ID A0A398B0W9_9BACI Unreviewed; 656 AA.
AC A0A398B0W9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=D1953_17025 {ECO:0000313|EMBL:RID82954.1};
OS Peribacillus asahii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=228899 {ECO:0000313|EMBL:RID82954.1, ECO:0000313|Proteomes:UP000266016};
RN [1] {ECO:0000313|EMBL:RID82954.1, ECO:0000313|Proteomes:UP000266016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA001 {ECO:0000313|EMBL:RID82954.1,
RC ECO:0000313|Proteomes:UP000266016};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-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:RID82954.1}.
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DR EMBL; QWVS01000039; RID82954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398B0W9; -.
DR Proteomes; UP000266016; 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:UP000266016};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..301
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 656 AA; 73908 MW; 83A7776B0E311D14 CRC64;
MPSFFKERSM RSPLYGLFIV AVLCIGMFAY YNWIIAAIGV VVVSGLFYLT IQKMILHQRR
TEEYITTLSY RLKKVGEEAL LEMPIGIMLI NDDHYIEWTN PFLASCFAED SLAGRSLYDV
AESLVPLVKQ EIEMDIVTLN ERKFKVIHKR DERLLYFFDV TEQVEIEKTY EDERTVIATI
YLDNYDELTQ GMDDQRKSSL NSLVTSLLDK WAKENGVFLK RTSSERFITV FNENILHQLE
KGKFTILDEI RETTAKQNVP LTLSIGVGSG VSSLPELGAL AQSSLDLALS RGGDQVAIKQ
SNGKVKFFGG KTNPMEKRTR VRARVISHAL KDMVLESDKV IVMGHKNPDM DAIGSAIGIL
KVAQMNERDG YIVIDRQQLD NSVLRLMAEI ENKPELYTRF ISPDEVLEMV TDETLLVVVD
THKPSMVMDE RVLNRIDKVV VIDHHRRGEE FINHSLLVYM EPYASSTAEL VTELLEYQPK
RSKIDMLEST ALLAGIIVDT KSFTLRTGSR TFDAASYLRA RGADTVLVQK FLKEDVDTYI
ERAKLIKEVS FYKQGIAIAT SKDNAIHNQV LIAQAADTLL SMDGVSASFV IAKRSEDTVG
ISARSLGDIN VQVIMEMMNG GGHLTNAAAQ QIGSVEEVEK RLFEAIDEYL EGGQKE
//
