phospho-PhoP, resulting in the
CC repression of PAG and may lead to expression of some PRG (By
CC similarity). PhoP-regulated transcription is redox-sensitive, being
CC activated when the periplasm becomes more reducing (deletion of
CC dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between
CC DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues
CC of MgrB are required for its action on PhoQ, which then acts on PhoP.
CC Mediates magnesium influx to the cytosol by activation of mgtA.
CC Promotes expression of the two-component regulatory system rstA/rstB
CC and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.
CC {ECO:0000250, ECO:0000269|PubMed:10464230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Acetyl-CoA acts as a non-competitive inhibitor of
CC the PhoQ autokinase activity. Feedback inhibited by MgrB, which seems
CC to bind PhoQ, altering its activity and that of downstream effector
CC PhoP. {ECO:0000269|PubMed:12670981, ECO:0000269|PubMed:20041203,
CC ECO:0000269|PubMed:22267510}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.93 uM for ATP (at 22 degrees Celsius and pH 8, in the presence
CC of 50 mM KCl and 1 mM MgCl(2)) {ECO:0000269|PubMed:11493605,
CC ECO:0000269|PubMed:12670981};
CC KM=55 uM for ATP (at 22 degrees Celsius and pH 8, in the presence of
CC 25 mM KCl and 0.4 mM MgCl(2)) {ECO:0000269|PubMed:11493605,
CC ECO:0000269|PubMed:12670981};
CC -!- SUBUNIT: Homodimer; probably dimerizes via the cytoplasmic domain
CC (Probable). Probably interacts with MgrB in the periplasm, altering its
CC activity and that of downstream effector PhoP.
CC {ECO:0000269|PubMed:11493605, ECO:0000269|PubMed:15126461,
CC ECO:0000269|PubMed:18348979, ECO:0000305}.
CC -!- INTERACTION:
CC P23837; P23837: phoQ; NbExp=2; IntAct=EBI-1113605, EBI-1113605;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: The phoP/phoQ operon is positively autoregulated by both
CC PhoP and PhoQ in a Mg(2+)-dependent manner, inhibited at high Mg(2+)
CC concentrations (PubMed:10464230). Induced by dsbA disruption and
CC dithiothreitol (PubMed:22267510). {ECO:0000269|PubMed:10464230,
CC ECO:0000269|PubMed:22267510}.
CC -!- MISCELLANEOUS: There is a close linkage between the PhoP/PhoQ and Rcs
CC signaling systems, and both signaling systems respond to certain
CC external divalent cations (zinc and magnesium).
CC -!- MISCELLANEOUS: Two-component regulatory system EvgA/EvgS interacts with
CC PhoP/PhoQ via signal transduction mediated by phospho-EvgA.
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DR EMBL; D90393; BAA14391.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74213.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35951.1; -; Genomic_DNA.
DR EMBL; M81433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B41966; B41966.
DR RefSeq; NP_415647.1; NC_000913.3.
DR RefSeq; WP_000735412.1; NZ_STEB01000016.1.
DR PDB; 1ID0; X-ray; 1.60 A; A=335-486.
DR PDB; 3BQ8; X-ray; 2.50 A; A/B=43-190.
DR PDB; 3BQA; X-ray; 2.00 A; A/B=43-190.
DR PDB; 6A8U; X-ray; 1.85 A; A/B=43-190.
DR PDB; 6A8V; X-ray; 2.70 A; A/B=43-190.
DR PDBsum; 1ID0; -.
DR PDBsum; 3BQ8; -.
DR PDBsum; 3BQA; -.
DR PDBsum; 6A8U; -.
DR PDBsum; 6A8V; -.
DR AlphaFoldDB; P23837; -.
DR SMR; P23837; -.
DR BioGRID; 4260662; 3.
DR DIP; DIP-10501N; -.
DR IntAct; P23837; 2.
DR STRING; 511145.b1129; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR jPOST; P23837; -.
DR PaxDb; P23837; -.
DR PRIDE; P23837; -.
DR EnsemblBacteria; AAC74213; AAC74213; b1129.
DR EnsemblBacteria; BAA35951; BAA35951; BAA35951.
DR GeneID; 66670604; -.
DR GeneID; 946326; -.
DR KEGG; ecj:JW1115; -.
DR KEGG; eco:b1129; -.
DR PATRIC; fig|1411691.4.peg.1137; -.
DR EchoBASE; EB0725; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_42_0_6; -.
DR InParanoid; P23837; -.
DR OMA; TLVFIYD; -.
DR PhylomeDB; P23837; -.
DR BioCyc; EcoCyc:PHOQ-MON; -.
DR BioCyc; MetaCyc:PHOQ-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR SABIO-RK; P23837; -.
DR EvolutionaryTrace; P23837; -.
DR PRO; PR:P23837; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IMP:EcoCyc.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc.
DR GO; GO:0010350; P:cellular response to magnesium starvation; IMP:EcoCyc.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IMP:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR Gene3D; 3.30.450.140; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR015014; PhoQ_Sensor.
DR InterPro; IPR038429; PhoQ_Sensor_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08918; PhoQ_Sensor; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Hydrolase; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..486
FT /note="Sensor protein PhoQ"
FT /id="PRO_0000074837"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..194
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 215..266
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 274..480
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 385..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 415..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 434..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT SITE 202
FT /note="Plays a critical role in the switching between
FT kinase and phosphatase states"
FT MOD_RES 277
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 27
FT /note="V->N: Shows Mg(2+)-dependent signaling and partial
FT gene activation activity; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 30
FT /note="L->N: Shows Mg(2+)-dependent signaling and displays
FT higher gene activation activity than wild-type; when
FT associated with A-202."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 47
FT /note="T->L: No significant effect (with or without MgCl(2)
FT or CaCl(2))."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 48
FT /note="T->A,C,E,M,N,Q,S,V: No significant effect (with or
FT without MgCl(2) or CaCl(2))."
FT /evidence="ECO:0000269|PubMed:12218035"
FT MUTAGEN 48
FT /note="T->D,G,H,I,K,L,P,R: Confers less than 30% of the
FT wild-type levels of PhoP/PhoQ-signaling cascade in absence
FT of CaCl(2) or MgCl(2)."
FT /evidence="ECO:0000269|PubMed:12218035"
FT MUTAGEN 48
FT /note="T->F,W: Decreased sensitivity to repression by
FT calcium but not by magnesium."
FT /evidence="ECO:0000269|PubMed:12218035"
FT MUTAGEN 48
FT /note="T->Y: Higher activity than wild-type (with or
FT without MgCl(2) or CaCl(2))."
FT /evidence="ECO:0000269|PubMed:12218035"
FT MUTAGEN 50
FT /note="R->D: Large decrease in the transcriptional
FT activation of PhoQ-dependent genes."
FT /evidence="ECO:0000269|PubMed:18348979"
FT MUTAGEN 54
FT /note="G->D: Very large decrease in the transcriptional
FT activation of PhoQ-dependent genes."
FT /evidence="ECO:0000269|PubMed:18348979"
FT MUTAGEN 68
FT /note="N->L: No significant effect (with or without MgCl(2)
FT or CaCl(2))."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 90
FT /note="D->A: No significant effect (with or without MgCl(2)
FT or CaCl(2))."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 148..154
FT /note="EDDDDAE->QNNNNAQ: Unable to bind divalent cations in
FT vitro and impaired in the ability to respond to Mg(2+)
FT deprivation in vivo."
FT /evidence="ECO:0000269|PubMed:8900137"
FT MUTAGEN 149
FT /note="D->A: Wild-type effect concerning mgrB
FT transcription."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 150
FT /note="D->I: Wild-type effect concerning mgrB
FT transcription."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 151
FT /note="D->I: Wild-type effect concerning mgrB
FT transcription."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 152
FT /note="D->F: Wild-type effect concerning mgrB
FT transcription."
FT /evidence="ECO:0000269|PubMed:16041131"
FT MUTAGEN 179
FT /note="D->L,A: Locked-on mutant defective in Mg(2+)-sensing
FT and unable to control its phosphorylation state and
FT phosphotransfer to phoP."
FT /evidence="ECO:0000269|PubMed:16041131,
FT ECO:0000269|PubMed:18348979"
FT MUTAGEN 179
FT /note="D->R: Very large decrease in the transcriptional
FT activation of PhoQ-dependent genes."
FT /evidence="ECO:0000269|PubMed:16041131,
FT ECO:0000269|PubMed:18348979"
FT MUTAGEN 199
FT /note="L->N: Shows Mg(2+)-dependent signaling and partial
FT gene activation activity; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 202
FT /note="N->A: Is blind to signal, fails to activate
FT transcription of PhoQ-dependent genes, and abrogates
FT transcription when coexpressed with wild-type PhoQ. Shows
FT no detectable autophosphorylation. Still displays
FT phosphatase activity. Recovers Mg(2+)-dependent signaling
FT and partial gene activation activity; when associated with
FT N-27 or N-199 or N-203 or N-205. Recovers Mg(2+)-dependent
FT signaling and displays higher gene activation activity than
FT wild-type; when associated with N-30."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 202
FT /note="N->I,L,M,F,W,Y,V,C,G,P: Is blind to signal, fails to
FT activate transcription of PhoQ-dependent genes, and
FT abrogates transcription when coexpressed with wild-type
FT PhoQ."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 202
FT /note="N->R,D,Q,E,H: Shows similar activity profile to
FT wild-type."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 203
FT /note="L->N: Shows Mg(2+)-dependent signaling and partial
FT gene activation activity; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 205
FT /note="L->N: Shows Mg(2+)-dependent signaling and partial
FT gene activation activity; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:20404199"
FT MUTAGEN 392
FT /note="K->A: 44-fold decrease in ATP affinity and 6-fold
FT decrease in activity."
FT /evidence="ECO:0000269|PubMed:11493605"
FT MUTAGEN 434
FT /note="R->A: 2-fold decrease in ATP affinity and 51-fold
FT decrease in activity."
FT /evidence="ECO:0000269|PubMed:11493605"
FT MUTAGEN 439
FT /note="R->A: 3-fold decrease in ATP affinity and 2-fold
FT increase in activity."
FT /evidence="ECO:0000269|PubMed:11493605"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3BQA"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:6A8U"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:6A8U"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6A8U"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1ID0"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:1ID0"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:1ID0"
FT HELIX 376..393
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 395..404
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 409..418
FT /evidence="ECO:0007829|PDB:1ID0"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1ID0"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1ID0"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:1ID0"
FT STRAND 468..476
FT /evidence="ECO:0007829|PDB:1ID0"
SQ SEQUENCE 486 AA; 55300 MW; 89C6D97A3C9B8809 CRC64;
MKKLLRLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY
TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR DVPWLMKMIQ PDWLKSNGFH
EIEADVNDTS LLLSGDHSIQ QQLQEVREDD DDAEMTHSVA VNVYPATSRM PKLTIVVVDT
IPVELKSSYM VWSWFIYVLS ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN
PATTRELTSL VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV
SDAEPVMLEQ ISRISQQIGY YLHRASMRGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV
NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI
PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITEQYEGKI VAGESMLGGA RMEVIFGRQH
SAPKDE
