PDEH_ECOLI
ID PDEH_ECOLI Reviewed; 255 AA.
AC P37646; Q2M7I7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cyclic di-GMP phosphodiesterase PdeH {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000269|PubMed:18765794};
GN Name=pdeH {ECO:0000303|PubMed:26148715}; Synonyms=yhjH;
GN OrderedLocusNames=b3525, JW3493;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP SEQUENCE REVISION.
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 INDUCTION, AND MEMBER OF THE FLAGELLAR REGULON.
RC STRAIN=K12;
RX PubMed=11031114; DOI=10.1006/jmbi.2000.4147;
RA Ko M., Park C.;
RT "Two novel flagellar components and H-NS are involved in the motor function
RT of Escherichia coli.";
RL J. Mol. Biol. 303:371-382(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-48, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18765794; DOI=10.1101/gad.475808;
RA Pesavento C., Becker G., Sommerfeldt N., Possling A., Tschowri N.,
RA Mehlis A., Hengge R.;
RT "Inverse regulatory coordination of motility and curli-mediated adhesion in
RT Escherichia coli.";
RL Genes Dev. 22:2434-2446(2008).
RN [6]
RP C-DI-GMP-BINDING.
RC STRAIN=K12 / MC4100;
RX PubMed=19240136; DOI=10.1101/gad.499409;
RA Tschowri N., Busse S., Hengge R.;
RT "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light
RT response of Escherichia coli.";
RL Genes Dev. 23:522-534(2009).
RN [7]
RP INDUCTION, RPOS-REPRESSION, AND DISRUPTION PHENOTYPE.
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 [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20303158; DOI=10.1016/j.cell.2010.01.018;
RA Boehm A., Kaiser M., Li H., Spangler C., Kasper C.A., Ackermann M.,
RA Kaever V., Sourjik V., Roth V., Jenal U.;
RT "Second messenger-mediated adjustment of bacterial swimming velocity.";
RL Cell 141:107-116(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / RP3098;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [10]
RP FUNCTION.
RX PubMed=23708798; DOI=10.1038/emboj.2013.120;
RA Lindenberg S., Klauck G., Pesavento C., Klauck E., Hengge R.;
RT "The EAL domain protein YciR acts as a trigger enzyme in a c-di-GMP
RT signalling cascade in E. coli biofilm control.";
RL EMBO J. 32:2001-2014(2013).
RN [11]
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: Involved in the control of the switch from cell motility to
CC adhesion via regulation of cellular levels of cyclic-di-GMP (c-di-GMP)
CC (PubMed:18765794). Part of a signaling cascade that regulates curli
CC biosynthesis. The cascade is composed of two c-di-GMP control modules,
CC in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates
CC the activity of the DgcM/PdeR pair (module II), which in turn regulates
CC activity of the transcription factor MlrA and expression of the master
CC biofilm regulator csgD (PubMed:23708798). Effect on flagella is
CC controlled via the c-di-GMP-binding flagellar brake protein YcgR
CC (PubMed:18765794). {ECO:0000269|PubMed:18765794,
CC ECO:0000269|PubMed:23708798}.
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:0000269|PubMed:18765794};
CC -!- INDUCTION: A class 3 flagellar gene, it is dependent on the master
CC transcriptional regulators FlhC and FlhD, and then FliA for expression.
CC Induced in early post-exponential phase at both 28 and 37 degrees
CC Celsius, it shuts down later than class 1 and class 2 operon genes.
CC Expression has to be shut down for adhesive curli fimbriae to be
CC induced, i.e. on solid medium where biofilms form. Repressed by RpoS.
CC {ECO:0000269|PubMed:11031114, ECO:0000269|PubMed:18765794,
CC ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Disruption leads to increased expression of
CC adhesive curli fimbriae genes (PubMed:18765794), including CsgD
CC (PubMed:19332833). Also leads to a severe reduction in swarm size and
CC swimming velocity, and 80% reduced concentrations of c-di-GMP.
CC Disruption of ycgR, or concomitant disruption of dosC, dgcE, dgcQ and
CC dgcN completely restores motility, suggesting these 4 genes, together
CC with this c-di-GMP phosphodiesterase, form a network that regulates
CC cell motility by altering levels of c-di-GMP (PubMed:20303158).
CC Overlapping but different results were seen by another group, where
CC disruption of dgcJ, another probable diguanylate cyclase, partially
CC suppresses the pdeH disruption, full suppression requires concomitant
CC disruption of dgcJ, dgcQ and dgcE (PubMed:18765794).
CC {ECO:0000269|PubMed:18765794, ECO:0000269|PubMed:19332833,
CC ECO:0000269|PubMed:20303158, ECO:0000269|PubMed:20346719}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18502.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18502.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76550.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77769.1; -; Genomic_DNA.
DR PIR; H65150; H65150.
DR RefSeq; NP_417982.2; NC_000913.3.
DR RefSeq; WP_001295219.1; NZ_SSZK01000039.1.
DR AlphaFoldDB; P37646; -.
DR SMR; P37646; -.
DR BioGRID; 4262527; 12.
DR IntAct; P37646; 2.
DR STRING; 511145.b3525; -.
DR PaxDb; P37646; -.
DR PRIDE; P37646; -.
DR EnsemblBacteria; AAC76550; AAC76550; b3525.
DR EnsemblBacteria; BAE77769; BAE77769; BAE77769.
DR GeneID; 66672590; -.
DR GeneID; 948042; -.
DR KEGG; ecj:JW3493; -.
DR KEGG; eco:b3525; -.
DR PATRIC; fig|511145.12.peg.3634; -.
DR EchoBASE; EB2162; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_089254_0_0_6; -.
DR InParanoid; P37646; -.
DR OMA; CGMANFS; -.
DR PhylomeDB; P37646; -.
DR BioCyc; EcoCyc:EG12252-MON; -.
DR BioCyc; MetaCyc:EG12252-MON; -.
DR PRO; PR:P37646; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
DR PROSITE; PS50883; EAL; 1.
PE 1: Evidence at protein level;
KW c-di-GMP; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..255
FT /note="Cyclic di-GMP phosphodiesterase PdeH"
FT /id="PRO_0000169573"
FT DOMAIN 13..255
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT MUTAGEN 48
FT /note="E->A: Loss of c-di-GMP phosphodiesterase activity."
FT /evidence="ECO:0000269|PubMed:18765794"
SQ SEQUENCE 255 AA; 29601 MW; F91C1893C8F1B508 CRC64;
MIRQVIQRIS NPEASIESLQ ERRFWLQCER AYTWQPIYQT CGRLMAVELL TVVTHPLNPS
QRLPPDRYFT EITVSHRMEV VKEQIDLLAQ KADFFIEHGL LASVNIDGPT LIALRQQPKI
LRQIERLPWL RFELVEHIRL PKDSTFASMC EFGPLWLDDF GTGMANFSAL SEVRYDYIKI
ARELFVMLRQ SPEGRTLFSQ LLHLMNRYCR GVIVEGVETP EEWRDVQNSP AFAAQGWFLS
RPAPIETLNT AVLAL
