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Entry version 61 (22 Apr 2020)
Sequence version 1 (19 Jan 2010)
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Protein

Virulence sensor histidine kinase PhoQ

Gene

phoQ

Organism
Salmonella typhimurium (strain 14028s / SGSC 2262)
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 PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg2+ environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg2+, PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg2+, acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.5 Publications

Miscellaneous

Substitutions experiments show that amino acid Thr-48 may be involved in the conformational changes responsible for the balance between kinase-dominant state and phosphatase-dominant state.
The PhoP/PhoQ-signaling cascade, which activates virulence membrane genes (pagC, pagO, pagD, pagK, pgtE and phoN), is induced by cationic antimicrobial peptides (CAMP) (polymyxin, alpha-helical peptide C18G and sheet peptide protegrin-1) at sublethal concentrations.

<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. EC:2.7.13.3

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 Publication, Mg2+1 PublicationNote: Binds up to 3 divalent cations (Ca2+ or Mg2+); their binding site probably overlaps with that of cationic antimicrobial peptides that induce the operon.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi123Divalent metal cation 11
Metal bindingi151Divalent metal cationBy similarity1
Metal bindingi152Divalent metal cationBy similarity1
Metal bindingi154Divalent metal cation 21
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei202Plays a critical role in the switching between kinase and phosphatase statesBy similarity1
Metal bindingi386MagnesiumBy similarity1
Metal bindingi443MagnesiumBy similarity1

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 bindingi386 – 394ATPBy similarity9
Nucleotide bindingi416 – 421ATPBy similarity6
Nucleotide bindingi435 – 447ATPBy similarityAdd BLAST13

<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

GO - Biological processi

<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 functionHydrolase, Kinase, Protein phosphatase, Transferase
Biological processGrowth regulation, Two-component regulatory system, Virulence
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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:
Virulence sensor histidine kinase PhoQ (EC:2.7.13.3, EC:3.1.3.-)
Alternative name(s):
Sensor histidine protein kinase/phosphatase PhoQ
<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:phoQ
Ordered Locus Names:STM14_1408
<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>OrganismiSalmonella typhimurium (strain 14028s / SGSC 2262)
<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 identifieri588858 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
<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
  • UP000002695 <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

<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 – 16Cytoplasmic1 PublicationAdd BLAST16
<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>Transmembranei17 – 37HelicalSequence analysisAdd BLAST21
Topological domaini38 – 193Periplasmic1 PublicationAdd BLAST156
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Topological domaini215 – 487Cytoplasmic1 PublicationAdd BLAST273

GO - Cellular componenti

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

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>Mutagenesisi47T → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi48T → I in pho-24; low affinity for Ca(2+). Confers to cells a PhoP constitutively active phenotype. Affects PhoP/PhoQ-signaling cascade and increase net phosphorylation of PhoP. No effect on initial rate of autophosphorylation and decreases phosphatase activity. 1 Publication1
Mutagenesisi83P → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi88I → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi89Y → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi93G → A: Retains a wild-type Mg(2+) response. Less sensitive to Mg(2+) response than wild-type and defective in Mg(2+) binding; when associated with R-97. 1 Publication1
Mutagenesisi96L → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi97W → A: Retains a wild-type Mg(2+) response. 1 Publication1
Mutagenesisi97W → R: Less sensitive to Mg(2+) response than wild-type and defective in Mg(2+) binding; when associated with A-93. 1 Publication1
Mutagenesisi120H → A: Less sensitive to Mg(2+)response and defective in Mg(2+) binding than wild-type. 1 Publication1
Mutagenesisi149D → A: Less sensitive to Mg(2+) response than wild-type. Retains a wild-type Mg(2+) response in strain PhoP* PhoQ expressing mutant phoP N-93. 1 Publication1
Mutagenesisi150D → A: Less sensitive to Mg(2+) response than wild-type in strain PhoP* PhoQ expressing mutant phoP N-93. 1 Publication1
Mutagenesisi151D → A: Less sensitive to Mg(2+) response than wild-type in strain PhoP* PhoQ expressing mutant phoP N-93. 1 Publication1
Mutagenesisi152D → A: Less sensitive to Mg(2+) response than wild-type in strain PhoP* PhoQ expressing mutant phoP N-93. 1 Publication1
Mutagenesisi156T → A: Less sensitive to Mg(2+) response and defective binding than wild-type. 2 Publications1
Mutagenesisi156T → K: Defective in antimicrobial peptide response. Further decrease; when associated with K-184. 2 Publications1
Mutagenesisi184E → K: Defective in antimicrobial peptide response. Further decrease; when associated with K-156. 1 Publication1
Mutagenesisi277H → A: Retains a wild-type Mg(2+) response only at 10 mM. 1 Publication1
Mutagenesisi277H → V: Retains a wild-type Mg(2+) response only at 10 mM in strain PhoP* PhoQ expressing mutant phoP N-93. Loss of autophosphorylation, irrespective of the presence of Mg(2+). Unable to promote phoP dephosphorylation even in presence of added Mg(2+). 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:4899
PHI:6318
PHI:7356

<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_00004245411 – 487Virulence sensor histidine kinase PhoQAdd BLAST487

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 residuei277Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1 Publication1

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
D0ZV89

<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

The phoP/phoQ operon is positively autoregulated by both PhoP and PhoQ in a Mg2+-dependent manner. Repressed by RcsB via sigma factor RpoS (Probable). Induced by antimicrobial peptides (similar to those in macrophages) and low Mg2+ concentrations.Curated1 Publication

<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; probably dimerizes via the cytoplasmic domain (By similarity).

Interacts with MgrB in the periplasm, altering its activity and that of downstream effector PhoP (Probable).

By similarityCurated

<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

3D structure databases

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

More...
SMRi
D0ZV89

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini215 – 266HAMPPROSITE-ProRule annotationAdd BLAST52
Domaini274 – 481Histidine kinasePROSITE-ProRule annotationAdd BLAST208

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>Regioni51 – 181Sensor domain, required for response to antimicrobial peptidesAdd BLAST131

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_42_0_6

KEGG Orthology (KO)

More...
KOi
K07637

Identification of Orthologs from Complete Genome Data

More...
OMAi
TLVFIYD

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.450.140, 1 hit
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
IPR036097 HisK_dim/P_sf
IPR015014 PhoQ_Sensor
IPR038429 PhoQ_Sensor_sf
IPR004358 Sig_transdc_His_kin-like_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02518 HATPase_c, 1 hit
PF08918 PhoQ_Sensor, 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
SM00387 HATPase_c, 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.

D0ZV89-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKFARHFLP LSLRVRFLLA TAGVVLVLSL AYGIVALVGY SVSFDKTTFR
60 70 80 90 100
LLRGESNLFY TLAKWENNKI SVELPENLDM QSPTMTLIYD ETGKLLWTQR
110 120 130 140 150
NIPWLIKSIQ PEWLKTNGFH EIETNVDATS TLLSEDHSAQ EKLKEVREDD
160 170 180 190 200
DDAEMTHSVA VNIYPATARM PQLTIVVVDT IPIELKRSYM VWSWFVYVLA
210 220 230 240 250
ANLLLVIPLL WIAAWWSLRP IEALAREVRE LEDHHREMLN PETTRELTSL
260 270 280 290 300
VRNLNQLLKS ERERYNKYRT TLTDLTHSLK TPLAVLQSTL RSLRNEKMSV
310 320 330 340 350
SKAEPVMLEQ ISRISQQIGY YLHRASMRGS GVLLSRELHP VAPLLDNLIS
360 370 380 390 400
ALNKVYQRKG VNISMDISPE ISFVGEQNDF VEVMGNVLDN ACKYCLEFVE
410 420 430 440 450
ISARQTDDHL HIFVEDDGPG IPHSKRSLVF DRGQRADTLR PGQGVGLAVA
460 470 480
REITEQYAGQ IIASDSLLGG ARMEVVFGRQ HPTQKEE
Length:487
Mass (Da):55,467
Last modified:January 19, 2010 - 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:iBDCFEFC56F4CA058
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
CP001363 Genomic DNA Translation: ACY87894.1

NCBI Reference Sequences

More...
RefSeqi
WP_001031687.1, NZ_CP043402.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ACY87894; ACY87894; STM14_1408

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
seo:STM14_1408

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|588858.6.peg.1378

<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
CP001363 Genomic DNA Translation: ACY87894.1
RefSeqiWP_001031687.1, NZ_CP043402.1

3D structure databases

SMRiD0ZV89
ModBaseiSearch...

PTM databases

iPTMnetiD0ZV89

Genome annotation databases

EnsemblBacteriaiACY87894; ACY87894; STM14_1408
KEGGiseo:STM14_1408
PATRICifig|588858.6.peg.1378

Phylogenomic databases

HOGENOMiCLU_000445_42_0_6
KOiK07637
OMAiTLVFIYD

Miscellaneous databases

PHI-baseiPHI:4899
PHI:6318
PHI:7356

Family and domain databases

Gene3Di3.30.450.140, 1 hit
3.30.565.10, 1 hit
InterProiView protein in InterPro
IPR003660 HAMP_dom
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR005467 His_kinase_dom
IPR036097 HisK_dim/P_sf
IPR015014 PhoQ_Sensor
IPR038429 PhoQ_Sensor_sf
IPR004358 Sig_transdc_His_kin-like_C
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF08918 PhoQ_Sensor, 1 hit
PRINTSiPR00344 BCTRLSENSOR
SMARTiView protein in SMART
SM00387 HATPase_c, 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 nameiPHOQ_SALT1
<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: D0ZV89
<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: November 13, 2013
Last sequence update: January 19, 2010
Last modified: April 22, 2020
This is version 61 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

Direct protein sequencing
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