ID A0A1M4X7B5_9LACT Unreviewed; 663 AA.
AC A0A1M4X7B5;
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=SAMN02745249_01377 {ECO:0000313|EMBL:SHE89410.1};
OS Atopostipes suicloacalis DSM 15692.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Atopostipes.
OX NCBI_TaxID=1121025 {ECO:0000313|EMBL:SHE89410.1, ECO:0000313|Proteomes:UP000184128};
RN [1] {ECO:0000313|EMBL:SHE89410.1, ECO:0000313|Proteomes:UP000184128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15692 {ECO:0000313|EMBL:SHE89410.1,
RC ECO:0000313|Proteomes:UP000184128};
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|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}.
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DR EMBL; FQUF01000019; SHE89410.1; -; Genomic_DNA.
DR RefSeq; WP_073298125.1; NZ_FQUF01000019.1.
DR AlphaFoldDB; A0A1M4X7B5; -.
DR STRING; 1121025.SAMN02745249_01377; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000184128; 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 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:UP000184128};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..311
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 663 AA; 75520 MW; B1101B808AD44553 CRC64;
MKPLNDKRLA SFFKIDSLNK VVSLVIAIQI FIVFISVVLK LWLGLLVLLL FIIMDVVLWR
LSERASEDLN SYISNLSYRI KRGEHEAIIK LPIGIIIYNE DLEIEWLSPY LQTGSKDAEP
IIGRKIQDVF DGILEAMEED DPENKIINWR DNYYRIRVEK DIHVIYLENV SYYIHIREEL
ERNRSVIGWL FLDNYDELIK GLDDRAISNF NSLLTTYLSN WARQHNIYYK RIENDKYLLL
LRHDELARLE DEDFNIVNNI RDYTSKRNLP LTVSIGVSYG EASFIELAEL SQKDLDLALG
RGGDQAIVRE VGQEPRYYGG NTNPMEKRTR VRSRMISEAL QEQIKQAPTT YVMGHAFPDM
DAIGSALGIA RIAMMLGKEA KVIVDQEKVG NDISNLLDEI SKYHETAKNI ISPEEAFEKI
TSEDLVVMVD HHKPSMSIAP HLNEKTNKVV IIDHHRRGDE FPDKPTLVYI EPYASSASEL
ITELFEYVSS DSNSINRIEA TTMLGGIIVD TNNFSLRTGS RTFDAASYLQ SVGANTTTIQ
RMLKESPENY LTRMEIVKNM EFVIDGMAVA HGEENEYHRQ VVAAQTADTI LSMTDVEASF
VIVRLDEETV GISARSLGKV NVQRVMEKMG GGGHLTNAAT QIKDLTITEV KEQLKQAIKE
INT
//
