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Protein

Cyclic diguanosine monophosphate-binding protein PA4608

Gene

PA4608

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei40Important for c-di-GMP binding1
Binding sitei77c-di-GMP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi6 – 13c-di-GMP1 Publication8

GO - Molecular functioni

  • cyclic-di-GMP binding Source: UniProtKB

GO - Biological processi

Keywordsi

Ligandc-di-GMP, Nucleotide-binding

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-4702-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic diguanosine monophosphate-binding protein PA46083 Publications
Short name:
c-di-GMP-binding protein PA46083 Publications
Alternative name(s):
Pilz domain-containing protein PA46083 Publications
Gene namesi
Ordered Locus Names:PA4608
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4608

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9R → A: Abolishes c-di-GMP binding. 1 Publication1
Mutagenesisi13R → A: Abolishes c-di-GMP binding. 1 Publication1
Mutagenesisi40G → A: Abolishes c-di-GMP binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004231811 – 125Cyclic diguanosine monophosphate-binding protein PA4608Add BLAST125

Proteomic databases

PaxDbiQ9HVI1

Interactioni

Subunit structurei

Monomer in both c-di-GMP-bound and free forms.3 Publications

Protein-protein interaction databases

STRINGi208964.PA4608

Structurei

Secondary structure

1125
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9HVI1
SMRiQ9HVI1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HVI1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 103PilZSequence analysisAdd BLAST97

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 13RXXXR motif; surrounds the surface of the c-di-GMP binding site2 Publications5
Motifi35 – 40DXSXXG motif; surrounds the surface of the c-di-GMP binding site2 Publications6

Domaini

Consists of a six-stranded anti-parallel beta-barrel core structure with an unstructured N-terminus in apo-form and a C-terminal alpha helix. In the holo-form the C-terminal helix is displaced by the ligand, thereby opening one side of the beta-barrel as a binding site, and the N-terminus containing the RXXXR motif wraps around the ligand and in turn ties the C-terminal helix in a loose conformation. The structural rearrangement upon ligand binding creates a significant change in surface charge distribution.3 Publications

Phylogenomic databases

HOGENOMiHOG000283213
OMAiGFVCRHI
PhylomeDBiQ9HVI1

Family and domain databases

InterProiView protein in InterPro
IPR027021 C-di-GMP_BP_PA4608
IPR009875 PilZ_domain
PfamiView protein in Pfam
PF07238 PilZ, 1 hit
PIRSFiPIRSF028141 C-di-GMP_BP_PA4608, 1 hit

Sequencei

Sequence statusi: Complete.

Q9HVI1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDQHDERRR FHRIAFDADS EILQGERRWE VLLHDVSLHG ILVGQPQDWN
60 70 80 90 100
GDPQRPFEAR LYLGLDVLIR MEISLAWARD GLLGFECQHI DLDSISHLRR
110 120
LVELNLGDEE LLERELALLV SAHDD
Length:125
Mass (Da):14,573
Last modified:March 1, 2001 - v1
Checksum:iAB6D8110967348B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG07996.1
PIRiH83068
RefSeqiNP_253298.1, NC_002516.2
WP_003094864.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG07996; AAG07996; PA4608
GeneIDi881102
KEGGipae:PA4608
PATRICifig|208964.12.peg.4823

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG07996.1
PIRiH83068
RefSeqiNP_253298.1, NC_002516.2
WP_003094864.1, NC_002516.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YWUNMR-A1-125[»]
2L74NMR-A1-125[»]
5XLYX-ray1.76B1-125[»]
5Y4RX-ray2.30C/D2-125[»]
ProteinModelPortaliQ9HVI1
SMRiQ9HVI1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4608

Proteomic databases

PaxDbiQ9HVI1

Protocols and materials databases

DNASUi881102
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07996; AAG07996; PA4608
GeneIDi881102
KEGGipae:PA4608
PATRICifig|208964.12.peg.4823

Organism-specific databases

PseudoCAPiPA4608

Phylogenomic databases

HOGENOMiHOG000283213
OMAiGFVCRHI
PhylomeDBiQ9HVI1

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-4702-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ9HVI1

Family and domain databases

InterProiView protein in InterPro
IPR027021 C-di-GMP_BP_PA4608
IPR009875 PilZ_domain
PfamiView protein in Pfam
PF07238 PilZ, 1 hit
PIRSFiPIRSF028141 C-di-GMP_BP_PA4608, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCDGBP_PSEAE
AccessioniPrimary (citable) accession number: Q9HVI1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 93 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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