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Protein

Osmolarity sensor protein EnvZ

Gene

envZ

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals (By similarity).By similarity

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei347ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi373 – 387ATPBy similarityAdd BLAST15

GO - Molecular functioni

Keywordsi

Molecular functionKinase, Transferase
Biological processTwo-component regulatory system
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Osmolarity sensor protein EnvZ (EC:2.7.13.3)
Gene namesi
Name:envZ
Ordered Locus Names:SF3423, S4340
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 15CytoplasmicCuratedAdd BLAST15
Transmembranei16 – 35HelicalCuratedAdd BLAST20
Topological domaini36 – 158PeriplasmicCuratedAdd BLAST123
Transmembranei159 – 179HelicalCuratedAdd BLAST21
Topological domaini180 – 450CytoplasmicCuratedAdd BLAST271

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000747621 – 450Osmolarity sensor protein EnvZAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi229 – 258Combined sources30
Helixi261 – 263Combined sources3
Helixi264 – 287Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LFRNMR-A/B228-289[»]
2LFSNMR-A/B228-289[»]
ProteinModelPortaliP0AEJ5
SMRiP0AEJ5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini180 – 232HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini240 – 440Histidine kinasePROSITE-ProRule annotationAdd BLAST201

Domaini

The HAMP domain by itself is intrinsically disordered.By similarity

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E0F Bacteria
ENOG410XTWD LUCA
HOGENOMiHOG000218774
KOiK07638
OMAiWIRPPQA

Family and domain databases

CDDicd06225 HAMP, 1 hit
cd00075 HATPase_c, 1 hit
cd00082 HisKA, 1 hit
Gene3Di3.30.565.10, 1 hit
InterProiView protein in InterPro
IPR003660 HAMP_dom
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR005467 His_kinase_dom
IPR003661 HisK_dim/P
IPR036097 HisK_dim/P_sf
IPR004358 Sig_transdc_His_kin-like_C
PfamiView protein in Pfam
PF00672 HAMP, 1 hit
PF02518 HATPase_c, 1 hit
PF00512 HisKA, 1 hit
PRINTSiPR00344 BCTRLSENSOR
SMARTiView protein in SMART
SM00304 HAMP, 1 hit
SM00387 HATPase_c, 1 hit
SM00388 HisKA, 1 hit
SUPFAMiSSF47384 SSF47384, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS50885 HAMP, 1 hit
PS50109 HIS_KIN, 1 hit

Sequencei

Sequence statusi: Complete.

P0AEJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL
60 70 80 90 100
AYEVRMLMTD KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR
110 120 130 140 150
WAQHYEFLSH QMAQQLGGPT EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT
160 170 180 190 200
EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR IQNRPLVDLE HAALQVGKGI
210 220 230 240 250
IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG VSHDLRTPLT
260 270 280 290 300
RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD
310 320 330 340 350
LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR
360 370 380 390 400
YGNGWIKVSS GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS
410 420 430 440 450
GTGLGLAIVQ RIVDNHNGML ELGTSERGGL SIRAWLPVPV TRAQGTTKEG
Length:450
Mass (Da):50,334
Last modified:December 20, 2005 - v1
Checksum:iD58444D038722146
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ288905 Genomic DNA Translation: CAC34269.1
AE005674 Genomic DNA Translation: AAN44884.1
AE014073 Genomic DNA Translation: AAP19295.1
RefSeqiNP_709177.1, NC_004337.2
WP_001253696.1, NZ_NIYV01000043.1

Genome annotation databases

EnsemblBacteriaiAAN44884; AAN44884; SF3423
AAP19295; AAP19295; S4340
GeneIDi1026481
KEGGisfl:SF3423
sfx:S4340
PATRICifig|198214.7.peg.4039

Similar proteinsi

Entry informationi

Entry nameiENVZ_SHIFL
AccessioniPrimary (citable) accession number: P0AEJ5
Secondary accession number(s): P02933
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: May 23, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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