ID A0A0K9GIW7_9BACI Unreviewed; 657 AA.
AC A0A0K9GIW7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=AC622_20170 {ECO:0000313|EMBL:KMY46217.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY46217.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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:KMY46217.1}.
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DR EMBL; LFZV01000001; KMY46217.1; -; Genomic_DNA.
DR RefSeq; WP_049672664.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9GIW7; -.
DR STRING; 1679169.AC622_20170; -.
DR PATRIC; fig|1679169.3.peg.4275; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000036953; 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.
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:UP000036953};
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 TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..299
FT /note="GGDEF"
FT /evidence="ECO:0000259|SMART:SM00267"
SQ SEQUENCE 657 AA; 73696 MW; DC5DB07A8A062C0F CRC64;
MPSYLKKQAI RYPIYALISV SVMIVGILAY YNWIFALVAS LLFVTFFFLI LQIESAVRKE
TEVYISTLSY RLKRVGEEAL LEMPIGILLY NDEFLVEWAN PYMAKCLEED TLVGKYIEQA
AEPLLPFLRK QETETILTFY NREYRIVHKP DEKLLYFFDV TEQTEIEKLY EDEQTVIGII
FLDNYDDVTQ GMDDQRKSGL NSFVTSLLNN WAKEYGVFLK RISSDRFIAV MNENILTELE
KTKFSILDDV RETTAKQNVP LTLSIGIGSG IPSLPDLGVI AQSSLDLALG RGGDQAAIKL
PNGKVKFYGG KTNPMEKRTR VRARVISHAL RDLIIDSDKV IIMGHKFPDM DAIGSSLGVL
KIAQMNDRDG YIILDRDELD SGVKRLLCEI KQKPELDAMF ISPENGVELI TEKTLLVVVD
THKPSLVIDD RIISRTEKIV VIDHHRRGEE FIDNSLLVYM EPYASSTAEL VTELIEYQPS
RVKLEMLEST ALLAGIIVDT KSFTFRTGSR TFDAASFLRG HGADTIMVQR LLKESVDSYL
QRAKLLSNVY FYKDGVAIAS GEVSGYVDQV LIAQAADTLL SMEGVSASFV LAKKEEDIIG
VSARSLGEVN VQVIMEQLGG GGHLTNAATQ LEKISMLKAE QMLKEAIDEQ LEGGTIS
//
