PDEA_ECOLI
ID PDEA_ECOLI Reviewed; 729 AA.
AC P23842; P76529; P76954;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeA {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN Name=pdeA {ECO:0000303|PubMed:26148715}; Synonyms=yfeA;
GN OrderedLocusNames=b2395, JW5391;
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=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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] OF 1-153.
RC STRAIN=K12;
RX PubMed=2201776; DOI=10.1016/0022-2836(90)90339-n;
RA Brun Y.V., Breton R., Lanouette P., Lapointe J.;
RT "Precise mapping and comparison of two evolutionarily related regions of
RT the Escherichia coli K-12 chromosome. Evolution of valU and lysT from an
RT ancestral tRNA operon.";
RL J. Mol. Biol. 214:825-843(1990).
RN [5]
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 [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}.
CC -!- INDUCTION: Expressed during exponential and post-exponential growth at
CC both 28 and 37 degrees Celsius. Repressed by RpoS.
CC {ECO:0000269|PubMed:19332833}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65719.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA65719.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA45395.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA45395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75454.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16267.2; -; Genomic_DNA.
DR EMBL; M13687; AAA65719.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X63976; CAA45395.1; ALT_SEQ; Genomic_DNA.
DR PIR; H65013; H65013.
DR PIR; S11411; S11411.
DR RefSeq; NP_416896.4; NC_000913.3.
DR RefSeq; WP_000497400.1; NZ_LN832404.1.
DR AlphaFoldDB; P23842; -.
DR SMR; P23842; -.
DR BioGRID; 4259186; 204.
DR DIP; DIP-12011N; -.
DR IntAct; P23842; 1.
DR STRING; 511145.b2395; -.
DR jPOST; P23842; -.
DR PaxDb; P23842; -.
DR PRIDE; P23842; -.
DR EnsemblBacteria; AAC75454; AAC75454; b2395.
DR EnsemblBacteria; BAA16267; BAA16267; BAA16267.
DR GeneID; 66673736; -.
DR GeneID; 946864; -.
DR KEGG; ecj:JW5391; -.
DR KEGG; eco:b2395; -.
DR PATRIC; fig|1411691.4.peg.4333; -.
DR EchoBASE; EB1135; -.
DR eggNOG; COG2199; Bacteria.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_023566_2_0_6; -.
DR InParanoid; P23842; -.
DR OMA; IRIFWRR; -.
DR PhylomeDB; P23842; -.
DR BioCyc; EcoCyc:EG11145-MON; -.
DR PRO; PR:P23842; -.
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 Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF05231; MASE1; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 2: Evidence at transcript level;
KW c-di-GMP; Cell membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..729
FT /note="Probable cyclic di-GMP phosphodiesterase PdeA"
FT /id="PRO_0000169216"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 348..476
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 488..729
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 729 AA; 83524 MW; F1CF1AA15D592650 CRC64;
MFVEHNLIKN IKIFTLAFTL TVVLIQLSRF ISPLAIIHSS YIFLAWMPLC VMLSILFIFG
WRGVVPVLCG MFCTNLWNFH LSFLQTAVML GSQTFVVLCA CAILRWQLGT RWRYGLTSRY
VWQRLFWLGL VTPIGIKCSM YLVGSFFDFP LKISTFFGDA DAIFTVVDLL SLFTAVLIYN
MLFYYLTRMI VSPHFAQILW RRDIAPSLGK EKRAFTLSWL AALSVLLLLL CTPYENDFIA
GYLVPVFFII FTLGVGKLRY PFLNLTWAVS TLCLLNYNQN FLQGVETEYS LAFILAVLIS
FSVCLLYMVR IYHRSEWLNR RWHLQALTDP LTLLPNFRAL EQAPEQEAGK SFCCLRIDNL
EFMSRHYGLM MRVHCIRSIC RTLLPLMQEN EKLYQLPGSE LLLVLSGPET EGRLQHMVNI
LNSRQIHWNN TGLDMGYGAA WGRFDGNQET LQPLLGQLSW LAEQSCAHHH VLALDSREEM
VSGQTTKQVL LLNTIRTALD QGDLLLYAQP IRNKEGEGYD EILARLKYDG GIMTPDKFLP
LIAQFNLSAR FDLQVLESLL KWLATHPCDK KGPRFSVNLM PLTLLQKNIA GRIIRLFKRY
HISPQAVILE ITEEQAFSNA ESSMYNIEQL HKFGFRIAID DFGTGYANYE RLKRLQADII
KIDGVFVKDI VTNTLDAMIV RSITDLAKAK SLSVVAEFVE TQQQQALLHK LGVQYLQGYL
IGRPQPLAD
