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UniProtKB - P0AEJ4 (ENVZ_ECOLI)

Entry version 133 (17 Jun 2020)
Sequence version 1 (20 Dec 2005)
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Protein

Sensor histidine kinase EnvZ

Gene

envZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (PubMed:2997120, PubMed:3536870). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (PubMed:2656684, PubMed:2668281, PubMed:2668953, PubMed:2674113, PubMed:2558046, PubMed:2277041, PubMed:1323560). Also dephosphorylates OmpR in the presence of ATP (PubMed:2668281, PubMed:2558046, PubMed:2277041, PubMed:1323560). The cytoplasmic dimerization domain (CDD) forms an osmosensitive core; increasing osmolarity stabilizes this segment (possibly by its contraction), enhancing the autophosphorylation rate and consequently, downstream phosphotransfer to OmpR and signaling (PubMed:22543870, PubMed:28256224). Autophosphorylation is greater when full-length EnvZ is reconstituted in a lipid environment, lipid-mediated allostery impacts the kinase function of EnvZ (PubMed:28256224). Involved in acid stress response; this requires EnvZ but not OmpR phosphorylation, and suggests that EnvZ senses cytoplasmic acidic pH (PubMed:29138484).12 Publications

Miscellaneous

Cross talk between this and the Che and Ntr two-component systems can occur at least in vitro.1 Publication
Two or more proline residues often cause ribosome stalling and decreased protein translation; the cytoplasmic strong stop motif IPPPL does not have this effect and instead is involved in homodimerization, while the weaker periplasmic stop motif VVPPA motif is involved in MzrA interaction.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.3 Publications1 Publication EC:2.7.13.3

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity is modulated by MzrA (PubMed:19432797, PubMed:20889743). In the presence of 0.2 M NaCl, 2.0 mM sodium cholate (bile salts) decreases expression from the ompC promoter; how this is mediated is unknown (PubMed:28423182). Autophosphorylation is inhibited by the angucycline antibiotic waldiomycin in a non-competitive manner; waldiomycin prevents dimerization of the cytoplasmic domain and autophosphorylation (PubMed:27999439).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei243ATPCombined sources1
Binding sitei373ATPCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi347 – 351ATPCombined sources5
Nucleotide bindingi392 – 393ATPCombined sources2
Nucleotide bindingi402 – 406ATPCombined sources5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Transferase
Biological processStress response, Two-component regulatory system
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:ENVZ-MONOMER
ECOL316407:JW3367-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.13.3 2026

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sensor histidine kinase EnvZCurated (EC:2.7.13.31 Publication)
Alternative name(s):
Osmolarity sensor protein EnvZCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:envZ
Synonyms:ompB, perA, tpo
Ordered Locus Names:b3404, JW3367
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 15Cytoplasmic1 PublicationAdd BLAST15
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei16 – 35Helical1 PublicationAdd BLAST20
Topological domaini36 – 158Periplasmic1 PublicationAdd BLAST123
Transmembranei159 – 179Helical1 PublicationAdd BLAST21
Topological domaini180 – 450Cytoplasmic3 PublicationsAdd BLAST271

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No expression of OmpC or OmpF during growth at 0% sucrose, low expression of OmpF at 15% sucrose (PubMed:3056929). Single deletion of envZ has no OmpC or OmpF at 0% sucrose, low levels of OmpC and very low levels of OmpF at 15% sucrose. Deletion of both ompR and envZ leads to loss of both OmpC and OmpF expression at 0% and 15% sucrose (PubMed:2277041).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 38MRRLR…VLNFA → MTMITDSL in envZ115; low constitutive expression of OmpC or OmpF at low and high osmolarity. Phosphorylates and dephosphorylates OmpR. 2 PublicationsAdd BLAST38
Mutagenesisi18L → F: No OmpC, constitutive OmpF, with or without sucrose. No change in phosphorylation or dephosphorylation of OmpR. 1 Publication1
Mutagenesisi41P → L or S: Constitutive OmpC, no OmpF, with or without sucrose. Phosphorylates but does not dephosphorylate OmpR. 1 Publication1
Mutagenesisi73 – 74PP → AA: Decreased interaction with MzrA. 1 Publication2
Mutagenesisi180R → C: No OmpC, constitutive OmpF, with or without sucrose. Weakly phosphorylates OmpR, dephosphorylates normally. 1 Publication1
Mutagenesisi185P → L: Constitutive OmpC, no OmpF, with or without sucrose. Weakly phosphorylates but does not dephosphorylate OmpR. 1 Publication1
Mutagenesisi193A → L: Promotes the formation of alpha-helical secondary structure of the HAMP domain. 1 Publication1
Mutagenesisi193A → V: No effect. 1 Publication1
Mutagenesisi202 – 204PPP → AAA: Decreased protein homodimerization, constitutive OmpC, little to no OmpF with or without salt, no interaction with MzrA. 1 Publication3
Mutagenesisi234R → A: Autophosphorylation by cytoplasmic dimerization domain (CDD) is resistant to waldiomycin. 1 Publication1
Mutagenesisi242S → A: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin. 1 Publication1
Mutagenesisi243H → R: 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. 1 Publication1
Mutagenesisi243H → V: Does not autophosphorylate, does not transfer phosphate to OmpR, increased expression of ompC, decreased expression of OmpF. 1 Publication1
Mutagenesisi244D → A: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin. 1 Publication1
Mutagenesisi247T → A: Autophosphorylation by CDD is somewhat resistant to waldiomycin. 1 Publication1
Mutagenesisi247T → R in envZ11/MH1461; OmpF- OmpC constitutive. Also prevents expression of PhoA and LamB. Phosphorylates OmpR but does not dephosphorylate it. 3 Publications1
Mutagenesisi248P → A: Autophosphorylation by CDD is resistant to waldiomycin, CDD peptide probably no longer binds waldiomycin, alters structure. 1 Publication1
Mutagenesisi347N → D: Loss of ATP binding; loss of autophosphorylation. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000747591 – 450Sensor histidine kinase EnvZAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei243Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated (PubMed:3056929, PubMed:2656684, PubMed:2668281, PubMed:2668953, PubMed:8132603, PubMed:2277041). Incubation of isolated EnvZ C-terminal fragment (residues 180-450) with increasing levels of NaCl or sucrose increases its autophosphorylation (PubMed:17635923).1 Publication6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AEJ4

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0AEJ4

PRoteomics IDEntifications database

More...PRIDEi		P0AEJ4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0AEJ4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Part of the ompR-envZ operon.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:10426948, PubMed:15357641, PubMed:9817206, PubMed:28256224, PubMed:29953503, PubMed:27999439).

Interacts with MzrA (PubMed:19432797, PubMed:20889743, PubMed:29953503).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261266, 47 interactors

Database of interacting proteins

More...DIPi		DIP-48357N

Protein interaction database and analysis system

More...IntActi		P0AEJ4, 5 interactors

Molecular INTeraction database

More...MINTi		P0AEJ4

STRING: functional protein association networks

More...STRINGi		511145.b3404

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0AEJ4

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AEJ4

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini180 – 232HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini240 – 440Histidine kinasePROSITE-ProRule annotationAdd BLAST201

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni223 – 289Cytoplasmic dimerization domain (CDD), when dimerized forms osmosensitive core1 PublicationAdd BLAST67

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi71 – 75polyP-periplasmic motif1 Publication5
Motifi201 – 205polyP-cytoplasmic motif1 Publication5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The periplasmic domain interacts with MzrA (PubMed:20889743) (Probable). The periplasmic domain assumes a PDC sensor fold (PubMed:28423182). The HAMP domain by itself is intrinsically disordered (PubMed:17635923). The cytoplasmic dimerization domain (CDD, residues 223-289) forms an osmosensitive core; increasing osmolarity stabilizes this segment, enhancing its autophosphorylation rate and consequently, downstream phosphotransfer to OmpR and signaling (PubMed:17635923, PubMed:28256224). The autophosphorylation activity of the CDD is inhibited by the angucycline antibiotic waldiomycin which probably binds to it (PubMed:27999439). The soluble EnvZ C-terminal fragment (residues 180-450) is capable of conferring osmolarity-sensitive expression of OmpC in the absence of the membrane anchor (PubMed:17635923).1 Publication5 Publications

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105E0F Bacteria
ENOG410XTWD LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000445_89_27_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AEJ4

KEGG Orthology (KO)

More...KOi		K07638

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AEJ4

Family and domain databases

Conserved Domains Database

More...CDDi		cd06225 HAMP, 1 hit
cd00082 HisKA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.565.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00672 HAMP, 1 hit
PF02518 HATPase_c, 1 hit
PF00512 HisKA, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00344 BCTRLSENSOR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00304 HAMP, 1 hit
SM00387 HATPase_c, 1 hit
SM00388 HisKA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47384 SSF47384, 1 hit
SSF55874 SSF55874, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50885 HAMP, 1 hit
PS50109 HIS_KIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0AEJ4-1 [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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD58444D038722146
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J01656 Unassigned RNA Translation: AAA16242.1
U18997 Genomic DNA Translation: AAA58201.1
U00096 Genomic DNA Translation: AAC76429.1
AP009048 Genomic DNA Translation: BAE77887.1

Protein sequence database of the Protein Information Resource

More...PIRi		B25024 MMECZB

NCBI Reference Sequences

More...RefSeqi		NP_417863.1, NC_000913.3
WP_001253696.1, NZ_STEB01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76429; AAC76429; b3404
BAE77887; BAE77887; BAE77887

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947272

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3367
eco:b3404

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3325

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01656 Unassigned RNA Translation: AAA16242.1
U18997 Genomic DNA Translation: AAA58201.1
U00096 Genomic DNA Translation: AAC76429.1
AP009048 Genomic DNA Translation: BAE77887.1
PIRiB25024 MMECZB
RefSeqiNP_417863.1, NC_000913.3
WP_001253696.1, NZ_STEB01000004.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXDNMR-A290-450[»]
1JOYNMR-A/B223-289[»]
1NJVmodel-A/B223-450[»]
3ZCCX-ray1.25A/B229-288[»]
3ZRVX-ray1.65A/B229-290[»]
3ZRWX-ray2.25A/C/D229-289[»]
B231-289[»]
3ZRXX-ray1.25A/B229-289[»]
4CTIX-ray2.85A/B/C/D228-450[»]
4KP4X-ray3.00A/B223-253[»]
A/B266-450[»]
5B1NX-ray1.33A223-289[»]
5B1OX-ray2.30A/B223-289[»]
5XGAX-ray1.95A36-158[»]
SMRiP0AEJ4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261266, 47 interactors
DIPiDIP-48357N
IntActiP0AEJ4, 5 interactors
MINTiP0AEJ4
STRINGi511145.b3404

Chemistry databases

DrugBankiDB04395 Phosphoaminophosphonic Acid-Adenylate Ester

PTM databases

iPTMnetiP0AEJ4

Proteomic databases

jPOSTiP0AEJ4
PaxDbiP0AEJ4
PRIDEiP0AEJ4

Genome annotation databases

EnsemblBacteriaiAAC76429; AAC76429; b3404
BAE77887; BAE77887; BAE77887
GeneIDi947272
KEGGiecj:JW3367
eco:b3404
PATRICifig|1411691.4.peg.3325

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0265

Phylogenomic databases

eggNOGiENOG4105E0F Bacteria
ENOG410XTWD LUCA
HOGENOMiCLU_000445_89_27_6
InParanoidiP0AEJ4
KOiK07638
PhylomeDBiP0AEJ4

Enzyme and pathway databases

BioCyciEcoCyc:ENVZ-MONOMER
ECOL316407:JW3367-MONOMER
BRENDAi2.7.13.3 2026

Miscellaneous databases

EvolutionaryTraceiP0AEJ4

Protein Ontology

More...PROi		PR:P0AEJ4

Family and domain databases

CDDicd06225 HAMP, 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiENVZ_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AEJ4
Secondary accession number(s): P02933, Q2M769
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: June 17, 2020
This is version 133 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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