| Tag | Content |
|---|
| CPLM ID | CPLM-006843 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable diguanylate cyclase YegE |
Protein Synonyms/Alias | DGC |
Gene Name | yegE |
Gene Synonyms/Alias | b2067; JW2052 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 502 | LQSRSPFKLEFRITV | acetylation | [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 | Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. |
Sequence Annotation | DOMAIN 300 370 PAS 1.
DOMAIN 374 426 PAC 1.
DOMAIN 501 552 PAC 2.
DOMAIN 553 623 PAS 2.
DOMAIN 626 680 PAC 3.
DOMAIN 712 845 GGDEF.
DOMAIN 855 1104 EAL.
ACT_SITE 763 763 Proton acceptor (Potential).
METAL 720 720 Magnesium (By similarity).
METAL 763 763 Magnesium (By similarity).
BINDING 728 728 Substrate (By similarity).
BINDING 737 737 Substrate (By similarity). |
Keyword | Complete proteome; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1105 AA |
Protein Sequence | MSKQSQHVLI ALPHPLLHLV SLGLVSFIFT LFSLELSQFG TQLAPLWFPT SIMMVAFYRH 60
AGRMWPGIAL SCSLGNIAAS ILLFSTSSLN MTWTTINIVE AVVGAVLLRK LLPWYNPLQN 120
LADWLRLALG SAIVPPLLGG VLVVLLTPGD DPLRAFLIWV LSESIGALAL VPLGLLFKPH 180
YLLRHRNPRL LFESLLTLAI TLTLSWLSML YLPWPFTFII VLLMWSAVRL PRMEAFLIFL 240
TTVMMVSLMM AADPSLLATP RTYLMSHMPW LPFLLILLPA NIMTMVMYAF RAERKHISES 300
ETHFRNAMEY SAIGMALVGT EGQWLQTNKA LCQFLGYSQE ELRGLTFQQL TWPEDLNKDL 360
QQVEKLISGE INTYSMEKRY YNRNGDVVWA LLAVSLVRHT DGTPLYFIAQ IEDINELKRT 420
EQVNQQLMER ITLANEAGGI GIWEWELKPN IFSWDKRMFE LYEIPPHIKP NWQVWYECVL 480
PEDRQHAEKV IRDSLQSRSP FKLEFRITVK DGIRHIRALA NRVLNKEGEV ERLLGINMDM 540
TEVKQLNEAL FQEKERLHIT LDSIGEAVVC IDMAMKITFM NPVAEKMSGW TQEEALGVPL 600
LTVLHITFGD NGPLMENIYS ADTSRSAIEQ DVVLHCRSGG SYDVHYSITP LSTLDGSNIG 660
SVLVIQDVTE SRKMLRQLSY SASHDALTHL ANRASFEKQL RILLQTVNST HQRHALVFID 720
LDRFKAVNDS AGHAAGDALL RELASLMLSM LRSSDVLARL GGDEFGLLLP DCNVESARFI 780
ATRIISAVND YHFIWEGRVH RVGASAGITL IDDNNHQAAE VMSQADIACY ASKNGGRGRV 840
TVYEPQQAAA HSERAAMSLD EQWRMIKENQ LMMLAHGVAS PRIPEARNLW LISLKLWSCE 900
GEIIDEQTFR RSFSDPALSH ALDRRVFHEF FQQAAKAVAS KGISISLPLS VAGLSSATLV 960
NDLLEQLENS PLPPRLLHLI IPAEAILDHA ESVQKLRLAG CRIVLSQVGR DLQIFNSLKA 1020
NMADYLLLDG ELCANVQGNL MDEMLITIIQ GHAQRLGMKT IAGPVVLPLV MDTLSGIGVD 1080
LIYGEVIADA QPLDLLVNSS YFAIN 1105 |
Gene Ontology | GO:0052621; F:diguanylate cyclase activity; IGI:EcoCyc. GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro. GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0023014; P:signal transduction by phosphorylation; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |