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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
 
 
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