ID A0A1M5D3E6_9CLOT Unreviewed; 680 AA.
AC A0A1M5D3E6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=SAMN02745158_04401 {ECO:0000313|EMBL:SHF61529.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF61529.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHF61529.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF61529.1,
RC ECO:0000313|Proteomes:UP000184245};
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|PIRNR:PIRNR026583}.
CC -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC {ECO:0000256|PIRNR:PIRNR026583}.
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DR EMBL; FQVI01000054; SHF61529.1; -; Genomic_DNA.
DR RefSeq; WP_072854890.1; NZ_FQVI01000054.1.
DR AlphaFoldDB; A0A1M5D3E6; -.
DR STRING; 1122155.SAMN02745158_04401; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000184245; 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; IPR014528; GdpP/PdeA.
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 PIRSF; PIRSF026583; YybT; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR026583};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Membrane {ECO:0000256|PIRNR:PIRNR026583, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184245};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..520
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 558..671
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 680 AA; 76876 MW; 81995D68F683C0A8 CRC64;
MDKKVKIKGQ LKTYLQWPAI LTVLLLIMNI ALYVVNKQAG ALASIFLAVY ILIVAILYFY
NRPVLMSELI SFATQYGQVQ KNLLEEFLLP YALMDSQGKL LWMNHEFSQM TGKSKKYHKS
ITSIFEDITA DALPREEERT QLCFQFEEKD FRASMTKVSM AELFEGSDMM EAQGENYLVA
LYLFDETEIN RYIRENEEEK LVVGLLYLDN YDEALDSVEE VRRSLLTALI DRKLNKYFGE
LDGLVKKLEK DKYFLVMRNR SLMELEKRRF DILEDVKTVN IGNDMAVTIS IGIGINSGSY
AQNYEYSRIA IDLALGRGGD QVVIKDGNQI SYFGGKSQQM GKSTRVKARV KAHALKEFMS
SKDKVVVMGH KISDVDSFGA GVGIYRAAKS LNKRAHIVVN NPTMSIRPLM QSFLNNPDYD
ENMFINSYEA KEIVDNNTVV VVVDTNKPSY TECDDLLHMT KTIVVLDHHR QGSEVIQNAV
LSYIEPYASS ACEMVAEILQ YFSDDIRIRN VEADSLYAGI MIDTNNFLAK TGVRTFEAAA
FLRRCGADVT RVRKMFRDDM ESYKARAEAV RHTENYRECY AISVCPSAGL DSPTVVAAQA
ANELLNIVSV KASFVLTEYN DQIYISARAI DEVNVQLIME RLGGGGHINI AGAQLKDMTL
DEAVALLKKT IDEMLEEGDI
//
