ID E0P200_9FIRM Unreviewed; 331 AA.
AC E0P200;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=HMPREF9166_2117 {ECO:0000313|EMBL:EFM22191.1};
OS Selenomonas sp. oral taxon 149 str. 67H29BP.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=864563 {ECO:0000313|EMBL:EFM22191.1, ECO:0000313|Proteomes:UP000004359};
RN [1] {ECO:0000313|EMBL:EFM22191.1, ECO:0000313|Proteomes:UP000004359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67H29BP {ECO:0000313|EMBL:EFM22191.1,
RC ECO:0000313|Proteomes:UP000004359};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFM22191.1}.
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DR EMBL; AEEJ01000054; EFM22191.1; -; Genomic_DNA.
DR AlphaFoldDB; E0P200; -.
DR eggNOG; COG1624; Bacteria.
DR HOGENOM; CLU_038561_0_1_9; -.
DR Proteomes; UP000004359; Unassembled WGS sequence.
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; 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 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}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW Membrane {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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01499}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01499}.
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT DOMAIN 141..301
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 331 AA; 36672 MW; 8F54C9B2BF7947B8 CRC64;
MYVEAILHAP SRNFFLRAPQ VTRIFPIRLE VLIYTEMGCK WNGMLGTWGV AMPLDFTMPT
QFRGILSTIT LLDVLDILIV AVILYRVYVM LKDTRAITLG KGILVLLGVT VVANYLNLHV
ISWLLQKAVT LLFVALPIVF QPELRRALEH LGQGKFFRPG TLLDDEEAQS TIREIRSAVK
ILSANKIGAL LVIERDMGLN DISATGIQID GLITSDFLMN VFIPNTPLHD GAAVIRGKRL
IAAGCLLPLT ENRSLSTELG TRHRAAIGLS EQCDALIVVV SEETGTISIA ENGHLHRHLD
GEQLTHILTP AFAYSSRSSI LDTIRSWREK S
//
