|
1 -> 38
|
MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFA
|
UniProt: In envZ115; low constitutive expression of OmpC or OmpF at low and high osmolarity. Phosphorylates and dephosphorylates OmpR..
|
|
16 -> 35
|
LLLIVTLLFASLVTTYLVVL
|
UniProt: Helical.
|
|
18 -> 18
|
L
|
UniProt: No OmpC, constitutive OmpF, with or without sucrose. No change in phosphorylation or dephosphorylation of OmpR..
|
|
35 -> 35
|
L
|
L → Q: causes an OmpF- OmpCconstitutive phenotype
|
|
41 -> 41
|
P
|
UniProt: Constitutive OmpC, no OmpF, with or without sucrose. Phosphorylates but does not dephosphorylate OmpR..
|
|
71 -> 75
|
VVPPA
|
UniProt: polyP-periplasmic motif; Sequence Annotation Type: short sequence motif.
|
|
73 -> 74
|
PP
|
UniProt: Decreased interaction with MzrA..
|
|
159 -> 179
|
PLFRYTLAIMLLAIGGAWLFI
|
UniProt: Helical.
|
|
177 -> 226
|
LFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAG
|
|
|
180 -> 180
|
R
|
UniProt: No OmpC, constitutive OmpF, with or without sucrose. Weakly phosphorylates OmpR, dephosphorylates normally..
|
|
185 -> 185
|
P
|
UniProt: Constitutive OmpC, no OmpF, with or without sucrose. Weakly phosphorylates but does not dephosphorylate OmpR..
|
|
193 -> 193
|
A
|
UniProt: Promotes the formation of alpha-helical secondary structure of the HAMP domain..
|
|
201 -> 205
|
IPPPL
|
polyP motif located in the cytoplasmic HAMP domain; implicated in dimerization and the ability to respond to osmotic stress
|
|
202 -> 204
|
PPP
|
UniProt: Decreased protein homodimerization, constitutive OmpC, little to no OmpF with or without salt, no interaction with MzrA..
|
|
223 -> 289
|
MAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLR
|
UniProt: Cytoplasmic dimerization domain (CDD), when dimerized forms osmosensitive core; Sequence Annotation Type: region of interest.
|
|
234 -> 234
|
R
|
UniProt: Autophosphorylation by cytoplasmic dimerization domain (CDD) is resistant to waldiomycin..
|
|
235 -> 289
|
TLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLR
|
|
|
239 -> 239
|
A
|
A → T: mutant retains phosphatase activity but lacks kinase activity; cells expressing the mutant protein (in the absence of wild type EnvZ) do not produce detectable levels of OmpC nor OmpF regardless of medium osmolarity
|
|
240 -> 440
|
GVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPV
|
UniProt: Histidine kinase.
|
|
241 -> 241
|
V
|
V → G: causes an OmpF- OmpCconstitutive phenotype; increased levels of phosphoOmpR compared to the wild-type (in low osmolarity medium) (see also |CITS: [19432797]|)
|
|
242 -> 242
|
S
|
UniProt: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin..
|
|
243 -> 243
|
H
|
UniProt: Does not autophosphorylate, does not dephosphorylate OmpR in vitro, no OmpC or OmpF at 0% sucrose, low levels of OmpC and very low levels of OmpF at 15% sucrose..
|
|
244 -> 244
|
D
|
UniProt: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin..
|
|
247 -> 247
|
T
|
T → R: causes the OmpF-, LamB-, PhoA-, OmpCconstitutive phenotype; mutant protein retains kinase activity but is defective in phospho-OmpR phosphatase activity in vitro (see also |CITS: [2160945][2656631][10973966][19432797]|)
|
|
248 -> 248
|
P
|
UniProt: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin, alters structure..
|
|
256 -> 265
|
TEMMSEQDGY
|
functionally important determinant of autophosphorylation mechanism (ie. cis or trans)
|
|
336 -> 438
|
SIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPV
|
|
|
347 -> 351
|
NAARY
|
UniProt: ATP.
|
|
351 -> 351
|
Y
|
Y → S: loss of kinase and phospho-OmpR phosphatase activity in vitro
|
|
392 -> 393
|
RG
|
UniProt: ATP.
|
|
397 -> 397
|
R
|
R → L: constitutively activated (9-fold increase in omr::lacZ activity compared to wild type); suppresses the envelope stress phenotype of a ΔbamB ΔdegP strain; mutant protein likely has diminished phosphatase activity
|
|
402 -> 406
|
TGLGL
|
UniProt: ATP.
|