ENVZ_ECOLI
ID ENVZ_ECOLI Reviewed; 450 AA.
AC P0AEJ4; P02933; Q2M769;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sensor histidine kinase EnvZ {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:2668953};
DE AltName: Full=Osmolarity sensor protein EnvZ {ECO:0000305};
GN Name=envZ; Synonyms=ompB, perA, tpo; OrderedLocusNames=b3404, JW3367;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RX PubMed=6292200; DOI=10.1016/s0021-9258(18)33502-6;
RA Mizuno T., Wurtzel E.T., Inouye M.;
RT "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of
RT the ompB operon of Escherichia coli and characterization of its gene
RT product.";
RL J. Biol. Chem. 257:13692-13698(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, AND SEQUENCE REVISION
RP TO N-TERMINUS.
RC STRAIN=K12;
RX PubMed=2997120; DOI=10.1128/jb.164.2.578-584.1985;
RA Comeau D.E., Ikenaka K., Tsung K., Inouye M.;
RT "Primary characterization of the protein products of the Escherichia coli
RT ompB locus: structure and regulation of synthesis of the OmpR and EnvZ
RT proteins.";
RL J. Bacteriol. 164:578-584(1985).
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 FUNCTION, AND MUTAGENESIS OF THR-247.
RX PubMed=3536870; DOI=10.1128/jb.168.3.1309-1314.1986;
RA Matsuyama S., Mizuno T., Mizushima S.;
RT "Interaction between two regulatory proteins in osmoregulatory expression
RT of ompF and ompC genes in Escherichia coli: a novel ompR mutation
RT suppresses pleiotropic defects caused by an envZ mutation.";
RL J. Bacteriol. 168:1309-1314(1986).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=2824492; DOI=10.1016/s0021-9258(18)49274-5;
RA Forst S., Comeau D., Norioka S., Inouye M.;
RT "Localization and membrane topology of EnvZ, a protein involved in
RT osmoregulation of OmpF and OmpC in Escherichia coli.";
RL J. Biol. Chem. 262:16433-16438(1987).
RN [7]
RP PHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--ALA-38.
RX PubMed=3056929; DOI=10.1128/jb.170.12.5971-5973.1988;
RA Igo M.M., Silhavy T.J.;
RT "EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is
RT phosphorylated in vitro.";
RL J. Bacteriol. 170:5971-5973(1988).
RN [8]
RP FUNCTION IN PHOSPHORYLATING OMPR, CATALYTIC ACTIVITY, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=2656684; DOI=10.1016/s0021-9258(18)81828-2;
RA Aiba H., Mizuno T., Mizushima S.;
RT "Transfer of phosphoryl group between two regulatory proteins involved in
RT osmoregulatory expression of the ompF and ompC genes in Escherichia coli.";
RL J. Biol. Chem. 264:8563-8567(1989).
RN [9]
RP FUNCTION IN PHOSPHORYLATING AND DEPHOSPHORYLATING OMPR, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF THR-247.
RX PubMed=2668281; DOI=10.1016/s0021-9258(18)71647-5;
RA Aiba H., Nakasai F., Mizushima S., Mizuno T.;
RT "Evidence for the physiological importance of the phosphotransfer between
RT the two regulatory components, EnvZ and OmpR, in osmoregulation in
RT Escherichia coli.";
RL J. Biol. Chem. 264:14090-14094(1989).
RN [10]
RP FUNCTION IN PHOSPHORYLATING OMPR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
RP AND MUTAGENESIS OF HIS-243.
RX PubMed=2668953; DOI=10.1073/pnas.86.16.6052;
RA Forst S., Delgado J., Inouye M.;
RT "Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the
RT ompF and ompC genes in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6052-6056(1989).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND PHOSPHORYLATION.
RX PubMed=2674113; DOI=10.1093/oxfordjournals.jbchem.a122817;
RA Aiba H., Nakasai F., Mizushima S., Mizuno T.;
RT "Phosphorylation of a bacterial activator protein, OmpR, by a protein
RT kinase, EnvZ, results in stimulation of its DNA-binding ability.";
RL J. Biochem. 106:5-7(1989).
RN [12]
RP FUNCTION IN PHOSPHORYLATING AND DEPHOSPHORYLATING OMPR, CROSSTALK BETWEEN
RP TWO-COMPONENT SYSTEMS, AND MUTAGENESIS OF 1-MET--ALA-38.
RX PubMed=2558046; DOI=10.1101/gad.3.11.1725;
RA Igo M.M., Ninfa A.J., Stock J.B., Silhavy T.J.;
RT "Phosphorylation and dephosphorylation of a bacterial transcriptional
RT activator by a transmembrane receptor.";
RL Genes Dev. 3:1725-1734(1989).
RN [13]
RP FUNCTION IN PHOSPHORYLATING AND DEPHOSPHORYLATING OMPR,
RP AUTOPHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-243.
RX PubMed=2277041; DOI=10.1093/oxfordjournals.jbchem.a123225;
RA Kanamaru K., Aiba H., Mizuno T.;
RT "Transmembrane signal transduction and osmoregulation in Escherichia coli:
RT I. Analysis by site-directed mutagenesis of the amino acid residues
RT involved in phosphotransfer between the two regulatory components, EnvZ and
RT OmpR.";
RL J. Biochem. 108:483-487(1990).
RN [14]
RP FUNCTION IN PHOSPHORYLATING AND DEPHOSPHORYLATING OMPR, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LEU-18; PRO-41; ARG-180; PRO-185 AND THR-247.
RX PubMed=1323560; DOI=10.1093/oxfordjournals.jbchem.a123823;
RA Tokishita S., Kojima A., Mizuno T.;
RT "Transmembrane signal transduction and osmoregulation in Escherichia coli:
RT functional importance of the transmembrane regions of membrane-located
RT protein kinase, EnvZ.";
RL J. Biochem. 111:707-713(1992).
RN [15]
RP PHOSPHORYLATION AT HIS-243.
RX PubMed=8132603; DOI=10.1016/s0021-9258(17)37029-1;
RA Roberts D.L., Bennett D.W., Forst S.A.;
RT "Identification of the site of phosphorylation on the osmosensor, EnvZ, of
RT Escherichia coli.";
RL J. Biol. Chem. 269:8728-8733(1994).
RN [16]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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 [17]
RP SUBUNIT.
RX PubMed=15357641; DOI=10.1042/bj20041125;
RA Khorchid A., Inouye M., Ikura M.;
RT "Structural characterization of Escherichia coli sensor histidine kinase
RT EnvZ: the periplasmic C-terminal core domain is critical for
RT homodimerization.";
RL Biochem. J. 385:255-264(2005).
RN [18]
RP DOMAIN, AND MUTAGENESIS OF ALA-193.
RX PubMed=17635923; DOI=10.1074/jbc.m701342200;
RA Kishii R., Falzon L., Yoshida T., Kobayashi H., Inouye M.;
RT "Structural and functional studies of the HAMP domain of EnvZ, an
RT osmosensing transmembrane histidine kinase in Escherichia coli.";
RL J. Biol. Chem. 282:26401-26408(2007).
RN [19]
RP INTERACTION WITH MZRA, AND ACTIVITY REGULATION.
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 [20]
RP INTERACTION WITH MZRA, AND ACTIVITY REGULATION.
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 [21]
RP MECHANISM, DOMAIN, AND AUTOPHOSPHORYLATION.
RX PubMed=22543870; DOI=10.1038/emboj.2012.99;
RA Wang L.C., Morgan L.K., Godakumbura P., Kenney L.J., Anand G.S.;
RT "The inner membrane histidine kinase EnvZ senses osmolality via helix-coil
RT transitions in the cytoplasm.";
RL EMBO J. 31:2648-2659(2012).
RN [22]
RP ERRATUM OF PUBMED:22543870.
RX PubMed=26427760; DOI=10.15252/embj.201592753;
RA Wang L.C., Morgan L.K., Godakumbura P., Kenney L.J., Anand G.S.;
RT "The inner membrane histidine kinase EnvZ senses osmolality via helix-coil
RT transitions in the cytoplasm.";
RL EMBO J. 34:2481-2481(2015).
RN [23]
RP MECHANISM, AND SUBUNIT.
RX PubMed=28256224; DOI=10.1016/j.bpj.2016.12.027;
RA Ghosh M., Wang L.C., Ramesh R., Morgan L.K., Kenney L.J., Anand G.S.;
RT "Lipid-mediated regulation of embedded receptor kinases via parallel
RT allosteric relays.";
RL Biophys. J. 112:643-654(2017).
RN [24]
RP FUNCTION IN ACID STRESS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=29138484; DOI=10.1038/s41467-017-02030-0;
RA Chakraborty S., Winardhi R.S., Morgan L.K., Yan J., Kenney L.J.;
RT "Non-canonical activation of OmpR drives acid and osmotic stress responses
RT in single bacterial cells.";
RL Nat. Commun. 8:1587-1587(2017).
RN [25]
RP INTERACTION WITH MZRA, SUBUNIT, AND MUTAGENESIS OF 73-PRO-PRO-74 AND
RP 202-PRO--PRO-204.
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).
RN [26] {ECO:0007744|PDB:1BXD}
RP STRUCTURE BY NMR OF 290-450 IN COMPLEX WITH ATP ANALOG, MUTAGENESIS OF
RP ASN-347, AND AUTOPHOSPHORYLATION.
RX PubMed=9817206; DOI=10.1038/23968;
RA Tanaka T., Saha S.K., Tomomori C., Ishima R., Liu D., Tong K.I., Park H.,
RA Dutta R., Qin L., Swindells M.B., Yamazaki T., Ono A.M., Kainosho M.,
RA Inouye M., Ikura M.;
RT "NMR structure of the histidine kinase domain of the E. coli osmosensor
RT EnvZ.";
RL Nature 396:88-92(1998).
RN [27] {ECO:0007744|PDB:1JOY}
RP STRUCTURE BY NMR OF 223-289, AND SUBUNIT.
RX PubMed=10426948; DOI=10.1038/11495;
RA Tomomori C., Tanaka T., Dutta R., Park H., Saha S.K., Zhu Y., Ishima R.,
RA Liu D., Tong K.I., Kurokawa H., Qian H., Inouye M., Ikura M.;
RT "Solution structure of the homodimeric core domain of Escherichia coli
RT histidine kinase EnvZ.";
RL Nat. Struct. Biol. 6:729-734(1999).
RN [28]
RP 3D-STRUCTURE MODELING OF 223-450, AND TOPOLOGY.
RX PubMed=12691749; DOI=10.1016/s0022-2836(03)00275-4;
RA Cai S./J., Khorchid A., Ikura M., Inouye M.;
RT "Probing catalytically essential domain orientation in histidine kinase
RT EnvZ by targeted disulfide crosslinking.";
RL J. Mol. Biol. 328:409-418(2003).
RN [29] {ECO:0007744|PDB:5XGA}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 36-158 IN THE PRESENCE OF
RP DETERGENT, ACTIVITY REGULATION, AND DOMAIN.
RC STRAIN=K12 / MC4100;
RX PubMed=28423182; DOI=10.1002/1873-3468.12658;
RA Hwang E., Cheong H.K., Kim S.Y., Kwon O., Blain K.Y., Choe S., Yeo K.J.,
RA Jung Y.W., Jeon Y.H., Cheong C.;
RT "Crystal structure of the EnvZ periplasmic domain with CHAPS.";
RL FEBS Lett. 591:1419-1428(2017).
RN [30] {ECO:0007744|PDB:5B1N, ECO:0007744|PDB:5B1O}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 223-289, X-RAY CRYSTALLOGRAPHY
RP (2.30 ANGSTROMS) OF MUTATED 223-289, ACTIVITY REGULATION, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF ARG-234; SER-242; ASP-244; THR-247 AND PRO-248.
RX PubMed=27999439; DOI=10.1038/ja.2016.151;
RA Eguchi Y., Okajima T., Tochio N., Inukai Y., Shimizu R., Ueda S.,
RA Shinya S., Kigawa T., Fukamizo T., Igarashi M., Utsumi R.;
RT "Angucycline antibiotic waldiomycin recognizes common structural motif
RT conserved in bacterial histidine kinases.";
RL J. Antibiot. 70:251-258(2017).
CC -!- FUNCTION: Member of the two-component regulatory system EnvZ/OmpR
CC involved in osmoregulation (particularly of genes ompF and ompC) as
CC well as other genes (PubMed:2997120, PubMed:3536870). EnvZ functions as
CC a membrane-associated protein kinase that phosphorylates OmpR in
CC response to environmental signals; at low osmolarity OmpR activates
CC ompF transcription, while at high osmolarity it represses ompF and
CC activates ompC transcription (PubMed:2656684, PubMed:2668281,
CC PubMed:2668953, PubMed:2674113, PubMed:2558046, PubMed:2277041,
CC PubMed:1323560). Also dephosphorylates OmpR in the presence of ATP
CC (PubMed:2668281, PubMed:2558046, PubMed:2277041, PubMed:1323560). The
CC cytoplasmic dimerization domain (CDD) forms an osmosensitive core;
CC increasing osmolarity stabilizes this segment (possibly by its
CC contraction), enhancing the autophosphorylation rate and consequently,
CC downstream phosphotransfer to OmpR and signaling (PubMed:22543870,
CC PubMed:28256224). Autophosphorylation is greater when full-length EnvZ
CC is reconstituted in a lipid environment, lipid-mediated allostery
CC impacts the kinase function of EnvZ (PubMed:28256224). Involved in acid
CC stress response; this requires EnvZ but not OmpR phosphorylation, and
CC suggests that EnvZ senses cytoplasmic acidic pH (PubMed:29138484).
CC {ECO:0000269|PubMed:1323560, ECO:0000269|PubMed:22543870,
CC ECO:0000269|PubMed:2277041, ECO:0000269|PubMed:2558046,
CC ECO:0000269|PubMed:2656684, ECO:0000269|PubMed:2668281,
CC ECO:0000269|PubMed:2668953, ECO:0000269|PubMed:2674113,
CC ECO:0000269|PubMed:28256224, ECO:0000269|PubMed:29138484,
CC ECO:0000269|PubMed:2997120, ECO:0000269|PubMed:3536870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:2668953,
CC ECO:0000305|PubMed:2656684, ECO:0000305|PubMed:2668281,
CC ECO:0000305|PubMed:2674113};
CC -!- ACTIVITY REGULATION: Activity is modulated by MzrA (PubMed:19432797,
CC PubMed:20889743). In the presence of 0.2 M NaCl, 2.0 mM sodium cholate
CC (bile salts) decreases expression from the ompC promoter; how this is
CC mediated is unknown (PubMed:28423182). Autophosphorylation is inhibited
CC by the angucycline antibiotic waldiomycin in a non-competitive manner;
CC waldiomycin prevents dimerization of the cytoplasmic domain and
CC autophosphorylation (PubMed:27999439). {ECO:0000269|PubMed:19432797,
CC ECO:0000269|PubMed:20889743, ECO:0000269|PubMed:27999439,
CC ECO:0000269|PubMed:28423182}.
CC -!- SUBUNIT: Homodimer (PubMed:10426948, PubMed:15357641, PubMed:9817206,
CC PubMed:28256224, PubMed:29953503, PubMed:27999439). Interacts with MzrA
CC (PubMed:19432797, PubMed:20889743, PubMed:29953503).
CC {ECO:0000269|PubMed:10426948, ECO:0000269|PubMed:15357641,
CC ECO:0000269|PubMed:19432797, ECO:0000269|PubMed:20889743,
CC ECO:0000269|PubMed:27999439, ECO:0000269|PubMed:28256224,
CC ECO:0000269|PubMed:29953503, ECO:0000269|PubMed:9817206}.
CC -!- INTERACTION:
CC P0AEJ4; P0AEJ4: envZ; NbExp=2; IntAct=EBI-1121750, EBI-1121750;
CC P0AEJ4; P42615: mzrA; NbExp=3; IntAct=EBI-1121750, EBI-6412632;
CC P0AEJ4; P0AA16: ompR; NbExp=2; IntAct=EBI-1121750, EBI-369514;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1323560,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2824492}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:1323560,
CC ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:2824492}.
CC -!- INDUCTION: Part of the ompR-envZ operon. {ECO:0000305|PubMed:2997120,
CC ECO:0000305|PubMed:6292200}.
CC -!- DOMAIN: The periplasmic domain interacts with MzrA (PubMed:20889743)
CC (Probable). The periplasmic domain assumes a PDC sensor fold
CC (PubMed:28423182). The HAMP domain by itself is intrinsically
CC disordered (PubMed:17635923). The cytoplasmic dimerization domain (CDD,
CC residues 223-289) forms an osmosensitive core; increasing osmolarity
CC stabilizes this segment, enhancing its autophosphorylation rate and
CC consequently, downstream phosphotransfer to OmpR and signaling
CC (PubMed:17635923, PubMed:28256224). The autophosphorylation activity of
CC the CDD is inhibited by the angucycline antibiotic waldiomycin which
CC probably binds to it (PubMed:27999439). The soluble EnvZ C-terminal
CC fragment (residues 180-450) is capable of conferring osmolarity-
CC sensitive expression of OmpC in the absence of the membrane anchor
CC (PubMed:17635923). {ECO:0000269|PubMed:17635923,
CC ECO:0000269|PubMed:20889743, ECO:0000269|PubMed:27999439,
CC ECO:0000269|PubMed:28256224, ECO:0000269|PubMed:28423182,
CC ECO:0000305|PubMed:19432797}.
CC -!- PTM: Autophosphorylated (PubMed:3056929, PubMed:2656684,
CC PubMed:2668281, PubMed:2668953, PubMed:8132603, PubMed:2277041).
CC Incubation of isolated EnvZ C-terminal fragment (residues 180-450) with
CC increasing levels of NaCl or sucrose increases its autophosphorylation
CC (PubMed:17635923). {ECO:0000269|PubMed:17635923,
CC ECO:0000269|PubMed:2277041, ECO:0000269|PubMed:2656684,
CC ECO:0000269|PubMed:2668281, ECO:0000269|PubMed:2668953,
CC ECO:0000269|PubMed:8132603, ECO:0000303|PubMed:3056929}.
CC -!- DISRUPTION PHENOTYPE: No expression of OmpC or OmpF during growth at 0%
CC sucrose, low expression of OmpF at 15% sucrose (PubMed:3056929). Single
CC deletion of envZ has no OmpC or OmpF at 0% sucrose, low levels of OmpC
CC and very low levels of OmpF at 15% sucrose. Deletion of both ompR and
CC envZ leads to loss of both OmpC and OmpF expression at 0% and 15%
CC sucrose (PubMed:2277041). {ECO:0000269|PubMed:2277041,
CC ECO:0000269|PubMed:3056929}.
CC -!- MISCELLANEOUS: Cross talk between this and the Che and Ntr two-
CC component systems can occur at least in vitro.
CC {ECO:0000269|PubMed:2558046}.
CC -!- MISCELLANEOUS: Two or more proline residues often cause ribosome
CC stalling and decreased protein translation; the cytoplasmic strong stop
CC motif IPPPL does not have this effect and instead is involved in
CC homodimerization, while the weaker periplasmic stop motif VVPPA motif
CC is involved in MzrA interaction. {ECO:0000269|PubMed:29953503}.
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DR EMBL; J01656; AAA16242.1; -; Unassigned_RNA.
DR EMBL; U18997; AAA58201.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76429.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77887.1; -; Genomic_DNA.
DR PIR; B25024; MMECZB.
DR RefSeq; NP_417863.1; NC_000913.3.
DR RefSeq; WP_001253696.1; NZ_STEB01000004.1.
DR PDB; 1BXD; NMR; -; A=290-450.
DR PDB; 1JOY; NMR; -; A/B=223-289.
DR PDB; 3ZCC; X-ray; 1.25 A; A/B=229-288.
DR PDB; 3ZRV; X-ray; 1.65 A; A/B=229-290.
DR PDB; 3ZRW; X-ray; 2.25 A; A/C/D=229-289, B=231-289.
DR PDB; 3ZRX; X-ray; 1.25 A; A/B=229-289.
DR PDB; 4CTI; X-ray; 2.85 A; A/B/C/D=228-450.
DR PDB; 4KP4; X-ray; 3.00 A; A/B=223-253, A/B=266-450.
DR PDB; 5B1N; X-ray; 1.33 A; A=223-289.
DR PDB; 5B1O; X-ray; 2.30 A; A/B=223-289.
DR PDB; 5XGA; X-ray; 1.95 A; A=36-158.
DR PDBsum; 1BXD; -.
DR PDBsum; 1JOY; -.
DR PDBsum; 3ZCC; -.
DR PDBsum; 3ZRV; -.
DR PDBsum; 3ZRW; -.
DR PDBsum; 3ZRX; -.
DR PDBsum; 4CTI; -.
DR PDBsum; 4KP4; -.
DR PDBsum; 5B1N; -.
DR PDBsum; 5B1O; -.
DR PDBsum; 5XGA; -.
DR AlphaFoldDB; P0AEJ4; -.
DR SMR; P0AEJ4; -.
DR BioGRID; 4261266; 47.
DR DIP; DIP-48357N; -.
DR IntAct; P0AEJ4; 5.
DR MINT; P0AEJ4; -.
DR STRING; 511145.b3404; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR iPTMnet; P0AEJ4; -.
DR jPOST; P0AEJ4; -.
DR PaxDb; P0AEJ4; -.
DR PRIDE; P0AEJ4; -.
DR EnsemblBacteria; AAC76429; AAC76429; b3404.
DR EnsemblBacteria; BAE77887; BAE77887; BAE77887.
DR GeneID; 66672714; -.
DR GeneID; 947272; -.
DR KEGG; ecj:JW3367; -.
DR KEGG; eco:b3404; -.
DR PATRIC; fig|1411691.4.peg.3325; -.
DR EchoBASE; EB0265; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_27_6; -.
DR InParanoid; P0AEJ4; -.
DR OMA; WIRPPQA; -.
DR PhylomeDB; P0AEJ4; -.
DR BioCyc; EcoCyc:ENVZ-MON; -.
DR BioCyc; MetaCyc:ENVZ-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P0AEJ4; -.
DR PRO; PR:P0AEJ4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; 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:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoliWiki.
DR GO; GO:0016310; P:phosphorylation; IDA:EcoliWiki.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoliWiki.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:EcoliWiki.
DR GO; GO:0006970; P:response to osmotic stress; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..450
FT /note="Sensor histidine kinase EnvZ"
FT /id="PRO_0000074759"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2824492"
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:2824492"
FT TOPO_DOM 36..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2824492"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:2824492"
FT TOPO_DOM 180..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996,
FT ECO:0000305|PubMed:17635923, ECO:0000305|PubMed:2824492"
FT DOMAIN 180..232
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 240..440
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 223..289
FT /note="Cytoplasmic dimerization domain (CDD), when
FT dimerized forms osmosensitive core"
FT /evidence="ECO:0000269|PubMed:17635923"
FT MOTIF 71..75
FT /note="polyP-periplasmic motif"
FT /evidence="ECO:0000303|PubMed:29953503"
FT MOTIF 201..205
FT /note="polyP-cytoplasmic motif"
FT /evidence="ECO:0000303|PubMed:29953503"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4KP4"
FT BINDING 347..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4KP4"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4KP4"
FT BINDING 392..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4KP4"
FT BINDING 402..406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4KP4"
FT MOD_RES 243
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:8132603"
FT MUTAGEN 1..38
FT /note="MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFA->MTMITDSL: In
FT envZ115; low constitutive expression of OmpC or OmpF at low
FT and high osmolarity. Phosphorylates and dephosphorylates
FT OmpR."
FT /evidence="ECO:0000269|PubMed:2558046,
FT ECO:0000269|PubMed:3056929"
FT MUTAGEN 18
FT /note="L->F: No OmpC, constitutive OmpF, with or without
FT sucrose. No change in phosphorylation or dephosphorylation
FT of OmpR."
FT /evidence="ECO:0000269|PubMed:1323560"
FT MUTAGEN 41
FT /note="P->L,S: Constitutive OmpC, no OmpF, with or without
FT sucrose. Phosphorylates but does not dephosphorylate OmpR."
FT /evidence="ECO:0000269|PubMed:1323560"
FT MUTAGEN 73..74
FT /note="PP->AA: Decreased interaction with MzrA."
FT /evidence="ECO:0000269|PubMed:29953503"
FT MUTAGEN 180
FT /note="R->C: No OmpC, constitutive OmpF, with or without
FT sucrose. Weakly phosphorylates OmpR, dephosphorylates
FT normally."
FT /evidence="ECO:0000269|PubMed:1323560"
FT MUTAGEN 185
FT /note="P->L: Constitutive OmpC, no OmpF, with or without
FT sucrose. Weakly phosphorylates but does not dephosphorylate
FT OmpR."
FT /evidence="ECO:0000269|PubMed:1323560"
FT MUTAGEN 193
FT /note="A->L: Promotes the formation of alpha-helical
FT secondary structure of the HAMP domain."
FT /evidence="ECO:0000269|PubMed:17635923"
FT MUTAGEN 193
FT /note="A->V: No effect."
FT /evidence="ECO:0000269|PubMed:17635923"
FT MUTAGEN 202..204
FT /note="PPP->AAA: Decreased protein homodimerization,
FT constitutive OmpC, little to no OmpF with or without salt,
FT no interaction with MzrA."
FT /evidence="ECO:0000269|PubMed:29953503"
FT MUTAGEN 234
FT /note="R->A: Autophosphorylation by cytoplasmic
FT dimerization domain (CDD) is resistant to waldiomycin."
FT /evidence="ECO:0000269|PubMed:27999439"
FT MUTAGEN 242
FT /note="S->A: Autophosphorylation by CDD is resistant to
FT waldiomycin, CDD peptide probably no longer binds
FT waldiomycin."
FT /evidence="ECO:0000269|PubMed:27999439"
FT MUTAGEN 243
FT /note="H->R: Does not autophosphorylate, does not
FT dephosphorylate OmpR in vitro, no OmpC or OmpF at 0%
FT sucrose, low levels of OmpC and very low levels of OmpF at
FT 15% sucrose."
FT /evidence="ECO:0000269|PubMed:2277041"
FT MUTAGEN 243
FT /note="H->V: Does not autophosphorylate, does not transfer
FT phosphate to OmpR, increased expression of ompC, decreased
FT expression of OmpF."
FT /evidence="ECO:0000269|PubMed:2668953"
FT MUTAGEN 244
FT /note="D->A: Autophosphorylation by CDD is resistant to
FT waldiomycin, CDD peptide probably no longer binds
FT waldiomycin."
FT /evidence="ECO:0000269|PubMed:27999439"
FT MUTAGEN 247
FT /note="T->A: Autophosphorylation by CDD is somewhat
FT resistant to waldiomycin."
FT /evidence="ECO:0000269|PubMed:27999439"
FT MUTAGEN 247
FT /note="T->R: In envZ11/MH1461; OmpF- OmpC constitutive.
FT Also prevents expression of PhoA and LamB. Phosphorylates
FT OmpR but does not dephosphorylate it."
FT /evidence="ECO:0000269|PubMed:1323560,
FT ECO:0000269|PubMed:2668281, ECO:0000269|PubMed:3536870"
FT MUTAGEN 248
FT /note="P->A: Autophosphorylation by CDD is resistant to
FT waldiomycin, CDD peptide probably no longer binds
FT waldiomycin, alters structure."
FT /evidence="ECO:0000269|PubMed:27999439"
FT MUTAGEN 347
FT /note="N->D: Loss of ATP binding; loss of
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9817206"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5XGA"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5XGA"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:5XGA"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5XGA"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5XGA"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5XGA"
FT HELIX 229..257
FT /evidence="ECO:0007829|PDB:3ZCC"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3ZCC"
FT HELIX 264..287
FT /evidence="ECO:0007829|PDB:3ZCC"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4CTI"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1BXD"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:4KP4"
FT HELIX 334..350
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4KP4"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4CTI"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:4KP4"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:4KP4"
FT HELIX 402..415
FT /evidence="ECO:0007829|PDB:4CTI"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:4CTI"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:1BXD"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:4CTI"
SQ SEQUENCE 450 AA; 50334 MW; D58444D038722146 CRC64;
MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL AYEVRMLMTD
KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR WAQHYEFLSH QMAQQLGGPT
EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR
IQNRPLVDLE HAALQVGKGI IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG
VSHDLRTPLT RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD
LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR YGNGWIKVSS
GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS GTGLGLAIVQ RIVDNHNGML
ELGTSERGGL SIRAWLPVPV TRAQGTTKEG
