ID A0A398CJW2_9BACL Unreviewed; 660 AA.
AC A0A398CJW2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=D3H35_24245 {ECO:0000313|EMBL:RIE01469.1};
OS Cohnella faecalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE01469.1, ECO:0000313|Proteomes:UP000266340};
RN [1] {ECO:0000313|EMBL:RIE01469.1, ECO:0000313|Proteomes:UP000266340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE01469.1,
RC ECO:0000313|Proteomes:UP000266340};
RA Zhu H.;
RT "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL Submitted (SEP-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:RIE01469.1}.
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DR EMBL; QXJM01000040; RIE01469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398CJW2; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000266340; 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 InterPro; IPR000160; GGDEF_dom.
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:UP000266340};
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..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 179..307
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 660 AA; 74154 MW; D31D822837325B22 CRC64;
MPKFLVQRWH GMHIVWALLL IFMLTVALAW YHWVLGLIGL ILGGAVAAFG ILAERAFRKD
LNDYVLTLSH RIKSVGSDVI GHLPFGIVIY NEDKDIQWHN AYISTVVGRP SVVGETLTHI
FPALQQASKE KEKDKDKETV VETTIGGRVF ELMFRPAERM VYVSDITERW TLKKRYEEEK
LALGIVIMDN LEEIAQGMDE QQRAIMLSRV TGEINEWALR YGLYLRRLSS DRYMIITNLG
TLKHLEQTRF DLLDEVRELT QDQKLPMTLS IGLASGVDNV VELGHLAQSS LDIALGRGGD
QAVVKVGQRQ NFYGGKSNAV EKRTRVRARV ISHALRDLIK ESDHVIVMGH KMPDMDAIGA
AIGVVKAAQI CGKEAYIVLE GINPAIQKMM EMLKEDEKLI RRFISPEQAL ALMHKRSLAI
VVDTHKATMV AEPRLLQATD RIVIVDHHRR SEEFIDDAVL VYMEPYASST CELVTELLQY
IHERVALDVR EATALLAGIT VDTKSFALRT GSRTFEAASF LRRNGADSML IQRMLKEDLE
EYVKKAEIIR HANVYREHIA IAAYDSGKQV PQLLIAQSAD TLLNMTGIKA SFVVAQRPDG
LIGISARSLG QINVQIVMER MGGGGHFTNA ASQLQGTVQE VADKLKQTLI ELEDKERLFE
//
