GenomeNet

Database: UniProt
Entry: A0A075RCI4_BRELA
LinkDB: A0A075RCI4_BRELA
Original site: A0A075RCI4_BRELA 
ID   A0A075RCI4_BRELA        Unreviewed;       645 AA.
AC   A0A075RCI4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   Name=nrnA_2 {ECO:0000313|EMBL:AIG28903.1};
GN   ORFNames=BRLA_c046400 {ECO:0000313|EMBL:AIG28903.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG28903.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG28903.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG28903.1,
RC   ECO:0000313|Proteomes:UP000005850};
RX   PubMed=21914864; DOI=10.1128/JB.05696-11;
RA   Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT   "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT   invertebrates.";
RL   J. Bacteriol. 193:5535-5536(2011).
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   ---------------------------------------------------------------------------
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; CP007806; AIG28903.1; -; Genomic_DNA.
DR   RefSeq; WP_003334012.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075RCI4; -.
DR   STRING; 1042163.BRLA_c046400; -.
DR   KEGG; blr:BRLA_c046400; -.
DR   eggNOG; COG3887; Bacteria.
DR   HOGENOM; CLU_018278_0_0_9; -.
DR   Proteomes; UP000005850; 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   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; IPR029787; Nucleotide_cyclase.
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   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50887; GGDEF; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR026583};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR026583, ECO:0000313|EMBL:AIG28903.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..299
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   645 AA;  72312 MW;  8C0C7F05744A005B CRC64;
     MPKFLFKRWY GLHMVLALSF SLVLVAILTL YHWIYGAIGI VCIIGLILAT LQIEKRFQQD
     LKMYIATINH RVKKASEGVL QEMPIGILLF NEDREVEWTN PYMQQMTNME NLIGKELAEL
     FPALEWKAEQ KKLDFTFGER IYEVLIRPEE RLLYFTDVTE YKELAIRYQQ EKTIVGIIHL
     DNLDELSQVM DDQSRTLLTT SVSGVILEWA QKHGILLRRM SSDKFLAVMD RATLDRLEET
     RFDILDVVRE MTADNKIPIT LSIGVGAAMP SLVEVGKNAQ SSLDIALGRG GDQAAVKVGN
     KLTFYGGKSN AVEKRTRVRA RVIAHALRDL IHEAEQVIVM GHKNADMDSI GACLGVIKTV
     QIHNKPGFIV LDEVNPAIER LMKEVNQSPL AEAFISPDQA LQIVSSRTLL VIVDTHRPSL
     VVESRLLQET SRIVVIDHHR RSEEFINDPV LLYLEPYASS TAELVTELLQ YQTDRVSLDS
     VTATGLLAGI VVDTKSFAFR TGSRTFEAAS FLRRNGADTA MVQRFLKEDI QQFVKRARVV
     MNTEVYRDKM AIAVGDPKET YTQVQVAQAA EALLTLEGVQ ASFVIAMRAD EVVLISARSL
     GDINVQSIME KMGGGGHLNG AATQMKDIAI PDAVRLLKDV IDTEL
//
DBGET integrated database retrieval system