ID A0A1M5YG87_9CLOT Unreviewed; 663 AA.
AC A0A1M5YG87;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=SAMN02745196_02909 {ECO:0000313|EMBL:SHI10919.1};
OS Clostridium collagenovorans DSM 3089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHI10919.1, ECO:0000313|Proteomes:UP000184526};
RN [1] {ECO:0000313|EMBL:SHI10919.1, ECO:0000313|Proteomes:UP000184526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3089 {ECO:0000313|EMBL:SHI10919.1,
RC ECO:0000313|Proteomes:UP000184526};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FQXP01000014; SHI10919.1; -; Genomic_DNA.
DR RefSeq; WP_072832719.1; NZ_FQXP01000014.1.
DR AlphaFoldDB; A0A1M5YG87; -.
DR STRING; 1121306.SAMN02745196_02909; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000184526; Unassembled WGS sequence.
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; 3.90.1640.10; 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 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 SUPFAM; SSF64182; DHH phosphoesterases; 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:UP000184526};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..314
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 663 AA; 74312 MW; 9515993A084048A8 CRC64;
MNNKYKNLVP DNKVYLILIT LLIIALFYYE HFGLAAIFIS IFLVSILLNV KAYIDKKSKF
QKFIENLSSD MNIATSNHII NSPFSLILMG GRGEVLWYNQ KASSLLHERQ LLGKSIKDIS
KELNIKQIHE GKKQVFKYVE IENRYYDVFV TAIDKSQKPI IEDSVALLTF CDVTDKFNLE
ENIKNDKYTI MLIEVDNLND VLKTTSENEG PLLSAAIERT LNNYAQGLQG MIKKYASNKY
IVVAQNKFIK KEVENKFEIL DQIRDLYFGN KLAVTLSIGI GVGGVTANEN YGYSESAKEL
ALGRGGDQVV LKNRDKLSFF GGKTKEVEKR TKVKARVIAH ALVDLVNESD RVFIMGHKNA
DIDCIGAAIG LGSVIRNLGK RYNIILEEIG EGTKKVIEEV KKEYDNEKIF ISSDQCFTEI
TDNSLLIIVD VHNKNHVESM EIVNKSNRVV IIDHHRKSPD FISNNILSYI ETYASSTAEL
VTEMIPYMVD KPNVKVIEAI ALLSGICVDT KNFTFKTGVR TFEAAAFLRR LGADTVAVKK
MFSQNLDVYI KKADIIKNVQ VINDIAIAIC PQNIDNNIIA AQVADELITI SPIKASFALV
NIKDNIFISG RSLDDINVQV ILEGLNGGGH MNMAGAKLVN TSMDEAVELL KDSISKYLRE
GEK
//
