PDEK_ECOLI
ID PDEK_ECOLI Reviewed; 662 AA.
AC P37649; Q2M7J1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable cyclic di-GMP phosphodiesterase PdeK {ECO:0000305};
DE EC=3.1.4.52 {ECO:0000250|UniProtKB:P21514};
GN Name=pdeK {ECO:0000303|PubMed:26148715}; Synonyms=yhjK;
GN OrderedLocusNames=b3529, JW5943;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP INDUCTION.
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 -!- INTERACTION:
CC P37649; P77319: hscC; NbExp=3; IntAct=EBI-562146, EBI-562084;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed at 28 degrees Celsius in stationary phase.
CC {ECO:0000269|PubMed:19332833}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77765.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18506.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76554.4; -; Genomic_DNA.
DR EMBL; AP009048; BAE77765.1; ALT_INIT; Genomic_DNA.
DR PIR; S47750; S47750.
DR RefSeq; NP_417986.4; NC_000913.3.
DR RefSeq; WP_001266293.1; NZ_SSZK01000039.1.
DR AlphaFoldDB; P37649; -.
DR SMR; P37649; -.
DR BioGRID; 4262160; 7.
DR DIP; DIP-12384N; -.
DR IntAct; P37649; 1.
DR STRING; 511145.b3529; -.
DR jPOST; P37649; -.
DR PaxDb; P37649; -.
DR PRIDE; P37649; -.
DR EnsemblBacteria; AAC76554; AAC76554; b3529.
DR EnsemblBacteria; BAE77765; BAE77765; BAE77765.
DR GeneID; 948048; -.
DR KEGG; ecj:JW5943; -.
DR KEGG; eco:b3529; -.
DR PATRIC; fig|511145.12.peg.3640; -.
DR EchoBASE; EB2165; -.
DR eggNOG; COG2199; Bacteria.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_000445_70_46_6; -.
DR OMA; DREMGMQ; -.
DR PhylomeDB; P37649; -.
DR BioCyc; EcoCyc:EG12256-MON; -.
DR BioCyc; MetaCyc:EG12256-MON; -.
DR PRO; PR:P37649; -.
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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR033419; GAPES3.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF17154; GAPES3; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00672; HAMP; 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.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW c-di-GMP; Cell membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..662
FT /note="Probable cyclic di-GMP phosphodiesterase PdeK"
FT /id="PRO_0000169574"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 180..236
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 268..400
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 409..662
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 662 AA; 74381 MW; 62CFA842B5851302 CRC64;
MRVSRSLTIK QMAMVAAVVL VFVFIFCTVL LFHLVQQNRY NTATQLESIA RSVREPLSSA
ILKGDIPEAE AILASIKPAG VVSRADVVLP NQFQALRKSF IPERPVPVMV TRLFELPVQI
SLGVYSLERP ANPQPIAYLV LQADSFRMYK FVMSTLSTLV TIYLLLSLIL TVAISWCINR
LILHPLRNIA RELNAIPAKE LVGHQLALPR LHQDDEIGML VRSYNLNQQL LQRHYEEQNE
NAMRFPVSDL PNKALLMEML EQVVARKQTT ALMIITCETL RDTAGVLKEA QREILLLTLV
EKLKSVLSPR MILAQISGYD FAVIANGVQE PWHAITLGQQ VLTIMSERLP IERIQLRPHC
SIGVAMFYGD LTAEQLYSRA ISAAFTARHK GKNQIQFFDP QQMEAAQKRL TEESDILNAL
ENHQFAIWLQ PQVEMTSGKL VSAEVLLRIQ QPDGSWDLPD GLIDRIECCG LMVTVGHWVL
EESCRLLAAW QERGIMLPLS VNLSALQLMH PNMVADMLEL LTRYRIQPGT LILEVTESRR
IDDPHAAVAI LRPLRNAGVR VALDDFGMGY AGLRQLQHMK SLPIDVLKID KMFVEGLPGD
SSMIAAIIML AQSLNLQMIA EGVETEAQRD WLAKAGVGIA QGFLFARPLP IEIFEESYLE
EK
