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Entry version 174 (02 Jun 2021)
Sequence version 4 (04 Dec 2007)
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Protein

Oxygen sensor protein DosP

Gene

dosP

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

Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957).

Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.

3 Publications

Miscellaneous

Binds O2 with a dissociation constant of about 74 µM.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Has c-di-GMP PDE activity in both Fe2+ and Fe3+-bound forms; this activity is increased 6-7 fold by binding of O2 and CO (PubMed:15995192) and NO (PubMed:17535805). Has cAMP PDE activity only when the heme is in the Fe2+ form. cAMP PDE activity is inhibited by oxidation of the heme iron and by binding of external ligands such as CO and NO. Also strongly inhibited by etazolate hydrochloride, a selective cAMP PDE inhibitor. PDE activity is inhibited in the absence of oxygen.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

For the EAL domain, residues 532-799.1 Publication
  1. KM=36 µM for c-di-GMP

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi69Iron (heme proximal ligand)1
Metal bindingi87Iron (heme distal ligand)1

<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
Biological processSensory transduction, Transcription, Transcription regulation
Ligandc-di-GMP, Heme, Iron, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6783-MONOMER
MetaCyc:G6783-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P76129

<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_and_taxonomy_section">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:
Oxygen sensor protein DosP (EC:3.1.4.52)
Alternative name(s):
Direct oxygen-sensing phosphodiesterase
Short name:
Direct oxygen sensor protein
Ec DOS
Heme-regulated cyclic di-GMP phosphodiesterase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:dosP
Synonyms:dos, pdeO1 Publication, yddU
Ordered Locus Names:b1489, JW1484
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 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_and_biotech_section">'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>Mutagenesisi69H → A or G: Loss of heme binding. 2 Publications1
Mutagenesisi75H → A or G: No loss of heme binding. 1 Publication1
Mutagenesisi87M → A or I: Ferrous heme iron changes from an exclusively hexacoordinate low-spin form to an exclusively pentacoordinate high-spin form. Ferric heme iron remains hexacoordinate but becomes a mixture of high and low spin. Increases c-di-GMP PDE activity 7-fold in absence of O(2), CO or NO, no additional increase upon addition of gases (M-A only). 3 Publications1
Mutagenesisi87M → H: No change in heme coordination; increases c-di-GMP PDE activity 2-fold in absence of O(2), CO or NO, and 2-fold more upon addition of gases. 3 Publications1
Mutagenesisi89R → A, E or I: The Fe(2+)-O(2) form loses c-di-GMP PDE activity, due to reduced O(2) affinity and/or increased auto-oxidation. NO and CO forms are less affected. 2 Publications1
Mutagenesisi91L → F: Alters O(2) binding, increases auto-oxidation. 1 Publication1
Mutagenesisi91L → T: Increases auto-oxidation. 1 Publication1
Mutagenesisi107L → F: Significantly reduces heme-binding affinity; increases auto-oxidation. 1 Publication1
Mutagenesisi107L → T: Increases auto-oxidation. 1 Publication1
Mutagenesisi582H → A: Loss of cAMP PDE activity. 1 Publication1
Mutagenesisi586H → A: Loss of cAMP PDE activity. 1 Publication1

<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_00000799821 – 799Oxygen sensor protein DosPAdd BLAST799

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

The heme distal ligand is coordinated by Met-87 in the active Fe2+ (ferrous) form, by O2 in the O2-bound form and by H2O in the inactive Fe3+ (ferric) form.

Proteomic databases

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

More...
PaxDbi
P76129

PRoteomics IDEntifications database

More...
PRIDEi
P76129

<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

Expressed in the late exponential growth phase and at higher levels in the stationary phase. A member of the dosCP operon. Expression is RpoS dependent and is higher at 28 degrees Celsius than at 37 degrees Celsius.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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:19864414); has been previously suggested to be a homotetramer based on size exclusion chromatography (PubMed:11970957).

Forms a complex with DosC.

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259419, 16 interactors
850182, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3982, dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex

Protein interaction database and analysis system

More...
IntActi
P76129, 3 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1489

<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

1799
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
P76129

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
P76129

<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_and_domains_section">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>Domaini10 – 81PAS 1PROSITE-ProRule annotationAdd BLAST72
Domaini134 – 207PAS 2PROSITE-ProRule annotationAdd BLAST74
Domaini208 – 260PACPROSITE-ProRule annotationAdd BLAST53
Domaini402 – 532GGDEFPROSITE-ProRule annotationAdd BLAST131
Domaini541 – 795EALPROSITE-ProRule annotationAdd BLAST255

<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 EAL domain (residues 532 to 799) is a cyclic dinucleotide di-GMP (c-di-GMP) PDE hydrolyzing c-di-GMP to 5'pGpG; it has no activity on cAMP.1 Publication
Binding of an external ligand to the heme located in the N-terminal sensory domain displaces the distal heme ligand from Met-87 to the ligand and triggers a conformational change that regulates the activity of the C-terminal catalytic domain.
The heme-PAS domain (residues 1-139) forms homodimers.

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2199, Bacteria
COG2200, Bacteria
COG2202, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_70_20_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P76129

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P76129

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01948, EAL, 1 hit
cd01949, GGDEF, 1 hit
cd00130, PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.450, 1 hit
3.30.70.270, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012226, Diguanyl_cyclase/Pdiesterase
IPR001633, EAL_dom
IPR035919, EAL_sf
IPR000160, GGDEF_dom
IPR029787, Nucleotide_cyclase
IPR001610, PAC
IPR000014, PAS
IPR000700, PAS-assoc_C
IPR035965, PAS-like_dom_sf
IPR043128, Rev_trsase/Diguanyl_cyclase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00563, EAL, 1 hit
PF00990, GGDEF, 1 hit
PF13426, PAS_9, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005925, Dos, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00052, EAL, 1 hit
SM00267, GGDEF, 1 hit
SM00086, PAC, 2 hits
SM00091, PAS, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF141868, SSF141868, 1 hit
SSF55073, SSF55073, 1 hit
SSF55785, SSF55785, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00254, GGDEF, 1 hit
TIGR00229, sensory_box, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50883, EAL, 1 hit
PS50887, GGDEF, 1 hit
PS50113, PAC, 1 hit
PS50112, PAS, 2 hits

<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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P76129-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLTDADNAA DGIFFPALEQ NMMGAVLINE NDEVMFFNPA AEKLWGYKRE
60 70 80 90 100
EVIGNNIDML IPRDLRPAHP EYIRHNREGG KARVEGMSRE LQLEKKDGSK
110 120 130 140 150
IWTRFALSKV SAEGKVYYLA LVRDASVEMA QKEQTRQLII AVDHLDRPVI
160 170 180 190 200
VLDPERHIVQ CNRAFTEMFG YCISEASGMQ PDTLLNIPEF PADNRIRLQQ
210 220 230 240 250
LLWKTARDQD EFLLLTRTGE KIWIKASISP VYDVLAHLQN LVMTFSDITE
260 270 280 290 300
ERQIRQLEGN ILAAMCSSPP FHEMGEIICR NIESVLNESH VSLFALRNGM
310 320 330 340 350
PIHWASSSHG AEIQNAQSWS ATIRQRDGAP AGILQIKTSS GAETSAFIER
360 370 380 390 400
VADISQHMAA LALEQEKSRQ HIEQLIQFDP MTGLPNRNNL HNYLDDLVDK
410 420 430 440 450
AVSPVVYLIG VDHIQDVIDS LGYAWADQAL LEVVNRFREK LKPDQYLCRI
460 470 480 490 500
EGTQFVLVSL ENDVSNITQI ADELRNVVSK PIMIDDKPFP LTLSIGISYD
510 520 530 540 550
LGKNRDYLLS TAHNAMDYIR KNGGNGWQFF SPAMNEMVKE RLVLGAALKE
560 570 580 590 600
AISNNQLKLV YQPQIFAETG ELYGIEALAR WHDPLHGHVP PSRFIPLAEE
610 620 630 640 650
IGEIENIGRW VIAEACRQLA EWRSQNIHIP ALSVNLSALH FRSNQLPNQV
660 670 680 690 700
SDAMHAWGID GHQLTVEITE SMMMEHDTEI FKRIQILRDM GVGLSVDDFG
710 720 730 740 750
TGFSGLSRLV SLPVTEIKID KSFVDRCLTE KRILALLEAI TSIGQSLNLT
760 770 780 790
VVAEGVETKE QFEMLRKIHC RVIQGYFFSR PLPAEEIPGW MSSVLPLKI
Length:799
Mass (Da):90,260
Last modified:December 4, 2007 - v4
<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:i4CE770D2A6B39D5F
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
U00096 Genomic DNA Translation: AAC74562.2
AP009048 Genomic DNA Translation: BAA15154.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D64902

NCBI Reference Sequences

More...
RefSeqi
NP_416006.4, NC_000913.3
WP_001360132.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74562; AAC74562; b1489
BAA15154; BAA15154; BAA15154

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945815

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1484
eco:b1489

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.778

<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
U00096 Genomic DNA Translation: AAC74562.2
AP009048 Genomic DNA Translation: BAA15154.1
PIRiD64902
RefSeqiNP_416006.4, NC_000913.3
WP_001360132.1, NZ_LN832404.1

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
1S66X-ray1.80L/U8-126[»]
1S67X-ray1.50L/U8-126[»]
1V9YX-ray1.32A/B1-139[»]
1V9ZX-ray1.90A/B1-139[»]
1VB6X-ray1.56A/B1-139[»]
4HU3X-ray3.30A529-799[»]
4HU4X-ray2.40A/B529-799[»]
SMRiP76129
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259419, 16 interactors
850182, 1 interactor
ComplexPortaliCPX-3982, dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex
IntActiP76129, 3 interactors
STRINGi511145.b1489

Proteomic databases

PaxDbiP76129
PRIDEiP76129

Genome annotation databases

EnsemblBacteriaiAAC74562; AAC74562; b1489
BAA15154; BAA15154; BAA15154
GeneIDi945815
KEGGiecj:JW1484
eco:b1489
PATRICifig|1411691.4.peg.778

Organism-specific databases

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

More...
EchoBASEi
EB3553

Phylogenomic databases

eggNOGiCOG2199, Bacteria
COG2200, Bacteria
COG2202, Bacteria
HOGENOMiCLU_000445_70_20_6
InParanoidiP76129
PhylomeDBiP76129

Enzyme and pathway databases

BioCyciEcoCyc:G6783-MONOMER
MetaCyc:G6783-MONOMER
SABIO-RKiP76129

Miscellaneous databases

EvolutionaryTraceiP76129

Protein Ontology

More...
PROi
PR:P76129

Family and domain databases

CDDicd01948, EAL, 1 hit
cd01949, GGDEF, 1 hit
cd00130, PAS, 2 hits
Gene3Di3.20.20.450, 1 hit
3.30.70.270, 1 hit
InterProiView protein in InterPro
IPR012226, Diguanyl_cyclase/Pdiesterase
IPR001633, EAL_dom
IPR035919, EAL_sf
IPR000160, GGDEF_dom
IPR029787, Nucleotide_cyclase
IPR001610, PAC
IPR000014, PAS
IPR000700, PAS-assoc_C
IPR035965, PAS-like_dom_sf
IPR043128, Rev_trsase/Diguanyl_cyclase
PfamiView protein in Pfam
PF00563, EAL, 1 hit
PF00990, GGDEF, 1 hit
PF13426, PAS_9, 2 hits
PIRSFiPIRSF005925, Dos, 1 hit
SMARTiView protein in SMART
SM00052, EAL, 1 hit
SM00267, GGDEF, 1 hit
SM00086, PAC, 2 hits
SM00091, PAS, 2 hits
SUPFAMiSSF141868, SSF141868, 1 hit
SSF55073, SSF55073, 1 hit
SSF55785, SSF55785, 2 hits
TIGRFAMsiTIGR00254, GGDEF, 1 hit
TIGR00229, sensory_box, 2 hits
PROSITEiView protein in PROSITE
PS50883, EAL, 1 hit
PS50887, GGDEF, 1 hit
PS50113, PAC, 1 hit
PS50112, PAS, 2 hits

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiDOSP_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: P76129
Secondary accession number(s): P76872, P77708
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 4, 2007
Last modified: June 2, 2021
This is version 174 of the entry and version 4 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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