ID   PDEI_ECOLI              Reviewed;         782 AA.
AC   P75800;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeI {ECO:0000305};
DE            EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN   Name=pdeI {ECO:0000303|PubMed:26148715}; Synonyms=yliE;
GN   OrderedLocusNames=b0833, JW0817;
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   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   [5]
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   [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). Overexpression
CC       reduces biofilm formation. Cyclic-di-GMP is a second messenger which
CC       controls cell surface-associated traits in bacteria (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 membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a weak reduction in
CC       swarm size. {ECO:0000269|PubMed:20303158}.
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DR   EMBL; U00096; AAC73920.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35528.1; -; Genomic_DNA.
DR   PIR; A64821; A64821.
DR   RefSeq; NP_415354.1; NC_000913.3.
DR   RefSeq; WP_001360263.1; NZ_LN832404.1.
DR   AlphaFoldDB; P75800; -.
DR   SMR; P75800; -.
DR   BioGRID; 4259986; 11.
DR   STRING; 511145.b0833; -.
DR   jPOST; P75800; -.
DR   PaxDb; P75800; -.
DR   PRIDE; P75800; -.
DR   EnsemblBacteria; AAC73920; AAC73920; b0833.
DR   EnsemblBacteria; BAA35528; BAA35528; BAA35528.
DR   GeneID; 945462; -.
DR   KEGG; ecj:JW0817; -.
DR   KEGG; eco:b0833; -.
DR   PATRIC; fig|1411691.4.peg.1445; -.
DR   EchoBASE; EB3249; -.
DR   eggNOG; COG2200; Bacteria.
DR   HOGENOM; CLU_000445_78_2_6; -.
DR   OMA; EMNPDSI; -.
DR   PhylomeDB; P75800; -.
DR   BioCyc; EcoCyc:G6433-MON; -.
DR   PRO; PR:P75800; -.
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   CDD; cd01948; EAL; 1.
DR   Gene3D; 3.20.20.450; -; 1.
DR   InterPro; IPR033418; CHASE9.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   Pfam; PF17153; CHASE9; 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..782
FT                   /note="Probable cyclic di-GMP phosphodiesterase PdeI"
FT                   /id="PRO_0000168729"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          527..781
FT                   /note="EAL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ   SEQUENCE   782 AA;  90049 MW;  608DFB0068611DFB CRC64;
     MLSLYEKIKI RLIILFLLAA LSFIGLFFII NYQLVSERAV KRADSRFELI QKNVGYFFKD
     IERSALTLKD SLYLLKNTEE IQRAVILKME MMPFLDSVGL VLDDNKYYLF SRRANDKIVV
     YHQEQVNGPL VDESGRVIFA DFNPSKRPWS VASDDSNNSW NPAYNCFDRP GKKCISFTLH
     INGKDHDLLA VDKIHVDLNW RYLNEYLDQI SANDEVLFLK QGHEIIAKNQ LAREKLIIYN
     SEGNYNIIDS VDTEYIEKTS AVPNNALFEI YFYYPGGNLL NASDKLFYLP FAFIIIVLLV
     VYLMTTRVFR RQFSEMTELV NTLAFLPDST DQIEALKIRE GDAKEIISIK NSIAEMKDAE
     IERSNKLLSL ISYDQESGFI KNMAIIESNN NQYLAVGIIK LCGLEAVEAV FGVDERNKIV
     RKLCQRIAEK YAQCCDIVTF NADLYLLLCR ENVQTFTRKI AMVNDFDSSF GYRNLRIHKS
     AICEPLQGEN AWSYAEKLKL AISSIRDHMF SEFIFCDDAK LNEIEENIWI ARNIRHAMEI
     GELFLVYQPI VDINTRAILG AEALCRWVSA ERGIISPLKF ITIAEDIGFI NELGYQIIKT
     AMGEFRHFSQ RASLKDDFLL HINVSPWQLN EPHFHERFTT IMKENGLKAN SLCVEITETV
     IERINEHFYL NIEQLRKQGV RISIDDFGTG LSNLKRFYEI NPDSIKVDSQ FTGDIFGTAG
     KIVRIIFDLA RYNRIPVIAE GVESEDVARE LIKLGCVQAQ GYLYQKPMPF SAWDKSGKLV
     KE