ID A0A3M7TR07_9BACI Unreviewed; 655 AA.
AC A0A3M7TR07;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=EBO34_15075 {ECO:0000313|EMBL:RNA68004.1};
OS Alteribacter keqinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA68004.1, ECO:0000313|Proteomes:UP000278746};
RN [1] {ECO:0000313|EMBL:RNA68004.1, ECO:0000313|Proteomes:UP000278746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KQ-3 {ECO:0000313|EMBL:RNA68004.1,
RC ECO:0000313|Proteomes:UP000278746};
RA Wang H.;
RT "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkaline lake.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RNA68004.1}.
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DR EMBL; RHIB01000002; RNA68004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7TR07; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000278746; 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; 3.30.70.270; -; 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; 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 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:UP000278746};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..300
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 655 AA; 73647 MW; 16DC29644ADEFF84 CRC64;
MPNFLMKRWH GYHVVALLGI AILFTGILTY YQWQIGLVGF LGIAIVFIFV LRARIQFEKD
LTDYVSTLSY RVNKAGEEAV MKLPIGMVLY NEAGIIQWVN PYMSALLADD VLGENVDIIS
EDLPVLMEDE GKEFLLTLGE RKYRVVNESN ERLLYFFNAT EEQEIKELFE RDKTVIGLIY
LDNYDEVTQG MEDQLRSKLL THVTNVLNSW AKDQDIFLRR IASDRFIAIF NEEALYNLEE
DRFTLLDEVR EGTAQEKVAL TLSIGVGSGH SSLRELGALA QSSLDLALGR GGDQVAIKQS
DGKVRFYGGK SNAMEKRTRV RARVISHAIR DFVKESDRVI IMGHKNPDMD SIGAAIGMLK
IAQVNNKDAF IVLDPDNVNQ SVHKLLEAIQ DHDDLWAHFI TPEEAREEMT DETLMVVVDT
HKPSLCIDTK LLDRVERIIV IDHHRRGEEF IEEAVLVYME PYASSTAELV TELLEYQPNH
PNLDVLEATA LLSGIIIDTK SFAIRTGSRT FDAASYLKSQ GADTTLVQKL MKEDLDQYVK
RANLVERAYI YTAGTAIARG EENQTYNQVL IAQAADTLLT MNNVVASFVI SELEDGRVSI
SARSLGEINV QVIMENMHGG GHLTNAATQI SGMSLEEAED LLKEKIDDYF KGGQS
//