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Database: UniProt
Entry: A0A1M4WXJ0_9BACL
LinkDB: A0A1M4WXJ0_9BACL
Original site: A0A1M4WXJ0_9BACL 
ID   A0A1M4WXJ0_9BACL        Unreviewed;       656 AA.
AC   A0A1M4WXJ0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=SAMN05444392_10419 {ECO:0000313|EMBL:SHE85956.1};
OS   Seinonella peptonophila.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Seinonella.
OX   NCBI_TaxID=112248 {ECO:0000313|EMBL:SHE85956.1, ECO:0000313|Proteomes:UP000184476};
RN   [1] {ECO:0000313|EMBL:SHE85956.1, ECO:0000313|Proteomes:UP000184476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44666 {ECO:0000313|EMBL:SHE85956.1,
RC   ECO:0000313|Proteomes:UP000184476};
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; FQVL01000004; SHE85956.1; -; Genomic_DNA.
DR   RefSeq; WP_073154426.1; NZ_FQVL01000004.1.
DR   AlphaFoldDB; A0A1M4WXJ0; -.
DR   STRING; 112248.SAMN05444392_10419; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000184476; 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   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.
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:UP000184476};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..161
FT                   /note="Cyclic-di-AMP phosphodiesterase GdpP-like PAS"
FT                   /evidence="ECO:0000259|Pfam:PF21370"
FT   DOMAIN          339..495
FT                   /note="DDH"
FT                   /evidence="ECO:0000259|Pfam:PF01368"
FT   DOMAIN          517..645
FT                   /note="DHHA1"
FT                   /evidence="ECO:0000259|Pfam:PF02272"
SQ   SEQUENCE   656 AA;  75323 MW;  1DACB68AB7C667DF CRC64;
     MPKFTKRYRH SYLLLFFLWL IFLVFIYHFT SNWWLTGLGG GLWFLSLLFV WLQGRLYQDE
     WRRALLLIQR RVIQGHRFAI HHLPYGLVLI NDDGVIEWHN QYVSKKMNVS TSSIGKVVDQ
     VFPLDLEHLR NPATVSEMAL GESTYEVSYD SKHQFLLFRD ITELVQLEEK YEQEQPIVGY
     LYIDNYDEVR QQLTDQEETI LLNTVNSMIS AWTERYQISL KRFDVDKMFF VTQALYLRKL
     IESHFDILDE MRNATHDQPI PLTLSMGVSN STGSVLDRAK TARAALNVAL ARGGDQTAVQ
     EKERLVFFGG KTNAIERRTR VRARVISHAM SNLFRANRRV VIMGHMNPDL DAIGAAVGVA
     CFAQYHQCEP HIILNESNPS IDRVWKKIKE YPTIESLFSL ASEVEDWIHE RDTLLVMVDT
     HRPSLTIEPK LLERVRHIVV IDHHRRGEDF VEDPILVYLE PYASSACELV TELLQYQDEQ
     CEMSAFEATL LLAGIVVDTK HFAFRTGSRT FEAASFLREK GADLALVQSL LKEDLDQYIK
     RAEMLKQTEM WGDEVAVAVG KEDEVYDQLL IAQAADTLLN MKGVAASFVI AKRKDGLVAI
     SARSQGEINV QLIMEAMGGG GHFTNAASQM KDCSLEETKE ILKKVVEKYS DREEKD
//
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