CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010246
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative cyclic-di-GMP phosphodiesterase AdrB 
Protein Synonyms/Alias
  
Gene Name
 adrB 
Gene Synonyms/Alias
 yoaD; b1815; JW1804 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
438TLRPDVLKIDKSFTAacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 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. 
Sequence Annotation
 DOMAIN 266 515 EAL.  
Keyword
 c-di-GMP; Complete proteome; Hydrolase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 532 AA 
Protein Sequence
MQKAQRIIKT YRRNRMIVCT ICALVTLAST LSVRFISQRN LNQQRVVQFA NHAVEELDKV 60
LLPLQAGSEV LLPLIGLPCS VAHLPLRKQA AKLQTVRSIG LVQDGTLYCS SIFGYRNVPV 120
VDILAELPAP QPLLRLTIDR ALIKGSPVLI QWTPAAGSSN AGVMEMINID LLTAMLLEPQ 180
LPQISSASLT VDKRHLLYGN GLVDSLPQPE DNENYQVSSQ RFPFTINVNG PGATALAWHY 240
LPTQLPLAVL LSLLVGYIAW LATAYRMSFS REINLGLAQH EFELFCQPLL NARSQQCIGV 300
EILLRWNNPR QGWISPDVFI PIAEEHHLIV PLTRYVMAET IRQRHVFPMS SQFHVGINVA 360
PSHFRRGVLI KDLNQYWFSA HPIQQLILEI TERDALLDVD YRIARELHRK NVKLAIDDFG 420
TGNSSFSWLE TLRPDVLKID KSFTAAIGSD AVNSTVTDII IALGQRLNIE LVAEGVETQE 480
QAKYLRRHGV HILQGYLYAQ PMPLRDFPKW LAGSQPPPAR HNGHITPIMP LR 532 
Gene Ontology
 GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:EC.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. 
Interpro
 IPR024744; CSS-motif_dom.
 IPR001633; Diguanylate_PEstase_EAL_dom. 
Pfam
 PF12792; CSS-motif
 PF00563; EAL 
SMART
 SM00052; EAL 
PROSITE
 PS50883; EAL 
PRINTS