ID A0A1S9IGI8_9CLOT Unreviewed; 661 AA.
AC A0A1S9IGI8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=BS638_02515 {ECO:0000313|EMBL:OOO69434.1};
OS Clostridium tepidum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO69434.1, ECO:0000313|Proteomes:UP000190256};
RN [1] {ECO:0000313|EMBL:OOO69434.1, ECO:0000313|Proteomes:UP000190256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO69434.1,
RC ECO:0000313|Proteomes:UP000190256};
RA Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA Samadpour M.;
RT "Clostridium tepidum sp. nov., a close relative of Clostridium sporogenes
RT and Clostridium botulinum Group I.";
RL Submitted (DEC-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}.
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:OOO69434.1}.
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DR EMBL; MRAE01000004; OOO69434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9IGI8; -.
DR STRING; 1962263.BS637_09845; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000190256; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Membrane {ECO:0000256|PIRNR:PIRNR026583, ECO:0000256|SAM:Phobius};
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 TRANSMEM 35..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..153
FT /note="Cyclic-di-AMP phosphodiesterase GdpP-like PAS"
FT /evidence="ECO:0000259|Pfam:PF21370"
FT DOMAIN 349..504
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 526..651
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
FT COILED 631..658
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 661 AA; 75501 MW; 4B198A410A1CF2A0 CRC64;
MSDNRYDNFI TNNKMYMFII AILIIIIFSY KHSKIGIVLT LIYFLLLFYN FKNTRNKKKE
LKEFIEDFST KMDNAFKSSL MNLPFPMMII SNDGEVLWYN QNFSLLLKEE GILGEHISNI
LKNFNFRYAL EGKKKSFKNI NFKDNYYNIY TNTFFDEEMG EKILLLYFYD VTDMFNILIN
MEKNKEAIML LEVDNLDEVL KSIDIDKQPL IIAEIERHIN SFSESMKAMI KKYEPNKYVL
SVQNSYIEKQ MEKKFDILDM IREIDTGNRM SPTLSIGVGK GAETPLENYS YALAAKELAL
GRGGDQSVVK NKDKFLFYGG KTKEVEKRTK VRARVIAHAL VNLINESSNI IIMGHTNADI
DCLGSAIGLH SVINQLEKKS YIILENYNKS SEFLLNKIKE EKGYENIFIS SKEALDIINE
DTLLIIVDSH NRGYVQNTDL VDKTNKIVII DHHRRATDYI EKSILSYIEP YASSTSELVT
EMIQYMVEKP NISPIIAEAL LAGIYVDTKN FYFKTGVRTF EAASFLKKFG ADTIDVKKFF
ASDLDTYIKK LEIIKSVHVK NDIAIAVCPE NIGDNVLAAQ AADELLNISG IQASFVFVTI
NKETYISGRS LGDINVQLIL EMLGGGGHMT MAGAKLEKVT LEEAVEKLEL AIDKYLREGE
G
//
