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Protein

Probable diguanylate cyclase DgcQ

Gene

dgcQ

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

Functioni

Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (By similarity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of cellulose production (PubMed:20303158).By similarity1 Publication

Catalytic activityi

2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.By similarity

Cofactori

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

Pathwayi: bacterial cellulose biosynthesis

This protein is involved in the pathway bacterial cellulose biosynthesis, which is part of Glycan metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway bacterial cellulose biosynthesis and in Glycan metabolism.

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 bindingi436MagnesiumBy similarity1
Sitei441Transition state stabilizerSequence analysis1
Binding sitei444SubstrateBy similarity1
Binding sitei449Substrate; via carbonyl oxygenBy similarity1
Binding sitei453SubstrateBy similarity1
Active sitei479Proton acceptorSequence analysis1
Metal bindingi479MagnesiumBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cellulose biosynthetic process Source: UniProtKB-KW
  • negative regulation of bacterial-type flagellum-dependent cell motility Source: EcoCyc

Keywordsi

Molecular functionTransferase
Biological processCellulose biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7049-MONOMER
UniPathwayiUPA00599
UPA00694

Protein family/group databases

TCDBi9.B.34.1.4 the kinase/phosphatase/cyclic-gmp synthase/cyclic di-gmp hydrolase (kpsh) family

Names & Taxonomyi

Protein namesi
Recommended name:
Probable diguanylate cyclase DgcQCurated (EC:2.7.7.65By similarity)
Short name:
DGCCurated
Alternative name(s):
Cellulose synthesis regulatory protein
Gene namesi
Name:dgcQ1 Publication
Synonyms:yedQ
Ordered Locus Names:b1956, JW5832
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14040 yedQ

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Transmembranei360 – 380HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001690971 – 564Probable diguanylate cyclase DgcQAdd BLAST564

Proteomic databases

PaxDbiP76330
PRIDEiP76330

Expressioni

Inductioni

Constitutively expressed at both 28 and 37 degrees Celsius. Induced by 0.3 M NaCl. Expression is RpoS dependent.2 Publications

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4261052, 3 interactors
STRINGi316385.ECDH10B_2098

Structurei

3D structure databases

ProteinModelPortaliP76330
SMRiP76330
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini428 – 563GGDEFPROSITE-ProRule annotationAdd BLAST136

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZU Bacteria
ENOG410XNMH LUCA
HOGENOMiHOG000121343
KOiK21085
OMAiWLVIRRM

Family and domain databases

CDDicd01949 GGDEF, 1 hit
InterProiView protein in InterPro
IPR033416 CHASE7
IPR000160 GGDEF_dom
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF17151 CHASE7, 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

Sequencei

Sequence statusi: Complete.

P76330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQHETKMENQ SWLKKLARRL GPGHVVNLCF IVVLLFSTLL TWREVVVLED
60 70 80 90 100
AYISSQRNHL ENVANALDKH LQYNVDKLIF LRNGMREALV APLDFTSLRD
110 120 130 140 150
AVTEFEQHRD EHAWKIELNR RRTLPVNGVS DALVSEGNLL SRENESLDNE
160 170 180 190 200
ITAALEVGYL LRLAHNSSSM VEQAMYVSRA GFYVSTQPTL FTRNVPTRYY
210 220 230 240 250
GYVTQPWFIG HSQRENRHRA VRWFTSQPEH ASNTEPQVTV SVPVDSNNYW
260 270 280 290 300
YGVLGMSIPV RTMQQFLRNA IDKNLDGEYQ LYDSKLRFLT SSNPDHPTGN
310 320 330 340 350
IFDPRELALL AQAMEHDTRG GIRMDSRYVS WERLDHFDGV LVRVHTLSEG
360 370 380 390 400
VRGDFGSISI ALTLLWALFT TMLLISWYVI RRMVSNMYVL QSSLQWQAWH
410 420 430 440 450
DTLTRLYNRG ALFEKARPLA KLCQTHQHPF SVIQVDLDHF KAINDRFGHQ
460 470 480 490 500
AGDRVLSHAA GLISSSLRAQ DVAGRVGGEE FCVILPGASL TEAAEVAERI
510 520 530 540 550
RLKLNEKEML IAKSTTIRIS ASLGVSSSEE TGDYDFEQLQ SLADRRLYLA
560
KQAGRNRVFA SDNA
Length:564
Mass (Da):64,283
Last modified:March 5, 2002 - v2
Checksum:i05FB02C1BE2A8938
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75022.2
AP009048 Genomic DNA Translation: BAA15784.1
PIRiH64959
RefSeqiNP_416465.2, NC_000913.3
WP_001350521.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75022; AAC75022; b1956
BAA15784; BAA15784; BAA15784
GeneIDi946471
KEGGiecj:JW5832
eco:b1956
PATRICifig|1411691.4.peg.296

Similar proteinsi

Entry informationi

Entry nameiDGCQ_ECOLI
AccessioniPrimary (citable) accession number: P76330
Secondary accession number(s): P94746
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: July 18, 2018
This is version 133 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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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