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Database: UniProt
Entry: U4KSG9_9MOLU
LinkDB: U4KSG9_9MOLU
Original site: U4KSG9_9MOLU 
ID   U4KSG9_9MOLU            Unreviewed;       245 AA.
AC   U4KSG9;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=dacA {ECO:0000256|HAMAP-Rule:MF_01499};
GN   ORFNames=BN85316220 {ECO:0000313|EMBL:CCV66643.1};
OS   Paracholeplasma brassicae.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Paracholeplasma.
OX   NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV66643.1, ECO:0000313|Proteomes:UP000032737};
RN   [1] {ECO:0000313|EMBL:CCV66643.1, ECO:0000313|Proteomes:UP000032737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX   PubMed=24158107; DOI=10.1159/000354322;
RA   Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA   Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT   "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT   A. laidlawii and Their Comparison to the Obligate Parasites from '
RT   Candidatus Phytoplasma'.";
RL   J. Mol. Microbiol. Biotechnol. 24:19-36(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; FO681348; CCV66643.1; -; Genomic_DNA.
DR   RefSeq; WP_030005495.1; NC_022549.1.
DR   AlphaFoldDB; U4KSG9; -.
DR   STRING; 61635.BN85316220; -.
DR   KEGG; abra:BN85316220; -.
DR   HOGENOM; CLU_038561_1_0_14; -.
DR   OrthoDB; 9807385at2; -.
DR   Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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; 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; 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:UP000032737};
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        12..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          76..234
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   245 AA;  28049 MW;  871D4EABC9E0E1FD CRC64;
     MTEWVKILLD GYIVWIVVYF LISFFIGSKR VFKIFLSVVF IYLITFFAKH FKLEASYEIL
     TYVETWLPLA LIVILAPDIR RSFETAWLLD NKKDMAVLGS QETKNHIVEA VMYLSSQKIG
     ALITIEKHNS LDQYADRAII MNSLVSKELL INIFTPLTPL HDGAVIIRGD SIRCAGAYYV
     LSESTKYDKT MGSRHRAALG ISEVTDSFTI VVSEETGTIS IVMEGIMLKI NDREKIYEYL
     NMFMK
//
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