GenomeNet

Database: UniProt
Entry: K0J161_AMPXN
LinkDB: K0J161_AMPXN
Original site: K0J161_AMPXN 
ID   K0J161_AMPXN            Unreviewed;       656 AA.
AC   K0J161;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   10-JUN-2026, entry version 53.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   OrderedLocusNames=AXY_23870 {ECO:0000313|EMBL:BAM48519.1};
OS   Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS   / NBRC 15112 / Ep01).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Amphibacillus.
OX   NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM48519.1, ECO:0000313|Proteomes:UP000006294};
RN   [1] {ECO:0000313|EMBL:BAM48519.1, ECO:0000313|Proteomes:UP000006294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC   Ep01 {ECO:0000313|Proteomes:UP000006294};
RA   Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA   Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA   Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA   Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL   Submitted (JAN-2011) 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR026583-50};
CC       Note=For phosphodiesterase activity, probably binds 2 Mn(2+) per
CC       subunit. {ECO:0000256|PIRSR:PIRSR026583-50};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC       {ECO:0000256|PIRNR:PIRNR026583}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012050; BAM48519.1; -; Genomic_DNA.
DR   RefSeq; WP_015011097.1; NC_018704.1.
DR   AlphaFoldDB; K0J161; -.
DR   STRING; 698758.AXY_23870; -.
DR   KEGG; axl:AXY_23870; -.
DR   PATRIC; fig|698758.3.peg.2393; -.
DR   eggNOG; COG3887; Bacteria.
DR   HOGENOM; CLU_018278_0_0_9; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000006294; Chromosome.
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   FunFam; 3.90.1640.10:FF:000002; Cyclic-di-AMP phosphodiesterase; 1.
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   InterPro; IPR051319; Oligoribo/pAp-PDE_c-di-AMP_PDE.
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; PF24898; GGDEF_GdpP; 1.
DR   Pfam; PF21370; PAS_GdpP; 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   Manganese {ECO:0000256|PIRSR:PIRSR026583-50};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR026583-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006294};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          173..302
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         420
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         420
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         444
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT   BINDING         499
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ   SEQUENCE   656 AA;  74433 MW;  CC8C6E93F6DAD3D4 CRC64;
     MRNTIEKYSP SMHIILIYLI AFILLGFTWF LQWILGLVMT ILLGLSLYYT IRQEQREIVE
     QEKYIMTLSH RVRKVGEEAL LEMPVGILLY NDAFEIEWVN PYLNQFVKEG TFVGKSLDVF
     SKDIITAIKE DKPKVNFYLE DCHFAVTIKK EERLLYFLDQ TKQVKIQHHY NNVKPVLGII
     YLDNYDETTK TMDDTGRSQL NSHVTSILNK WSNHYGIYLK RISQDRFLAV LNQQILEALE
     KSKFEILDEF RELILDNNNV PLTISFGIGH RSNQLTVLGE LAQSSLDLAL GRGGDQVVIK
     DTEGKVRFFG GKTNPMEKRT RVRARVISNA LKQLMVESEQ VFIMGHQSPD MDSVGSAIGI
     LKMALANEIE AFIVLDVNEL NFGVSRLIQE FKDTELWDYI ISPDQAIELV TKGSLIVVVD
     THRPSIVIES RLLNKTDHIV VIDHHRRGEE FIEDPTLVYM EPYASSTAEL VTELIEYQAP
     LVKLSRLEAT ALLAGIVVDT KNFNFRTGSR TFDAASYLRS KGADTILVQN FLKDDLEDFI
     KRSHLIERTT IYKNNIAIAV AEPGQTFNSV VIAQTADTLL GMRNILASFV ISERSDQRIG
     ISARSAGDIN VQLIMEQMGG GGHLSNAATQ LENISVQEAY QQLIEIIDQS IEGGNE
//
DBGET integrated database retrieval system