Tag | Content |
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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 |
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438 | TLRPDVLKIDKSFTA | acetylation | [1] |
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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. |
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