PDEC_ECOLI
ID PDEC_ECOLI Reviewed; 528 AA.
AC P32701; P76789; Q2M6P3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeC {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN Name=pdeC {ECO:0000303|PubMed:26148715}; Synonyms=yjcC;
GN OrderedLocusNames=b4061, JW4022;
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=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 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 [5]
RP FUNCTION IN BIOFILM FORMATION.
RC STRAIN=K12 / AB400;
RX PubMed=19460094; DOI=10.1111/j.1365-2958.2009.06739.x;
RA Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D.,
RA Keck W., Ackermann M., Schirmer T., Jenal U.;
RT "Second messenger signalling governs Escherichia coli biofilm induction
RT upon ribosomal stress.";
RL Mol. Microbiol. 72:1500-1516(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). Cyclic-di-GMP is a
CC second messenger which controls cell surface-associated traits in
CC bacteria. Overexpression reduces biofilm formation (PubMed:19460094).
CC {ECO:0000250|UniProtKB:P21514, ECO:0000269|PubMed:19460094}.
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 inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed during transition into stationary phase, at both
CC 28 and 37 degrees Celsius. Expression is RpoS dependent.
CC {ECO:0000269|PubMed:19332833}.
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DR EMBL; U00006; AAC43155.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77031.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78063.1; -; Genomic_DNA.
DR PIR; D65214; D65214.
DR RefSeq; NP_418485.1; NC_000913.3.
DR RefSeq; WP_000019548.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P32701; -.
DR SMR; P32701; -.
DR BioGRID; 4260840; 7.
DR DIP; DIP-12548N; -.
DR IntAct; P32701; 6.
DR STRING; 511145.b4061; -.
DR PaxDb; P32701; -.
DR PRIDE; P32701; -.
DR EnsemblBacteria; AAC77031; AAC77031; b4061.
DR EnsemblBacteria; BAE78063; BAE78063; BAE78063.
DR GeneID; 948568; -.
DR KEGG; ecj:JW4022; -.
DR KEGG; eco:b4061; -.
DR PATRIC; fig|511145.12.peg.4182; -.
DR EchoBASE; EB1882; -.
DR eggNOG; COG4943; Bacteria.
DR HOGENOM; CLU_000445_131_1_6; -.
DR InParanoid; P32701; -.
DR OMA; RLIAHFY; -.
DR PhylomeDB; P32701; -.
DR BioCyc; EcoCyc:EG11938-MON; -.
DR BioCyc; MetaCyc:EG11938-MON; -.
DR BRENDA; 3.1.4.52; 2026.
DR PRO; PR:P32701; -.
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; IDA:EcoCyc.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW c-di-GMP; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..528
FT /note="Probable cyclic di-GMP phosphodiesterase PdeC"
FT /id="PRO_0000169719"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 268..520
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 528 AA; 60801 MW; F6E4819954912F31 CRC64;
MSHRARHQLL ALPGIIFLVL FPIILSLWIA FLWAKSEVNN QLRTFAQLAL DKSELVIRQA
DLVSDAAERY QGQVCTPAHQ KRMLNIIRGY LYINELIYAR DNHFLCSSLI APVNGYTIAP
ADYKREPNVS IYYYRDTPFF SGYKMTYMQR GNYVAVINPL FWSEVMSDDP TLQWGVYDTV
TKTFFSLSKE ASAATFSPLI HLKDLTVQRN GYLYATVYST KRPIAAIVAT SYQRLITHFY
NHLIFALPAG ILGSLVLLLL WLRIRQNYLS PKRKLQRALE KHQLCLYYQP IIDIKTEKCI
GAEALLRWPG EQGQIMNPAE FIPLAEKEGM IEQITDYVID NVFRDLGDYL ATHADRYVSI
NLSASDFHTS RLIARINQKT EQYAVRPQQI KFEVTEHAFL DVDKMTPIIL AFRQAGYEVA
IDDFGIGYSN LHNLKSLNVD ILKIDKSFVE TLTTHKTSHL IAEHIIELAH SLGLKTIAEG
VETEEQVNWL RKRGVRYCQG WFFAKAMPPQ VFMQWMEQLP ARELTRGQ
