CDPD_THEMA
ID CDPD_THEMA Reviewed; 368 AA.
AC Q9WY30; G4FHA0; R4NN00;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cyclic di-GMP phosphodiesterase TM_0186;
DE EC=3.1.4.- {ECO:0000269|PubMed:26786892};
GN OrderedLocusNames=TM_0186 {ECO:0000312|EMBL:AAD35279.1};
GN ORFNames=Tmari_0184 {ECO:0000312|EMBL:AGL49110.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP GLU-169; HIS-173 AND ASP-289.
RX PubMed=26786892; DOI=10.1021/acs.biochem.5b01227;
RA Miner K.D., Kurtz D.M. Jr.;
RT "Active site metal occupancy and cyclic di-GMP phosphodiesterase activity
RT of Thermotoga maritima HD-GYP.";
RL Biochemistry 55:970-979(2016).
CC -!- FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of
CC cyclic diguanylate (c-di-GMP) to GMP. Hydrolyzes c-di-GMP to GMP in a
CC two-step reaction, via the linear intermediate 5'-
CC phosphoguanylyl(3'->5')guanosine (pGpG). {ECO:0000269|PubMed:26786892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclic di-3',5'-guanylate + 2 H2O = 2 GMP + 2 H(+);
CC Xref=Rhea:RHEA:52928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58805;
CC Evidence={ECO:0000269|PubMed:26786892};
CC -!- ACTIVITY REGULATION: Can function in vivo with either divalent iron or
CC manganese occupying di- and trimetal sites. Dimetal is necessary and
CC sufficient to catalyze conversion of c-di-GMP to pGpG, but conversion
CC of pGpG to GMP requires an occupied trimetal site.
CC {ECO:0000269|PubMed:26786892}.
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DR EMBL; AE000512; AAD35279.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49110.1; -; Genomic_DNA.
DR PIR; E72408; E72408.
DR RefSeq; NP_228001.1; NC_000853.1.
DR RefSeq; WP_004082825.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WY30; -.
DR SMR; Q9WY30; -.
DR EnsemblBacteria; AAD35279; AAD35279; TM_0186.
DR EnsemblBacteria; AGL49110; AGL49110; Tmari_0184.
DR KEGG; tma:TM0186; -.
DR KEGG; tmm:Tmari_0184; -.
DR KEGG; tmw:THMA_0187; -.
DR PATRIC; fig|243274.17.peg.184; -.
DR InParanoid; Q9WY30; -.
DR OMA; RCANTQF; -.
DR OrthoDB; 1755994at2; -.
DR BRENDA; 3.1.4.52; 6331.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW c-di-GMP; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..368
FT /note="Cyclic di-GMP phosphodiesterase TM_0186"
FT /id="PRO_0000440638"
FT DOMAIN 2..114
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 148..345
FT /note="HD-GYP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01176"
FT REGION 341..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 260
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26786892"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26786892"
FT MOD_RES 49
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 169
FT /note="E->A: Can form pGpG but not GMP."
FT /evidence="ECO:0000269|PubMed:26786892"
FT MUTAGEN 173
FT /note="H->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26786892"
FT MUTAGEN 289
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26786892"
SQ SEQUENCE 368 AA; 41788 MW; FBF5E61DB5738BCC CRC64;
MTVLIVEDDD ITREAMGQYL KLSGFNVIEA ENGEKAVELS ENVDVALVDV MLPGMSGIEV
VNKIKAKNPS CVVFVVTAYD DTEIVKKCVE AGADDFIKKP VNLELLRLKI THALRNRVFH
MYRNSYLKSL KKKLFLLEKT AEEFFTEYED FLFEVLEILN MLSEYRDMET HRHTERVGWL
SGRIAEEMGM SEVFVTEIQF AAPLHDIGKI GIPDRILLKP GILTPEEFEI MKQHTTIGFR
ILSRSNSPIL QLGAEIALTH HERWDGSGYP RGLKEREIPI SGLIVAVADS FDAMVSRRPY
KNPKPLEEAF REIESLSGKL YSPEVVEAFL KLEKEITDVY RREKDEDTSH NGGRSHQSSP
GEGVEGIR
