ID YDIV_ECOLI Reviewed; 237 AA. AC P76204; Q2MB51; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 154. DE RecName: Full=Putative anti-FlhC(2)FlhD(4) factor YdiV; DE AltName: Full=c-di-GMP regulator CdgR; GN Name=ydiV; Synonyms=cdgR; OrderedLocusNames=b1707, JW1697; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP INDUCTION, AND RPOS-DEPENDENCE. RC STRAIN=K12 / MC4100; RX PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x; RA Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.; RT "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia RT coli."; RL Mol. Microbiol. 62:1014-1034(2006). RN [4] RP INDUCTION BY AI-1 IN AN SDIA-DEPENDENT FASHION, REPRESSION BY GLUCOSE, AND RP DISRUPTION PHENOTYPE. RC STRAIN=K12 / W3110 / ZK126; RX PubMed=18560382; DOI=10.1038/cr.2008.67; RA Zhou X., Meng X., Sun B.; RT "An EAL domain protein and cyclic AMP contribute to the interaction between RT the two quorum sensing systems in Escherichia coli."; RL Cell Res. 18:937-948(2008). RN [5] RP POSSIBLE FUNCTION, INTERACTION WITH FLHC(2)FLHD(4), INDUCTION, AND RP DISRUPTION PHENOTYPE. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=22461489; DOI=10.1099/mic.0.056036-0; RA Wada T., Hatamoto Y., Kutsukake K.; RT "Functional and expressional analyses of the anti-FlhD4C2 factor gene ydiV RT in Escherichia coli."; RL Microbiology 158:1533-1542(2012). CC -!- FUNCTION: Upon overexpression acts as a novel anti-FlhC(2)FlhD(4) CC factor, decreasing its DNA-binding activity, able to negatively CC regulate expression of flagellar class II operons including FliC. CC -!- INDUCTION: Induced by extracellular autoinducer AI-1 (Vibrio fischeri CC autoinducer oxoC6), in an SdiA-dependent fashion. Repressed by glucose. CC Induced at pH 5.0 in an RpoS-dependent fashion. Very poorly expressed CC in both rich and nutrient-poor medium due to inefficient translation CC (at protein level). {ECO:0000269|PubMed:17010156, CC ECO:0000269|PubMed:18560382, ECO:0000269|PubMed:22461489}. CC -!- DISRUPTION PHENOTYPE: A double sdiA/ydiV deletion mutant leads to CC decreased cAMP levels which inhibits quorum sensing system 2. Repressed CC by glucose. Unlike the case in Salmonella typhimurium, disruption has CC no effect on motility or FliC levels. {ECO:0000269|PubMed:18560382, CC ECO:0000269|PubMed:22461489}. CC -!- SIMILARITY: Belongs to the YdiV family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00096; AAC74777.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76505.1; -; Genomic_DNA. DR PIR; C64929; C64929. DR RefSeq; NP_416222.1; NC_000913.3. DR RefSeq; WP_001300634.1; NZ_CP009789.1. DR PDB; 3TLQ; X-ray; 1.91 A; A/B=1-237. DR PDB; 4ES4; X-ray; 2.90 A; A/C/E/G=1-237. DR AlphaFoldDB; P76204; -. DR SMR; P76204; -. DR BioGRID; 4260299; 14. DR DIP; DIP-11763N; -. DR FunCoup; P76204; 15. DR IntAct; P76204; 5. DR STRING; 511145.b1707; -. DR PaxDb; 511145-b1707; -. DR EnsemblBacteria; AAC74777; AAC74777; b1707. DR GeneID; 93775870; -. DR GeneID; 946217; -. DR KEGG; ecj:JW1697; -. DR KEGG; eco:b1707; -. DR KEGG; ecoc:C3026_09775; -. DR PATRIC; fig|1411691.4.peg.550; -. DR EchoBASE; EB3738; -. DR eggNOG; COG2200; Bacteria. DR HOGENOM; CLU_089254_1_1_6; -. DR InParanoid; P76204; -. DR OMA; LSFEPFM; -. DR OrthoDB; 8552213at2; -. DR PhylomeDB; P76204; -. DR BioCyc; EcoCyc:G6925-MONOMER; -. DR EvolutionaryTrace; P76204; -. DR PRO; PR:P76204; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IBA:GO_Central. DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IMP:EcoCyc. DR GO; GO:1900190; P:regulation of single-species biofilm formation; IBA:GO_Central. DR FunFam; 3.20.20.450:FF:000005; Cyclic di-GMP regulator CdgR; 1. DR Gene3D; 3.20.20.450; EAL domain; 1. DR InterPro; IPR001633; EAL_dom. DR InterPro; IPR035919; EAL_sf. DR PANTHER; PTHR33121:SF69; ANTI-FLHC(2)FLHD(4) FACTOR YDIV-RELATED; 1. DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1. DR Pfam; PF00563; EAL; 1. DR SUPFAM; SSF141868; EAL domain-like; 1. DR PDBsum; 3TLQ; -. DR PDBsum; 4ES4; -. PE 1: Evidence at protein level; KW 3D-structure; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1..237 FT /note="Putative anti-FlhC(2)FlhD(4) factor YdiV" FT /id="PRO_0000168997" FT DOMAIN 1..237 FT /note="EAL" FT TURN 4..8 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 9..19 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 25..36 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 54..70 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 88..96 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 121..126 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 128..136 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 179..189 FT /evidence="ECO:0007829|PDB:3TLQ" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 204..210 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:3TLQ" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:3TLQ" FT HELIX 228..234 FT /evidence="ECO:0007829|PDB:3TLQ" SQ SEQUENCE 237 AA; 27046 MW; 5684FCD246D7C16F CRC64; MKIFLENLYH SDCYFLPIRD NQQVLVGVEL ITHFSSEDGT VRIPTSRVIA QLTEEQHWQL FSEQLELLKS CQHFFIQHKL FAWLNLTPQV ATLLLERDNY AGELLKYPFI ELLINENYPH LNEGKDNRGL LSLSQVYPLV LGNLGAGNST MKAVFDGLFT RVMLDKSFIQ QQITHRSFEP FIRAIQAQIS PCCNCIIAGG IDTAEILAQI TPFDFHALQG CLWPAVPINQ ITTLVQR //