ID A0A6N8CQ69_9BACI Unreviewed; 655 AA.
AC A0A6N8CQ69;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 10-JUN-2026, entry version 22.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|ARBA:ARBA00066839, ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=GMB86_03475 {ECO:0000313|EMBL:MTT31075.1};
OS Terrilactibacillus tamarindi.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Terrilactibacillus.
OX NCBI_TaxID=2599694 {ECO:0000313|EMBL:MTT31075.1, ECO:0000313|Proteomes:UP000440978};
RN [1] {ECO:0000313|EMBL:MTT31075.1, ECO:0000313|Proteomes:UP000440978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCM23-1 {ECO:0000313|EMBL:MTT31075.1,
RC ECO:0000313|Proteomes:UP000440978};
RA Kingkaew E., Tanasupawat S.;
RT "Terrilactibacillus tamarindus sp. nov. BCM23-1 isolated from bark of
RT Tamarindus indica.";
RL Submitted (NOV-2019) 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 EC=3.1.4.59; Evidence={ECO:0000256|ARBA:ARBA00051753};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR026583-50};
CC Note=For phosphodiesterase activity, probably binds 2 Mn(2+) per
CC subunit. {ECO:0000256|PIRSR:PIRSR026583-50};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC {ECO:0000256|ARBA:ARBA00061474, 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:MTT31075.1}.
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DR EMBL; WNHB01000004; MTT31075.1; -; Genomic_DNA.
DR RefSeq; WP_155216875.1; NZ_WNHB01000004.1.
DR AlphaFoldDB; A0A6N8CQ69; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000440978; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106409; F:cyclic-di-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
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 FunFam; 3.10.310.30:FF:000002; Cyclic-di-AMP phosphodiesterase; 1.
DR FunFam; 3.90.1640.10:FF:000002; Cyclic-di-AMP phosphodiesterase; 1.
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 InterPro; IPR051319; Oligoribo/pAp-PDE_c-di-AMP_PDE.
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; PF24898; GGDEF_GdpP; 1.
DR Pfam; PF21370; PAS_GdpP; 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}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026583};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR026583-
KW 50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR026583-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000440978};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..301
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 655 AA; 73765 MW; 6EE6A2DAAA48EBD8 CRC64;
MSNQFKHRWR NDQLLVFGLL FLLLLIIVAI INWVVGLAGF LLLIALVIWY VRNDARFEKD
LKEYITTLSY RLKKVGEEAL LEMPIGIVLY DEKGHIEWIN HYMTAQSEGD RFLNQPLDKI
SEDLPEFIQS DDTDTFLTIQ GLKYHVISRK TERLLYFFDV TELMELKQKH FDEQTVFAII
CLDNYDEVTQ GVADQVRSNI NNAMTSTIQN WAIEHGIYLK RISSDRFVGI LNEKILQELE
EDHFIVLDRV REKILVSHIP LTLSIGVGSG TSSLPELGQY AQSALDLALG RGGDQVAIKH
PDGKVKFYGG KSNPVEKRTR VRARVISHAL SELIVESDQV IVMGHQYPDM DAIGACIGIL
KIAEVNGKEA RIVVDPKNYG AGVIKLVEEL RKNEELWSKF ISPEEAEEKM TRGTLVVVVD
THKPSMVMDA KLLPMADRVV IIDHHRRAEE FVKDPVLVYM EPYASSTCEL VTELIEYQSK
DLSLDVIEAT SMLAGITVDT KSFTFRTGSR TFDAASQLRS HGADTILVQK LLRDDLNQFN
MRAHLIKDTT IYKDHIAIAL GTEDQTYDQV LIAQTADTLL TMEGVKASFV VCMRKDNKVG
ISARSLGEIN VQLIMESVGG GGHLTNAATQ LEDESIGEAY DLLKQAIDNY LQGGM
//
