ID   M1Z519_9FIRM            Unreviewed;       666 AA.
AC   M1Z519;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=CUESP1_0645 {ECO:0000313|EMBL:SHD76029.1};
OS   [Clostridium] ultunense Esp.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC   Schnuerera.
OX   NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD76029.1, ECO:0000313|Proteomes:UP000245423};
RN   [1] {ECO:0000313|EMBL:SHD76029.1, ECO:0000313|Proteomes:UP000245423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD76029.1};
RA   Manzoor S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has phosphodiesterase (PDE) activity against cyclic-di-AMP
CC       (c-di-AMP). {ECO:0000256|PIRNR:PIRNR026583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-
CC         adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171;
CC         Evidence={ECO:0000256|PIRNR:PIRNR026583};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC       {ECO:0000256|PIRNR:PIRNR026583}.
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DR   EMBL; LT669839; SHD76029.1; -; Genomic_DNA.
DR   RefSeq; WP_005582422.1; NZ_LT669839.1.
DR   AlphaFoldDB; M1Z519; -.
DR   HOGENOM; CLU_018278_0_0_9; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000245423; Chromosome chri.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0106409; F:cyclic-di-AMP phosphodiesterase activity; IEA:RHEA.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.30; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR049553; GdpP-like_PAS.
DR   InterPro; IPR014528; GdpP/PdeA.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   PANTHER; PTHR47618; BIFUNCTIONAL OLIGORIBONUCLEASE AND PAP PHOSPHATASE NRNA; 1.
DR   PANTHER; PTHR47618:SF2; CYCLIC-DI-AMP PHOSPHODIESTERASE GDPP; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF21370; GdpP_PAS; 1.
DR   PIRSF; PIRSF026583; YybT; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50887; GGDEF; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR026583}; Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245423};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          185..313
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   666 AA;  75785 MW;  37AB1A6D666CF4D5 CRC64;
     MDNKNFFKWK DGRTYLIIIG GLIAIIAYYQ PILALLLAIA LAFLVYKYII TLREKEEEWT
     KYIEGLAEEF DTATKHAVFN MPFPLVMLEM DGTISWYNTR FIDMMEEKDI LNKKIDEILP
     KLRVETILKD ANKAPLKIEY NNQHYEVHYN IVDGKKTIST KGNIIMLYWV NKTEQALLYN
     RYEEEKIAVC LAYIDNYDEV KNTTPEINRP LVLAEIDKTI NAYATMNHGL VRKYENDKYI
     LIFESKSLQQ IQNRKFDILD RIREIDKGNS ISITLSMGVG INGKNPNENY EYARAAIDIA
     LGRGGDQAVV KDNNNLSFYG GKTKAIEKRN KVRSRVISHA LMQLIDQSEK VFVMGHKNAD
     MDSFGASIGI IRAVRNRNKK AYFILGGVNP SIKNIYVRME EEQPEYLDLI LEPEEAIDMV
     DRSSLLVVVD NHKPSFTEAP ELLDLTDKVV LIDHHRRGAE FIKDLVLTYL EPYASSTCEL
     VTEILYYMSD KMEMTKFEAD ALLAGITVDT KNFTFQTGVR TFEAASILKR AGADTTSVRQ
     LFRDDFNTFL HKAEVVKNSK VVFEKIAIGK LDSEMEDSIL IAAQSANDLL NINGVEATFV
     LTLWEGKVHI SGRSLGNISV QLILEKLGGG GHLTSAGTQI EGKTLEQVEE MLIEAIDEYL
     KEGEEE
//