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Protein

Putative cyclic-di-GMP phosphodiesterase AdrB

Gene

adrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May serve as a negative regulator of cellulose synthesis (as has been suggested for S.typhimurium); overexpression inhibits cell aggregation in strains able to produce adhesive curli fimbriae. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.

Catalytic activityi

Cyclic di-3',5'-guanylate + H2O = 5'-phosphoguanylyl(3'->5')guanosine.

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

c-di-GMP

Enzyme and pathway databases

BioCyciEcoCyc:G6996-MONOMER.
ECOL316407:JW1804-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative cyclic-di-GMP phosphodiesterase AdrB (EC:3.1.4.52)
Gene namesi
Name:adrB
Synonyms:yoaD
Ordered Locus Names:b1815, JW1804
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13516. adrB.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show increased aggregation, increased cellulose production but no increase in surface attachment.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Putative cyclic-di-GMP phosphodiesterase AdrBPRO_0000169033Add
BLAST

Proteomic databases

PaxDbiP76261.
PRIDEiP76261.

Expressioni

Inductioni

Expressed at 28 degrees Celsius in late stationary phase, constitutively expressed at low levels at 37 degrees Celsius, more highly expressed on plates than in liquid medium. Expression is RpoS- and CsgD-dependent.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4260346. 6 interactions.
IntActiP76261. 1 interaction.
STRINGi511145.b1815.

Structurei

3D structure databases

ProteinModelPortaliP76261.
SMRiP76261. Positions 273-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 515250EALPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EAL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107XTP. Bacteria.
COG2200. LUCA.
HOGENOMiHOG000273106.
InParanoidiP76261.
OMAiVYCQPII.
OrthoDBiEOG69GZGV.
PhylomeDBiP76261.

Family and domain databases

Gene3Di3.20.20.450. 1 hit.
InterProiIPR024744. CSS-motif_dom.
IPR001633. EAL_dom.
[Graphical view]
PfamiPF12792. CSS-motif. 1 hit.
PF00563. EAL. 1 hit.
[Graphical view]
SMARTiSM00052. EAL. 1 hit.
[Graphical view]
SUPFAMiSSF141868. SSF141868. 1 hit.
PROSITEiPS50883. EAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76261-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKAQRIIKT YRRNRMIVCT ICALVTLAST LSVRFISQRN LNQQRVVQFA
60 70 80 90 100
NHAVEELDKV LLPLQAGSEV LLPLIGLPCS VAHLPLRKQA AKLQTVRSIG
110 120 130 140 150
LVQDGTLYCS SIFGYRNVPV VDILAELPAP QPLLRLTIDR ALIKGSPVLI
160 170 180 190 200
QWTPAAGSSN AGVMEMINID LLTAMLLEPQ LPQISSASLT VDKRHLLYGN
210 220 230 240 250
GLVDSLPQPE DNENYQVSSQ RFPFTINVNG PGATALAWHY LPTQLPLAVL
260 270 280 290 300
LSLLVGYIAW LATAYRMSFS REINLGLAQH EFELFCQPLL NARSQQCIGV
310 320 330 340 350
EILLRWNNPR QGWISPDVFI PIAEEHHLIV PLTRYVMAET IRQRHVFPMS
360 370 380 390 400
SQFHVGINVA PSHFRRGVLI KDLNQYWFSA HPIQQLILEI TERDALLDVD
410 420 430 440 450
YRIARELHRK NVKLAIDDFG TGNSSFSWLE TLRPDVLKID KSFTAAIGSD
460 470 480 490 500
AVNSTVTDII IALGQRLNIE LVAEGVETQE QAKYLRRHGV HILQGYLYAQ
510 520 530
PMPLRDFPKW LAGSQPPPAR HNGHITPIMP LR
Length:532
Mass (Da):59,711
Last modified:April 27, 2001 - v2
Checksum:i977155A7D56C18C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74885.2.
AP009048 Genomic DNA. Translation: BAA15622.1.
PIRiG64942.
RefSeqiNP_416329.4. NC_000913.3.
WP_001295494.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74885; AAC74885; b1815.
BAA15622; BAA15622; BAA15622.
GeneIDi946336.
KEGGiecj:JW1804.
eco:b1815.
PATRICi32118949. VBIEscCol129921_1892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74885.2.
AP009048 Genomic DNA. Translation: BAA15622.1.
PIRiG64942.
RefSeqiNP_416329.4. NC_000913.3.
WP_001295494.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76261.
SMRiP76261. Positions 273-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260346. 6 interactions.
IntActiP76261. 1 interaction.
STRINGi511145.b1815.

Proteomic databases

PaxDbiP76261.
PRIDEiP76261.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74885; AAC74885; b1815.
BAA15622; BAA15622; BAA15622.
GeneIDi946336.
KEGGiecj:JW1804.
eco:b1815.
PATRICi32118949. VBIEscCol129921_1892.

Organism-specific databases

EchoBASEiEB3289.
EcoGeneiEG13516. adrB.

Phylogenomic databases

eggNOGiENOG4107XTP. Bacteria.
COG2200. LUCA.
HOGENOMiHOG000273106.
InParanoidiP76261.
OMAiVYCQPII.
OrthoDBiEOG69GZGV.
PhylomeDBiP76261.

Enzyme and pathway databases

BioCyciEcoCyc:G6996-MONOMER.
ECOL316407:JW1804-MONOMER.

Miscellaneous databases

PROiP76261.

Family and domain databases

Gene3Di3.20.20.450. 1 hit.
InterProiIPR024744. CSS-motif_dom.
IPR001633. EAL_dom.
[Graphical view]
PfamiPF12792. CSS-motif. 1 hit.
PF00563. EAL. 1 hit.
[Graphical view]
SMARTiSM00052. EAL. 1 hit.
[Graphical view]
SUPFAMiSSF141868. SSF141868. 1 hit.
PROSITEiPS50883. EAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion."
    Brombacher E., Baratto A., Dorel C., Landini P.
    J. Bacteriol. 188:2027-2037(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY CSGD, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / PHL565.
  5. "Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli."
    Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N., Hengge R.
    Microbiology 155:1318-1331(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, RPOS-DEPENDENCE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiADRB_ECOLI
AccessioniPrimary (citable) accession number: P76261
Secondary accession number(s): P97188, P97189
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: January 20, 2016
This is version 103 of the entry and version 2 of the sequence. [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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.