PDEG_ECOLI
ID PDEG_ECOLI Reviewed; 507 AA.
AC P75995;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeG {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN Name=pdeG {ECO:0000303|PubMed:26148715}; Synonyms=ycgG;
GN OrderedLocusNames=b1168, JW5174;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16139413; DOI=10.1016/j.biochi.2005.07.012;
RA Regonesi M.E., Del Favero M., Basilico F., Briani F., Benazzi L.,
RA Tortora P., Mauri P., Deho G.;
RT "Analysis of the Escherichia coli RNA degradosome composition by a
RT proteomic approach.";
RL Biochimie 88:151-161(2006).
RN [5]
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 [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. {ECO:0000250|UniProtKB:P21514}.
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}. Note=Found associated with the RNA degradosome.
CC {ECO:0000269|PubMed:16139413}.
CC -!- INDUCTION: Induced by 0.3 M NaCl in an RpoS-dependent fashion.
CC {ECO:0000269|PubMed:17010156}.
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DR EMBL; U00096; AAC74252.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36000.2; -; Genomic_DNA.
DR PIR; E64862; E64862.
DR RefSeq; NP_415686.2; NC_000913.3.
DR RefSeq; WP_001246499.1; NZ_LN832404.1.
DR AlphaFoldDB; P75995; -.
DR SMR; P75995; -.
DR BioGRID; 4261455; 14.
DR DIP; DIP-11554N; -.
DR IntAct; P75995; 1.
DR STRING; 511145.b1168; -.
DR PaxDb; P75995; -.
DR PRIDE; P75995; -.
DR EnsemblBacteria; AAC74252; AAC74252; b1168.
DR EnsemblBacteria; BAA36000; BAA36000; BAA36000.
DR GeneID; 945738; -.
DR KEGG; ecj:JW5174; -.
DR KEGG; eco:b1168; -.
DR PATRIC; fig|1411691.4.peg.1123; -.
DR EchoBASE; EB3647; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_000445_131_0_6; -.
DR InParanoid; P75995; -.
DR OMA; DKQMRNT; -.
DR PhylomeDB; P75995; -.
DR BioCyc; EcoCyc:G6608-MON; -.
DR PRO; PR:P75995; -.
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; IEA:UniProtKB-EC.
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 membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Probable cyclic di-GMP phosphodiesterase PdeG"
FT /id="PRO_0000168853"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 246..500
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 507 AA; 56906 MW; D144600B361285D8 CRC64;
MRNTLIPILV AICLFITGVA ILNIQLWYSA KAEYLAGARY AANNINHILE EASQATQTAV
NIAGKECNLE EQYQLGTEAA LKPHLRTIII LKQGIVWCTS LPGNRVLLSR IPVFPDSNLL
LAPAIDTVNR LPILLYQNQF ADTRILVTIS DQHIRGALNV PLKGVRYVLR VADDIIGPTG
DVMTLNGHYP YTEKVHSTKY HFTIIFNPPP LFSFYRLIDK GFGILIFILL IACAAAFLLD
RYFNKSATPE EILRRAINNG EIVPFYQPVV NGREGTLRGV EVLARWKQPH GGYISPAAFI
PLAEKSGLIV PLTQSLMNQV ARQMNAIASK LPEGFHIGIN FSASHIISPT FVDECLNFRD
SFTRRDLNLV LEVTEREPLN VDESLVQRLN ILHENGFVIA LDDFGTGYSG LSYLHDLHID
YIKIDHSFVG RVNADPESTR ILDCVLDLAR KLSISIVAEG VETKEQLDYL NQNYITFQQG
YYFYKPVTYI DLVKIILSKP KVKVVVE
