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PDEN_ECOLI
ID   PDEN_ECOLI              Reviewed;         518 AA.
AC   P76446; P77139; Q52613;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeN {ECO:0000305};
DE            EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN   Name=pdeN {ECO:0000303|PubMed:26148715}; Synonyms=rtn;
GN   OrderedLocusNames=b2176, JW2164;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kim C.S., Lee D.W., Chae K.-S., Hwang U.W.;
RT   "Structural analysis of an rtn gene isolated from Proteus vulgaris.";
RL   Mol. Cells 4:387-391(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-518, AND SHOWS THAT SEQUENCE
RP   DESCRIBED IN KIM ET AL ORIGINATES FROM E.COLI.
RC   STRAIN=K12 / MG1063;
RX   PubMed=9079933; DOI=10.1128/jb.179.7.2433-2434.1997;
RA   Hall B.G.;
RT   "The rtn gene of Proteus vulgaris is actually from Escherichia coli.";
RL   J. Bacteriol. 179:2433-2434(1997).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [7]
RP   INDUCTION, AND RPOS-REPRESSION.
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   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 inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expressed at both 28 and 37 degrees Celsius during
CC       exponential growth. Repressed by RpoS. {ECO:0000269|PubMed:19332833}.
CC   -!- CAUTION: Was originally (Ref.4) thought to originate from Proteus
CC       vulgaris, but was shown to originate from E.coli.
CC       {ECO:0000305|PubMed:9079933}.
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DR   EMBL; U00096; AAC75237.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15984.1; -; Genomic_DNA.
DR   EMBL; U12780; AAA50754.1; -; Genomic_DNA.
DR   EMBL; U83404; AAB51508.1; -; Genomic_DNA.
DR   PIR; G64986; G64986.
DR   RefSeq; NP_416681.1; NC_000913.3.
DR   RefSeq; WP_000470560.1; NZ_SSZK01000027.1.
DR   AlphaFoldDB; P76446; -.
DR   SMR; P76446; -.
DR   BioGRID; 4261095; 10.
DR   DIP; DIP-10813N; -.
DR   STRING; 511145.b2176; -.
DR   PaxDb; P76446; -.
DR   PRIDE; P76446; -.
DR   EnsemblBacteria; AAC75237; AAC75237; b2176.
DR   EnsemblBacteria; BAA15984; BAA15984; BAA15984.
DR   GeneID; 946695; -.
DR   KEGG; ecj:JW2164; -.
DR   KEGG; eco:b2176; -.
DR   PATRIC; fig|1411691.4.peg.60; -.
DR   EchoBASE; EB3830; -.
DR   eggNOG; COG2200; Bacteria.
DR   HOGENOM; CLU_000445_131_2_6; -.
DR   InParanoid; P76446; -.
DR   OMA; FLQGYWI; -.
DR   PhylomeDB; P76446; -.
DR   BioCyc; EcoCyc:G7148-MON; -.
DR   PRO; PR:P76446; -.
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   2: Evidence at transcript level;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Probable cyclic di-GMP phosphodiesterase PdeN"
FT                   /id="PRO_0000097517"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          261..514
FT                   /note="EAL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT   CONFLICT        482..518
FT                   /note="RWLSERGVNFMQGYWISRPLPLDDFVRWLKKPYTPQW -> D (in Ref.
FT                   4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   518 AA;  58588 MW;  BABA5768CBC47C41 CRC64;
     MFIRAPNFGR KLLLTCIVAG VMIAILVSCL QFLVAWHKHE VKYDTLITDV QKYLDTYFAD
     LKSTTDRLQP LTLDTCQQAN PELTARAAFS MNVRTFVLVK DKKTFCSSAT GEMDIPLNEL
     IPALDINKNV DMAILPGTPM VPNKPAIVIW YRNPLLKNSG VFAALNLNLT PSLFYSSRQE
     DYDGVALIIG NTALSTFSSR LMNVNELTDM PVRETKIAGI PLTVRLYADD WTWNDVWYAF
     LLGGMSGTVV GLLCYYLMSV RMRPGREIMT AIKREQFYVA YQPVVDTQAL RVTGLEVLLR
     WRHPVAGEIP PDAFINFAES QKMIVPLTQH LFELIARDAA ELEKVLPVGV KFGINIAPDH
     LHSESFKADI QKLLTSLPAH HFQIVLEITE RDMLKEQEAT QLFAWLHSVG VEIAIDDFGT
     GHSALIYLER FTLDYLKIDR GFINAIGTET ITSPVLDAVL TLAKRLNMLT VAEGVETPEQ
     ARWLSERGVN FMQGYWISRP LPLDDFVRWL KKPYTPQW
 
 
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