YDIV_ECOLI
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 03-AUG-2022, entry version 136.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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_STEB01000009.1.
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 PDBsum; 3TLQ; -.
DR PDBsum; 4ES4; -.
DR AlphaFoldDB; P76204; -.
DR SMR; P76204; -.
DR BioGRID; 4260299; 10.
DR DIP; DIP-11763N; -.
DR IntAct; P76204; 5.
DR STRING; 511145.b1707; -.
DR PaxDb; P76204; -.
DR PRIDE; P76204; -.
DR EnsemblBacteria; AAC74777; AAC74777; b1707.
DR EnsemblBacteria; BAE76505; BAE76505; BAE76505.
DR GeneID; 946217; -.
DR KEGG; ecj:JW1697; -.
DR KEGG; eco:b1707; -.
DR PATRIC; fig|1411691.4.peg.550; -.
DR EchoBASE; EB3738; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_089254_1_1_6; -.
DR OMA; SFEPFMR; -.
DR PhylomeDB; P76204; -.
DR BioCyc; EcoCyc:G6925-MON; -.
DR PRO; PR:P76204; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:EcoCyc.
DR Gene3D; 3.20.20.450; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR Pfam; PF00563; EAL; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
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..101
FT /evidence="ECO:0007829|PDB:3TLQ"
FT HELIX 102..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
