ID A0A1M7QP68_9BACI Unreviewed; 659 AA.
AC A0A1M7QP68;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05216179_3418 {ECO:0000313|EMBL:SHN33306.1};
OS Gracilibacillus kekensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1027249 {ECO:0000313|EMBL:SHN33306.1, ECO:0000313|Proteomes:UP000184184};
RN [1] {ECO:0000313|EMBL:SHN33306.1, ECO:0000313|Proteomes:UP000184184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10681 {ECO:0000313|EMBL:SHN33306.1,
RC ECO:0000313|Proteomes:UP000184184};
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; FRCZ01000008; SHN33306.1; -; Genomic_DNA.
DR RefSeq; WP_073203032.1; NZ_FRCZ01000008.1.
DR AlphaFoldDB; A0A1M7QP68; -.
DR STRING; 1027249.SAMN05216179_3418; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000184184; 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:UP000184184};
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..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..302
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 659 AA; 75028 MW; 168F169C9B88508C CRC64;
MPKFIDKPVV MGRHIIAIYI LSFLLLIFLF YYHWILGVIM AIFFTVSLYY SIKRERQLVD
QTEAYISTLS YRVKKVGEEA LLEMPIGIML YGEDYQIEWA NPYLNEFTKE DTLVGENLEI
LSDNLISQLK DSKDTFWLTI DEYDFQVYNK KEERLLYLFD RTKQTELHHM YQNEKTVLGI
IFLDNYEEIT QNMDDTAKSQ LNSQVTATLN KWSHEHEIYL KRTSQERFMA VMNQKILGEL
EKIKFEILDE VRELITDKNV PLTLSIGIGL GSESLPELGE LTQSSLDLAL GRGGDQVVIK
DDESGKVRFY GGKTNPMEKR TRVRARVISH ALKELVKESD QVLVMGHKAP DMDSIGSSIG
VLKIAQANDI EAYIVLDEND IDTGVQRLVE EMKEKEELWS HFIDPDSALD IVSKDTLLVI
VDTHKPSMVQ EEKLIQKTDH VVVIDHHRRG EEFVDHPTLV YMEPYASSTA ELVTELLEYQ
PSKLSLNMLE STALLAGIIV DTKSFTLRTG SRTFDAASYL RSKGADTVLV QKFLKEDLDI
YVKRSRLIEN TNIYRGNIAI SVGNSREPYG PVVIAQAADT LLTMTGVEAS FVISERKDGR
IGISARSLGD INVQVLMEKM NGGGHLTNAA TQLDDMAVID AYEWLKDIID EYYEGGDSE
//
