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Protein

Diguanylate cyclase DgcN

Gene

dgcN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Bifunctional protein that catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress. In the presence of high intracellular c-di-GMP levels, and in response to envelope stress, interacts with cell division proteins and halts cell division, without disassembling the Z ring, but by blocking its further progress toward cytokinesis (PubMed:27507823). Part of a network that regulates cell motility by altering levels of c-di-GMP (PubMed:20303158).2 Publications

Catalytic activityi

2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per monomer.By similarity

Enzyme regulationi

Inhibited by YfiR, which prevents relocation to the midcell. A reductive stress signal is required to inactivate YfiR and turn on the DGC activity of DgcN.1 Publication

Pathwayi: 3',5'-cyclic di-GMP biosynthesis

This protein is involved in the pathway 3',5'-cyclic di-GMP biosynthesis, which is part of Purine metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway 3',5'-cyclic di-GMP biosynthesis and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi286MagnesiumBy similarity1
Sitei291Transition state stabilizerSequence analysis1
Binding sitei294SubstrateBy similarity1
Binding sitei299Substrate; via carbonyl oxygenBy similarity1
Binding sitei303SubstrateBy similarity1
Active sitei329Proton acceptorSequence analysis1
Metal bindingi329MagnesiumBy similarity1

GO - Molecular functioni

  • diguanylate cyclase activity Source: EcoCyc
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to cell envelope stress Source: EcoCyc
  • negative regulation of bacterial-type flagellum-dependent cell motility Source: EcoCyc
  • signal transduction Source: InterPro

Keywordsi

Molecular functionTransferase
Biological processStress response
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12880-MONOMER
MetaCyc:EG12880-MONOMER
UniPathwayiUPA00599

Names & Taxonomyi

Protein namesi
Recommended name:
Diguanylate cyclase DgcNCurated (EC:2.7.7.651 Publication)
Short name:
DGCCurated
Gene namesi
Name:dgcN1 Publication
Synonyms:yfiN
Ordered Locus Names:b2604, JW2585
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12880 yfiN

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein Sequence analysis
  • Note: Localizes to the midcell in a Z ring-dependent manner in response to cell envelope stress.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24Cytoplasmic1 PublicationAdd BLAST24
Transmembranei25 – 45HelicalSequence analysisAdd BLAST21
Topological domaini46 – 52Periplasmic1 Publication7
Transmembranei53 – 73HelicalSequence analysisAdd BLAST21
Topological domaini74 – 112Cytoplasmic1 PublicationAdd BLAST39
Transmembranei113 – 133HelicalSequence analysisAdd BLAST21
Topological domaini134 – 154Periplasmic1 PublicationAdd BLAST21
Transmembranei155 – 175HelicalSequence analysisAdd BLAST21
Topological domaini176 – 408Cytoplasmic1 PublicationAdd BLAST233

GO - Cellular componenti

  • cell division site Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Deletion of the gene increases swimming motility and early biofilm formation (PubMed:21181144). Disruption partially suppresses the reduced motility of a pdeH disruption; concomitant disruption of dosC, dgcE, dgcQ and dgcN completely restores motility, suggesting these 4 genes, together with the c-di-GMP phosphodiesterase PdeH, form a network that regulates cell motility by altering levels of c-di-GMP (PubMed:20303158).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi329 – 330DE → AA: Fails to localize to the midcell when exposed to osmotic upshift. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001692701 – 408Diguanylate cyclase DgcNAdd BLAST408

Proteomic databases

PaxDbiP46139
PRIDEiP46139

Expressioni

Inductioni

Expressed at low levels at both 28 and 37 degrees Celsius during transition into stationary phase.1 Publication

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with the cell division proteins FtsZ and ZipA (PubMed:27507823).1 Publication1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263361, 13 interactors
STRINGi316385.ECDH10B_2771

Structurei

3D structure databases

ProteinModelPortaliP46139
SMRiP46139
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini183 – 236HAMPPROSITE-ProRule annotationAdd BLAST54
Domaini278 – 408GGDEFPROSITE-ProRule annotationAdd BLAST131

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108KHX Bacteria
COG2199 LUCA
HOGENOMiHOG000217416
InParanoidiP46139
KOiK21021
OMAiGNDFNAL

Family and domain databases

CDDicd01949 GGDEF, 1 hit
InterProiView protein in InterPro
IPR033417 CHASE8
IPR000160 GGDEF_dom
IPR003660 HAMP_dom
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF17152 CHASE8, 1 hit
PF00990 GGDEF, 1 hit
SMARTiView protein in SMART
SM00267 GGDEF, 1 hit
SUPFAMiSSF55073 SSF55073, 1 hit
TIGRFAMsiTIGR00254 GGDEF, 1 hit
PROSITEiView protein in PROSITE
PS50887 GGDEF, 1 hit
PS50885 HAMP, 1 hit

Sequencei

Sequence statusi: Complete.

P46139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDNDNSLNK RPTFKRALRN ISMTSIFITM MLIWLLLSVT SVLTLKQYAQ
60 70 80 90 100
KNLALTAATM TYSLEAAVVF ADGPAATETL AALGQQGQFS TAEVRDKQQN
110 120 130 140 150
ILASWHYTRK DPGDTFSNFI SHWLFPAPII QPIRHNGETI GEVRLTARDS
160 170 180 190 200
SISHFIWFSL AVLTGCILLA SGIAITLTRH LHNGLVEALK NITDVVHDVR
210 220 230 240 250
SNRNFSRRVS EERIAEFHRF ALDFNSLLDE MEEWQLRLQA KNAQLLRTAL
260 270 280 290 300
HDPLTGLANR AAFRSGINTL MNNSDARKTS ALLFLDGDNF KYINDTWGHA
310 320 330 340 350
TGDRVLIEIA KRLAEFGGLR HKAYRLGGDE FAMVLYDVQS ESEVQQICSA
360 370 380 390 400
LTQIFNLPFD LHNGHQTTMT LSIGYAMTIE HASAEKLQEL ADHNMYQAKH

QRAEKLVR
Length:408
Mass (Da):45,989
Last modified:November 1, 1997 - v2
Checksum:i720B6539EF43DB16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75653.1
AP009048 Genomic DNA Translation: BAA16489.2
X01818 Genomic DNA No translation available.
PIRiG65038
RefSeqiNP_417095.1, NC_000913.3
WP_000969032.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75653; AAC75653; b2604
BAA16489; BAA16489; BAA16489
GeneIDi947091
KEGGiecj:JW2585
eco:b2604
PATRICifig|1411691.4.peg.4135

Similar proteinsi

Entry informationi

Entry nameiDGCN_ECOLI
AccessioniPrimary (citable) accession number: P46139
Secondary accession number(s): P76598, P77005
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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