ID A0A1G9W899_9BACI Unreviewed; 656 AA.
AC A0A1G9W899;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=SAMN05216498_0633 {ECO:0000313|EMBL:SDM80471.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDM80471.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDM80471.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDM80471.1,
RC ECO:0000313|Proteomes:UP000199334};
RA de Groot N.N.;
RL Submitted (OCT-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; FNIG01000001; SDM80471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9W899; -.
DR STRING; 237069.SAMN05216498_0633; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000199334; 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 SMART; SM00267; GGDEF; 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:UP000199334};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..301
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 656 AA; 73950 MW; CD922CA15A07222C CRC64;
MNDIKELTEN KSIWLLYGLA GFLTIIVIYY EWLIGSVLTV VLAYLIYLTY RNETKNKQRT
ENYISTLSYR VKKVGEEALL EMPYGIILFS EDYQIEWCNP YMNHFMDGEQ SLIGETLADL
SDPLAAAVKD EDEEQWITLD DRQFQAIIKS EERLIYLFDR TDHIELENRY DNERTIIGVI
FLDNYEELTQ AMDDTSKSHL NSEVTSILNS WSNDYGIHLK RTSQERFIAV MNKEILTQLE
KTKFEILDEV RELISDQNVP LTLSIGIGRG SVDLPELGDL AQSSLDLALG RGGDQVAIKD
ESGRVKFYGG KTNPMEKRTR VRARVISHAL RELVMESEKV LIMGHVTPDM DSIGSSIGIL
KLAQQNGKKG YVVFDPDGVN TGVQRLMDRI GENDDLAEWF ITPEDSLDVV TKNTLIVVVD
THKPSMVMEE RLLSKTEHIV VIDHHRRGEE FVEEPTLVYM EPYASSTAEL VTELLEYQDG
PLKLDVLEAT ALLAGITVDT KSFTLRTGSR TFDAASYLRS KGADTVLVQN LLKEDIDLYI
KRSELVKNAT VYREGVAIAK GLDDGEYGTI IIAQAADTLL TMSNVKASFV IANRKDGKIG
VSARSLGEIN VQVIMEKMNG GGHLTNAATQ LDDTTLEQVE EQLRDIIEEY FEGGED
//
