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Database: UniProt
Entry: K8E2C8_CARML
LinkDB: K8E2C8_CARML
Original site: K8E2C8_CARML 
ID   K8E2C8_CARML            Unreviewed;       280 AA.
AC   K8E2C8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_01499};
DE            Short=DAC {ECO:0000256|HAMAP-Rule:MF_01499};
DE            EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_01499};
DE   AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
DE            Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
GN   Name=ybbP {ECO:0000313|EMBL:CCO10099.1};
GN   Synonyms=dacA {ECO:0000256|HAMAP-Rule:MF_01499};
GN   ORFNames=BN424_621 {ECO:0000313|EMBL:CCO10099.1};
OS   Carnobacterium maltaromaticum LMA28.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10099.1, ECO:0000313|Proteomes:UP000000212};
RN   [1] {ECO:0000313|Proteomes:UP000000212}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX   PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA   Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA   Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA   Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT   "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL   Genome Announc. 1:0-0(2013).
CC   -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into cyclic di-
CC       AMP (c-di-AMP), a second messenger used to regulate differing processes
CC       in different bacteria. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00000877, ECO:0000256|HAMAP-
CC         Rule:MF_01499};
CC   -!- SUBUNIT: Probably a homodimer. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01499}.
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DR   EMBL; HE999757; CCO10099.1; -; Genomic_DNA.
DR   RefSeq; WP_010049781.1; NC_019425.2.
DR   AlphaFoldDB; K8E2C8; -.
DR   STRING; 1234679.BN424_621; -.
DR   GeneID; 83607035; -.
DR   KEGG; cml:BN424_621; -.
DR   PATRIC; fig|1234679.3.peg.590; -.
DR   eggNOG; COG1624; Bacteria.
DR   HOGENOM; CLU_038561_0_1_9; -.
DR   OrthoDB; 9807385at2; -.
DR   Proteomes; UP000000212; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR   HAMAP; MF_01499; DacA; 1.
DR   InterPro; IPR014046; C-di-AMP_synthase.
DR   InterPro; IPR034701; CdaA.
DR   InterPro; IPR045585; CdaA_N.
DR   InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR   InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR   NCBIfam; TIGR00159; diadenylate cyclase CdaA; 1.
DR   PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR34185:SF1; DIADENYLATE CYCLASE; 1.
DR   Pfam; PF19293; CdaA_N; 1.
DR   Pfam; PF02457; DAC; 1.
DR   PIRSF; PIRSF004793; UCP004793; 1.
DR   SUPFAM; SSF143597; YojJ-like; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01499};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01499};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01499};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01499};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01499}; Reference proteome {ECO:0000313|Proteomes:UP000000212};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01499};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01499};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01499}.
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        41..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          84..243
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   280 AA;  31598 MW;  E3A11499E0A5C42D CRC64;
     MSIDWTQLFT WRNFFNVIDI LVVWFFVYKL ITLLKGTKAI QLLKGIAVII VIKMVSFLLN
     LETVDWLMDQ VISWGVIATI IVFQPEVRRG LEHLGRGAIF GRTKRQVDPT KRLIEALDKS
     VQYMAKRRIG ALISIEMETG LDEYIETGIP LDADISGELL INIFIPNTPL HDGAVIIKDY
     KIAAAAGYLP LSESSLIPKE LGTRHRAAIG LSEVTDAVTI IVSEETGGIS ITRNSELLRD
     LTQEEFVNYL IKEIVVKEEE HKKNPIQVFI DGFSKKEDSK
//
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