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Sensor histidine kinase CpxA (EC 2.7.13.3)

 CPXA_ECOLI              Reviewed;         457 AA.
P0AE82; P08336; Q2M8K8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Sensor histidine kinase CpxA;
EC=2.7.13.3 {ECO:0000269|PubMed:9401031};
Name=cpxA; Synonyms=ecfB, eup, ssd; OrderedLocusNames=b3911, JW3882;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
STRAIN=K12;
PubMed=3007473;
Albin R., Weber R.F., Silverman P.M.;
"The Cpx proteins of Escherichia coli K12. Immunologic detection of
the chromosomal cpxA gene product.";
J. Biol. Chem. 261:4698-4705(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3058985; DOI=10.1016/0022-2836(88)90013-7;
Weber R.F., Silverman P.M.;
"The cpx proteins of Escherichia coli K12. Structure of the cpxA
polypeptide as an inner membrane component.";
J. Mol. Biol. 203:467-478(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8346018; DOI=10.1093/nar/21.15.3391;
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the
region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
CHARACTERIZATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / AE2000;
PubMed=2185221; DOI=10.1128/jb.172.5.2456-2461.1990;
Rainwater S., Silverman P.M.;
"The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB,
ssd, and eup mutations all identify the same gene.";
J. Bacteriol. 172:2456-2461(1990).
[7]
FUNCTION.
STRAIN=K12;
PubMed=8432716; DOI=10.1128/jb.175.4.921-925.1993;
Silverman P.M., Tran L., Harris R., Gaudin H.M.;
"Accumulation of the F plasmid TraJ protein in cpx mutants of
Escherichia coli.";
J. Bacteriol. 175:921-925(1993).
[8]
FUNCTION, ENZYME REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=7883164; DOI=10.1101/gad.9.4.387;
Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.;
"The Cpx two-component signal transduction pathway of Escherichia coli
regulates transcription of the gene specifying the stress-inducible
periplasmic protease, DegP.";
Genes Dev. 9:387-398(1995).
[9]
ENZYME REGULATION.
PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
"The chaperone-assisted membrane release and folding pathway is sensed
by two signal transduction systems.";
EMBO J. 16:6394-6406(1997).
[10]
FUNCTION AS A KINASE AND PHOSPHATASE, CATALYTIC ACTIVITY, COFACTOR,
DOMAIN, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF ARG-33;
93-ARG--GLY-124 AND THR-252.
STRAIN=K12 / MC4100;
PubMed=9401031; DOI=10.1128/jb.179.24.7724-7733.1997;
Raivio T.L., Silhavy T.J.;
"Transduction of envelope stress in Escherichia coli by the Cpx two-
component system.";
J. Bacteriol. 179:7724-7733(1997).
[11]
FUNCTION, ENZYME REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=9473036;
Danese P.N., Silhavy T.J.;
"CpxP, a stress-combative member of the Cpx regulon.";
J. Bacteriol. 180:831-839(1998).
[12]
ENZYME REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=10972835; DOI=10.1046/j.1365-2958.2000.02074.x;
Raivio T.L., Laird M.W., Joly J.C., Silhavy T.J.;
"Tethering of CpxP to the inner membrane prevents spheroplast
induction of the cpx envelope stress response.";
Mol. Microbiol. 37:1186-1197(2000).
[13]
FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11830644; DOI=10.1073/pnas.042521699;
Otto K., Silhavy T.J.;
"Surface sensing and adhesion of Escherichia coli controlled by the
Cpx-signaling pathway.";
Proc. Natl. Acad. Sci. U.S.A. 99:2287-2292(2002).
[14]
SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[15]
FUNCTION, ENZYME REGULATION, AND PROBABLE SUBUNIT.
STRAIN=K12 / MC4100;
PubMed=16166523; DOI=10.1128/JB.187.19.6622-6630.2005;
Buelow D.R., Raivio T.L.;
"Cpx signal transduction is influenced by a conserved N-terminal
domain in the novel inhibitor CpxP and the periplasmic protease
DegP.";
J. Bacteriol. 187:6622-6630(2005).
[16]
FUNCTION, AND ENZYME REGULATION.
PubMed=17259177; DOI=10.1074/jbc.M605785200;
Fleischer R., Heermann R., Jung K., Hunke S.;
"Purification, reconstitution, and characterization of the CpxRAP
envelope stress system of Escherichia coli.";
J. Biol. Chem. 282:8583-8593(2007).
[17]
ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[18]
SUBUNIT.
STRAIN=K12 / MC4100;
PubMed=21317318; DOI=10.1128/JB.01296-10;
Thede G.L., Arthur D.C., Edwards R.A., Buelow D.R., Wong J.L.,
Raivio T.L., Glover J.N.;
"Structure of the periplasmic stress response protein CpxP.";
J. Bacteriol. 193:2149-2157(2011).
[19]
SUBUNIT.
PubMed=21239493; DOI=10.1074/jbc.M110.194092;
Zhou X., Keller R., Volkmer R., Krauss N., Scheerer P., Hunke S.;
"Structural basis for two-component system inhibition and pilus
sensing by the auxiliary CpxP protein.";
J. Biol. Chem. 286:9805-9814(2011).
[20]
FUNCTION, ENZYME REGULATION, INTERACTION WITH CPXP AND CPXR, AND
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=25207645; DOI=10.1371/journal.pone.0107383;
Tschauner K., Hoernschemeyer P., Mueller V.S., Hunke S.;
"Dynamic interaction between the CpxA sensor kinase and the
periplasmic accessory protein CpxP mediates signal recognition in E.
coli.";
PLoS ONE 9:E107383-E107383(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 188-457 IN COMPLEX WITH ADP;
ATP AND ATP ANALOG, FUNCTION, SUBUNIT, ACTIVE SITE, REACTION
MECHANISM, DOMAIN, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF SER-185;
LEU-186; ALA-197; ASN-204; GLY-222; MET-228 AND ASN-356.
PubMed=24492262; DOI=10.1371/journal.pbio.1001776;
Mechaly A.E., Sassoon N., Betton J.M., Alzari P.M.;
"Segmental helical motions and dynamical asymmetry modulate histidine
kinase autophosphorylation.";
PLoS Biol. 12:E1001776-E1001776(2014).
-!- FUNCTION: Histidine kinase member of the two-component regulatory
system CpxA/CpxR which responds to envelope stress response by
activating expression of downstream genes including cpxP, degP,
dsbA and ppiA (PubMed:7883164, PubMed:9401031, PubMed:9473036).
Activates CpxR by phosphorylation; has autokinase,
phosphotransferase and (in the presence of Mg(2+) and/or ATP or
ADP) phosphatase activity (PubMed:9401031, PubMed:17259177,
PubMed:24492262). The kinase activity is inhibited by periplasmic
accessory protein CpxP; proteolysis of CpxP relieves inhibition
(PubMed:16166523, PubMed:17259177, PubMed:25207645). Involved in
several diverse cellular processes, including the functioning of
acetohydroxyacid synthetase I, the biosynthesis of isoleucine and
valine, the TraJ protein activation activity for tra gene
expression in F plasmid (PubMed:8432716), and the synthesis,
translocation, or stability of cell envelope proteins
(PubMed:7883164). Activates transcription of periplasmic protease
degP, probably by phosphorylating the cognate response protein
CpxR; overexpression of an outer membrane lipoprotein NlpE also
leads to transcription of degP via CpxRA (PubMed:7883164).
Required for efficient binding of stationary phase cells to
hydrophobic surfaces, part of the process of biofilm formation
(PubMed:11830644). {ECO:0000269|PubMed:16166523,
ECO:0000269|PubMed:17259177, ECO:0000269|PubMed:24492262,
ECO:0000269|PubMed:25207645, ECO:0000269|PubMed:7883164,
ECO:0000269|PubMed:8432716, ECO:0000269|PubMed:9401031,
ECO:0000269|PubMed:9473036, ECO:0000305|PubMed:11830644}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine. {ECO:0000269|PubMed:9401031}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9401031};
Note=Phosphotransfer to CpxR is stimulated by Mg(2+) and/or
Mn(2+). {ECO:0000269|PubMed:9401031};
-!- ENZYME REGULATION: The two-component system is activated by
envelope stress such as overexpression of some (misfolded)
periplasmic proteins (PubMed:7883164, PubMed:9351822). Activated
by spheroplasting (which removes the periplasm) in an
autoregulatory cpxA-cpxR-dependent fashion (PubMed:10972835). Cpx
two-component system is induced at pH 8.0; in a degP deletion
mutant induction is halved (PubMed:9473036, PubMed:16166523). The
kinase activity is inhibited by periplasmic accessory protein
CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523,
PubMed:17259177, PubMed:25207645). Autokinase activity
reconstituted in liposomes is 50% inhibited by periplasmic
accessory protein CpxP, but CpxP has no effect on phosphatase
activity; autokinase stimulated by KCl, NH(4)Cl, RbCl, pH 7.5 and
8.0, inhibited by sensor kinase inhibitors
tetrachlorosalicylanilid and ethodin (PubMed:17259177).
{ECO:0000269|PubMed:10972835, ECO:0000269|PubMed:16166523,
ECO:0000269|PubMed:17259177, ECO:0000269|PubMed:25207645,
ECO:0000269|PubMed:7883164, ECO:0000269|PubMed:9351822,
ECO:0000269|PubMed:9473036}.
-!- SUBUNIT: The isolated cytoplasmic domain (residues 188-457)
crystallizes as a homodimer, and forms dimers of dimers in
solution which may be catalytically important (PubMed:24492262).
Interacts with periplasmic accessory protein CpxP
(PubMed:16166523, PubMed:21317318, PubMed:21239493,
PubMed:25207645); interaction with CpxP is not seen in vivo when
cells are grown in 0.3 M NaCl, or if the misfolded P pili protein
PapE is overexpressed (PubMed:25207645). Interacts with cognate
response regulator CpxR (PubMed:25207645).
{ECO:0000269|PubMed:24492262, ECO:0000269|PubMed:25207645,
ECO:0000305|PubMed:16166523}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-9141330, EBI-9141330;
P0AE88:cpxR; NbExp=3; IntAct=EBI-9141330, EBI-550918;
P76086:paaX; NbExp=3; IntAct=EBI-9141330, EBI-544692;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:25207645,
ECO:0000269|PubMed:3058985}; Multi-pass membrane protein
{ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:3058985}.
-!- DOMAIN: The periplasmic segment (residues 30-163) defines the
sensory domain (PubMed:9401031). Conformational changes in the
cytoplasmic HAMP domain modulate the mobility of the central
alpha-helices (which bend at Ser-238 and Pro-253) that allows
formation of 1 kinase-active state. {ECO:0000269|PubMed:24492262,
ECO:0000269|PubMed:9401031}.
-!- PTM: Autophosphorylated (PubMed:9401031, PubMed:24492262). Maximal
phosphorylation of the dimeric isolated cytoplasmic domain
(residues 188-457) is about 70%, suggesting the protein may be
hemiphosphorylated in vivo; probably occurs via a trans-
autophosphorylation mechanism, i.e. one subunit phopshorylates the
other (PubMed:24492262). {ECO:0000269|PubMed:24492262,
ECO:0000269|PubMed:9401031}.
-!- DISRUPTION PHENOTYPE: Loss of the Cpx envelope stress response
(PubMed:10972835). Decreased resistance to the antibiotic
amnikacin (PubMed:2185221). Single cpxA and double cpxR-cpxA
mutant decrease transcription of degP (PubMed:7883164). Decreased
transcription of cpxP (PubMed:9473036). Hypersensitive to alkaline
pH (greater than pH 8.8) (PubMed:9473036). Decreased numbers of
stationary phase cells bind to hydrophobic surfaces
(PubMed:11830644). Greatly increased resistance to hydroxyurea,
probably due to decreased recognition of mis-folded proteins which
eventually leads to decreased OH radical formation
(PubMed:20005847). {ECO:0000269|PubMed:10972835,
ECO:0000269|PubMed:11830644, ECO:0000269|PubMed:20005847,
ECO:0000269|PubMed:2185221, ECO:0000269|PubMed:7883164,
ECO:0000269|PubMed:9473036}.
-!- SEQUENCE CAUTION:
Sequence=AAA72540.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M13493; AAA72540.1; ALT_INIT; Genomic_DNA.
EMBL; M36795; AAA23600.1; -; Genomic_DNA.
EMBL; X13307; CAA31687.1; -; Genomic_DNA.
EMBL; L19201; AAB03044.1; -; Genomic_DNA.
EMBL; U00096; AAC76893.1; -; Genomic_DNA.
EMBL; AP009048; BAE77398.1; -; Genomic_DNA.
PIR; S40855; S40855.
RefSeq; NP_418347.1; NC_000913.3.
RefSeq; WP_000580417.1; NZ_LN832404.1.
PDB; 4BIU; X-ray; 3.65 A; A/B/C/D/E/F=188-457.
PDB; 4BIV; X-ray; 3.40 A; A/B=188-457.
PDB; 4BIW; X-ray; 2.85 A; A/B=188-457.
PDB; 4BIX; X-ray; 2.00 A; A/B=188-457.
PDB; 4BIY; X-ray; 3.30 A; A/B/C/D=188-457.
PDB; 4BIZ; X-ray; 2.65 A; A/B/C/D/E/F=188-457.
PDB; 4CB0; X-ray; 3.30 A; A/B=188-457.
PDB; 5LFK; X-ray; 3.09 A; A/B=188-457.
PDBsum; 4BIU; -.
PDBsum; 4BIV; -.
PDBsum; 4BIW; -.
PDBsum; 4BIX; -.
PDBsum; 4BIY; -.
PDBsum; 4BIZ; -.
PDBsum; 4CB0; -.
PDBsum; 5LFK; -.
ProteinModelPortal; P0AE82; -.
SMR; P0AE82; -.
BioGrid; 4262644; 12.
DIP; DIP-48358N; -.
IntAct; P0AE82; 2.
STRING; 316385.ECDH10B_4101; -.
iPTMnet; P0AE82; -.
PaxDb; P0AE82; -.
PRIDE; P0AE82; -.
EnsemblBacteria; AAC76893; AAC76893; b3911.
EnsemblBacteria; BAE77398; BAE77398; BAE77398.
GeneID; 948405; -.
KEGG; ecj:JW3882; -.
KEGG; eco:b3911; -.
PATRIC; fig|1411691.4.peg.2793; -.
EchoBASE; EB0161; -.
EcoGene; EG10163; cpxA.
eggNOG; ENOG4105E0F; Bacteria.
eggNOG; ENOG410XTWD; LUCA.
HOGENOM; HOG000269851; -.
InParanoid; P0AE82; -.
KO; K07640; -.
PhylomeDB; P0AE82; -.
BioCyc; EcoCyc:CPXA-MONOMER; -.
PRO; PR:P0AE82; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
GO; GO:0043708; P:cell adhesion involved in biofilm formation; IMP:CACAO.
GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
CDD; cd06225; HAMP; 1.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR032404; CpxA_peri.
InterPro; IPR003660; HAMP_dom.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
Pfam; PF16527; CpxA_peri; 1.
Pfam; PF00672; HAMP; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00512; HisKA; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00304; HAMP; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS50885; HAMP; 1.
PROSITE; PS50109; HIS_KIN; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell adhesion; Cell inner membrane;
Cell membrane; Complete proteome; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
Transmembrane; Transmembrane helix; Two-component regulatory system.
CHAIN 1 457 Sensor histidine kinase CpxA.
/FTId=PRO_0000074739.
TOPO_DOM 1 7 Cytoplasmic.
{ECO:0000305|PubMed:15919996}.
TRANSMEM 8 29 Helical. {ECO:0000305}.
TOPO_DOM 30 163 Periplasmic.
{ECO:0000305|PubMed:15919996,
ECO:0000305|PubMed:3058985}.
TRANSMEM 164 184 Helical. {ECO:0000305}.
TOPO_DOM 185 457 Cytoplasmic.
{ECO:0000305|PubMed:15919996,
ECO:0000305|PubMed:3058985}.
DOMAIN 185 237 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 245 455 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
NP_BIND 248 251 ATP. {ECO:0000269|PubMed:24492262}.
NP_BIND 359 364 ATP. {ECO:0000269|PubMed:24492262}.
NP_BIND 405 406 ATP. {ECO:0000269|PubMed:24492262}.
NP_BIND 416 421 ATP. {ECO:0000269|PubMed:24492262}.
ACT_SITE 248 248 Nucleophile.
{ECO:0000269|PubMed:24492262}.
BINDING 248 248 ATP. {ECO:0000269|PubMed:24492262}.
BINDING 386 386 ATP. {ECO:0000269|PubMed:24492262}.
MOD_RES 248 248 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107,
ECO:0000305|PubMed:24492262,
ECO:0000305|PubMed:9401031}.
MUTAGEN 33 33 R->C: In cpxA104; a cpxA gain of function
mutant, constitutively active.
{ECO:0000269|PubMed:9401031}.
MUTAGEN 93 124 Missing: In cpxA24; a cpxA gain of
function mutant, constitutively active,
up-regulation of the Cpx regulon members.
{ECO:0000269|PubMed:9401031}.
MUTAGEN 185 185 S->R: Nearly complete loss of response to
excess periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 186 186 L->Q: 30% decrease in response to excess
periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 197 197 A->V: Slight decrease in response to
excess periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 204 204 N->Y: 80% decrease in response to excess
periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 222 222 G->D: 90% decrease in response to excess
periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 222 222 G->R: 75% decrease in response to excess
periplasmic protein.
{ECO:0000269|PubMed:24492262}.
MUTAGEN 228 228 M->V: No response to excess periplasmic
protein, decreased autophosphorylation,
no phosphotransfer to CpxR, no tetramer
formation of the C-terminal domain in
solution. {ECO:0000269|PubMed:24492262}.
MUTAGEN 252 252 T->P: In cpxA101; a cpxA gain of function
mutant, decreased autophosphorylation,
decreased phosphotransfer to CpxR, loss
of phosphatase activity, responds to
periplasmic protein overproduction.
{ECO:0000269|PubMed:9401031}.
MUTAGEN 356 356 N->Y: Nearly complete loss of response to
excess periplasmic protein.
{ECO:0000269|PubMed:24492262}.
CONFLICT 68 68 W -> WW (in Ref. 1; AAA23600 and 2;
CAA31687). {ECO:0000305}.
CONFLICT 330 330 K -> R (in Ref. 1; AAA23600/AAA72540 and
2; CAA31687). {ECO:0000305}.
HELIX 189 200 {ECO:0000244|PDB:4BIV}.
TURN 201 203 {ECO:0000244|PDB:4BIV}.
HELIX 209 212 {ECO:0000244|PDB:4BIV}.
STRAND 214 216 {ECO:0000244|PDB:4BIV}.
HELIX 217 220 {ECO:0000244|PDB:4BIW}.
HELIX 221 249 {ECO:0000244|PDB:4BIX}.
HELIX 251 267 {ECO:0000244|PDB:4BIX}.
HELIX 272 296 {ECO:0000244|PDB:4BIX}.
STRAND 299 301 {ECO:0000244|PDB:4BIW}.
STRAND 306 309 {ECO:0000244|PDB:4BIX}.
HELIX 310 328 {ECO:0000244|PDB:4BIX}.
STRAND 331 336 {ECO:0000244|PDB:4BIX}.
STRAND 342 345 {ECO:0000244|PDB:4BIX}.
HELIX 347 364 {ECO:0000244|PDB:4BIX}.
STRAND 366 375 {ECO:0000244|PDB:4BIX}.
STRAND 377 386 {ECO:0000244|PDB:4BIX}.
HELIX 393 395 {ECO:0000244|PDB:4BIX}.
HELIX 398 400 {ECO:0000244|PDB:4BIX}.
HELIX 407 412 {ECO:0000244|PDB:4BIZ}.
HELIX 421 430 {ECO:0000244|PDB:4BIX}.
STRAND 434 439 {ECO:0000244|PDB:4BIX}.
STRAND 443 452 {ECO:0000244|PDB:4BIX}.
SEQUENCE 457 AA; 51624 MW; 720EE4A62885BA33 CRC64;
MIGSLTARIF AIFWLTLALV LMLVLMLPKL DSRQMTELLD SEQRQGLMIE QHVEAELAND
PPNDLMWWRR LFRAIDKWAP PGQRLLLVTT EGRVIGAERS EMQIIRNFIG QADNADHPQK
KKYGRVELVG PFSVRDGEDN YQLYLIRPAS SSQSDFINLL FDRPLLLLIV TMLVSTPLLL
WLAWSLAKPA RKLKNAADEV AQGNLRQHPE LEAGPQEFLA AGASFNQMVT ALERMMTSQQ
RLLSDISHEL RTPLTRLQLG TALLRRRSGE SKELERIETE AQRLDSMIND LLVMSRNQQK
NALVSETIKA NQLWSEVLDN AAFEAEQMGK SLTVNFPPGP WPLYGNPNAL ESALENIVRN
ALRYSHTKIE VGFAVDKDGI TITVDDDGPG VSPEDREQIF RPFYRTDEAR DRESGGTGLG
LAIVETAIQQ HRGWVKAEDS PLGGLRLVIW LPLYKRS


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