PDED_ECOLI
ID PDED_ECOLI Reviewed; 532 AA.
AC P76261; P97188; P97189;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeD {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN Name=pdeD {ECO:0000303|PubMed:26148715}; Synonyms=adrB, yoaD;
GN OrderedLocusNames=b1815, JW1804;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
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 [3]
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 [4]
RP REGULATION BY CSGD, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / PHL565;
RX PubMed=16513732; DOI=10.1128/jb.188.6.2027-2037.2006;
RA Brombacher E., Baratto A., Dorel C., Landini P.;
RT "Gene expression regulation by the Curli activator CsgD protein: modulation
RT of cellulose biosynthesis and control of negative determinants for
RT microbial adhesion.";
RL J. Bacteriol. 188:2027-2037(2006).
RN [5]
RP INDUCTION, AND RPOS-DEPENDENCE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [6]
RP NOMENCLATURE.
RX PubMed=26148715; DOI=10.1128/jb.00424-15;
RA Hengge R., Galperin M.Y., Ghigo J.M., Gomelsky M., Green J., Hughes K.T.,
RA Jenal U., Landini P.;
RT "Systematic nomenclature for GGDEF and EAL domain-containing cyclic di-GMP
RT turnover proteins of Escherichia coli.";
RL J. Bacteriol. 198:7-11(2015).
CC -!- FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of
CC cyclic-di-GMP (c-di-GMP) to 5'-pGpG (By similarity). May serve as a
CC negative regulator of cellulose synthesis (as has been suggested for
CC S.typhimurium); overexpression inhibits cell aggregation in strains
CC able to produce adhesive curli fimbriae. Cyclic-di-GMP is a second
CC messenger which controls cell surface-associated traits in bacteria
CC (PubMed:16513732). {ECO:0000250|UniProtKB:P21514,
CC ECO:0000269|PubMed:16513732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclic di-3',5'-guanylate + H2O = 5'-
CC phosphoguanylyl(3'->5')guanosine + H(+); Xref=Rhea:RHEA:24902,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58754,
CC ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000250|UniProtKB:P21514};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed at 28 degrees Celsius in late stationary phase,
CC constitutively expressed at low levels at 37 degrees Celsius, more
CC highly expressed on plates than in liquid medium. Expression is
CC RpoS- and CsgD-dependent. {ECO:0000269|PubMed:16513732,
CC ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show increased
CC aggregation, increased cellulose production but no increase in surface
CC attachment. {ECO:0000269|PubMed:16513732}.
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DR EMBL; U00096; AAC74885.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15622.1; -; Genomic_DNA.
DR PIR; G64942; G64942.
DR RefSeq; NP_416329.4; NC_000913.3.
DR RefSeq; WP_001295494.1; NZ_SSUW01000012.1.
DR AlphaFoldDB; P76261; -.
DR SMR; P76261; -.
DR BioGRID; 4260346; 6.
DR IntAct; P76261; 1.
DR STRING; 511145.b1815; -.
DR PaxDb; P76261; -.
DR PRIDE; P76261; -.
DR EnsemblBacteria; AAC74885; AAC74885; b1815.
DR EnsemblBacteria; BAA15622; BAA15622; BAA15622.
DR GeneID; 66674296; -.
DR GeneID; 946336; -.
DR KEGG; ecj:JW1804; -.
DR KEGG; eco:b1815; -.
DR PATRIC; fig|511145.12.peg.1892; -.
DR EchoBASE; EB3289; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_000445_131_2_6; -.
DR InParanoid; P76261; -.
DR OMA; IRFISQR; -.
DR PhylomeDB; P76261; -.
DR BioCyc; EcoCyc:G6996-MON; -.
DR PRO; PR:P76261; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; -; 1.
DR InterPro; IPR024744; CSS-motif_dom.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR Pfam; PF12792; CSS-motif; 1.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
DR PROSITE; PS50883; EAL; 1.
PE 2: Evidence at transcript level;
KW c-di-GMP; Cell membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Probable cyclic di-GMP phosphodiesterase PdeD"
FT /id="PRO_0000169033"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 266..515
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 532 AA; 59711 MW; 977155A7D56C18C7 CRC64;
MQKAQRIIKT YRRNRMIVCT ICALVTLAST LSVRFISQRN LNQQRVVQFA NHAVEELDKV
LLPLQAGSEV LLPLIGLPCS VAHLPLRKQA AKLQTVRSIG LVQDGTLYCS SIFGYRNVPV
VDILAELPAP QPLLRLTIDR ALIKGSPVLI QWTPAAGSSN AGVMEMINID LLTAMLLEPQ
LPQISSASLT VDKRHLLYGN GLVDSLPQPE DNENYQVSSQ RFPFTINVNG PGATALAWHY
LPTQLPLAVL LSLLVGYIAW LATAYRMSFS REINLGLAQH EFELFCQPLL NARSQQCIGV
EILLRWNNPR QGWISPDVFI PIAEEHHLIV PLTRYVMAET IRQRHVFPMS SQFHVGINVA
PSHFRRGVLI KDLNQYWFSA HPIQQLILEI TERDALLDVD YRIARELHRK NVKLAIDDFG
TGNSSFSWLE TLRPDVLKID KSFTAAIGSD AVNSTVTDII IALGQRLNIE LVAEGVETQE
QAKYLRRHGV HILQGYLYAQ PMPLRDFPKW LAGSQPPPAR HNGHITPIMP LR
