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Protein

Cyclic-di-GMP-binding biofilm dispersal mediator protein

Gene

bdcA

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

Functioni

Increases biofilm dispersal. Acts by binding directly to the signaling molecule cyclic-di-GMP, which decreases the intracellular concentration of cyclic-di-GMP and leads to biofilm dispersal. Also controls other biofilm-related phenotypes such as cell motility, cell size, cell aggregation and production of extracellular DNA and extracellular polysaccharides (EPS). Does not act as a phosphodiesterase.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei132SubstrateBy similarity1
Active sitei146Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 34NAD or NADPBy similarityAdd BLAST25

GO - Molecular functioni

  • cyclic-di-GMP binding Source: EcoCyc
  • NADPH binding Source: EcoCyc
  • oxidoreductase activity Source: InterPro

GO - Biological processi

  • single-species biofilm formation Source: EcoCyc

Keywordsi

Ligandc-di-GMP

Enzyme and pathway databases

BioCyciEcoCyc:G7880-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic-di-GMP-binding biofilm dispersal mediator protein
Gene namesi
Name:bdcA
Synonyms:yjgI
Ordered Locus Names:b4249, JW4207
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12528 bdcA

Pathology & Biotechi

Disruption phenotypei

Mutant shows decreased biofilm dispersal. Deletion increases the cyclic-di GMP concentration in the cell.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi50E → Q or V: Shows higher affinity for cyclic-di-GMP, increases swimming motility and biofilm dispersal. Biofilm formation is almost completely removed. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000548391 – 237Cyclic-di-GMP-binding biofilm dispersal mediator proteinAdd BLAST237

Proteomic databases

PaxDbiP39333
PRIDEiP39333

Expressioni

Inductioni

Expression is time dependent in biofilms and is controlled by BdcR.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4259560, 12 interactors
DIPiDIP-12604N
IntActiP39333, 2 interactors
STRINGi316385.ECDH10B_4443

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Beta strandi8 – 13Combined sources6
Helixi17 – 28Combined sources12
Beta strandi32 – 39Combined sources8
Helixi41 – 51Combined sources11
Beta strandi54 – 57Combined sources4
Helixi63 – 72Combined sources10
Beta strandi77 – 81Combined sources5
Helixi91 – 93Combined sources3
Helixi96 – 106Combined sources11
Helixi108 – 120Combined sources13
Beta strandi126 – 130Combined sources5
Helixi133 – 135Combined sources3
Helixi144 – 164Combined sources21
Helixi165 – 167Combined sources3
Beta strandi170 – 176Combined sources7
Helixi191 – 196Combined sources6
Beta strandi198 – 200Combined sources3
Helixi206 – 216Combined sources11
Helixi219 – 221Combined sources3
Beta strandi228 – 235Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5Z2LX-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-237[»]
ProteinModelPortaliP39333
SMRiP39333
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105F6U Bacteria
COG1028 LUCA
InParanoidiP39333
KOiK19336
OMAiTAPFIAM
PhylomeDBiP39333

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

P39333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAFTGKTVL ILGGSRGIGA AIVRRFVTDG ANVRFTYAGS KDAAKRLAQE
60 70 80 90 100
TGATAVFTDS ADRDAVIDVV RKSGALDILV VNAGIGVFGE ALELNADDID
110 120 130 140 150
RLFKINIHAP YHASVEAARQ MPEGGRILII GSVNGDRMPV AGMAAYAASK
160 170 180 190 200
SALQGMARGL ARDFGPRGIT INVVQPGPID TDANPANGPM RDMLHSLMAI
210 220 230
KRHGQPEEVA GMVAWLAGPE ASFVTGAMHT IDGAFGA
Length:237
Mass (Da):24,598
Last modified:July 15, 1998 - v2
Checksum:iA99A3F23CE0116C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA Translation: AAA97146.1 Sequence problems.
U00096 Genomic DNA Translation: AAC77206.1
AP009048 Genomic DNA Translation: BAE78247.1
PIRiD65237
RefSeqiNP_418670.1, NC_000913.3
WP_000500727.1, NZ_CP014272.1

Genome annotation databases

EnsemblBacteriaiAAC77206; AAC77206; b4249
BAE78247; BAE78247; BAE78247
GeneIDi948765
KEGGiecj:JW4207
eco:b4249
PATRICifig|511145.12.peg.4380

Similar proteinsi

Entry informationi

Entry nameiBDCA_ECOLI
AccessioniPrimary (citable) accession number: P39333
Secondary accession number(s): Q2M659
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: May 23, 2018
This is version 122 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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