(data stored in ACNUC7421 zone)

SWISSPROT: A4AVV8_MARSH

ID   A4AVV8_MARSH            Unreviewed;       270 AA.
AC   A4AVV8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, 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=dacA {ECO:0000256|HAMAP-Rule:MF_01499};
GN   OrderedLocusNames=FB2170_01652 {ECO:0000313|EMBL:EAR00038.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00038.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00038.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into
CC       cyclic di-AMP (c-di-AMP), a second messenger used to regulate
CC       differing processes in different bacteria. {ECO:0000256|HAMAP-
CC       Rule:MF_01499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP = c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500;
CC         EC=2.7.7.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01499,
CC         ECO:0000256|SAAS:SAAS01115408};
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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01499}.
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DR   EMBL; CP002157; EAR00038.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_01652; -.
DR   EnsemblBacteria; EAR00038; EAR00038; FB2170_01652.
DR   KEGG; fbc:FB2170_01652; -.
DR   eggNOG; ENOG4105C8B; Bacteria.
DR   eggNOG; COG1624; LUCA.
DR   HOGENOM; HOG000054800; -.
DR   OMA; ILWQGEL; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
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; -; 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   Pfam; PF02457; DisA_N; 1.
DR   PIRSF; PIRSF004793; UCP004793; 1.
DR   SUPFAM; SSF143597; SSF143597; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVV8.
DR   SWISS-2DPAGE; A4AVV8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772210};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772222};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772224};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01499}.
FT   TRANSMEM     20     37       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   TRANSMEM     44     61       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   TRANSMEM     67     89       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   DOMAIN       90    260       DAC. {ECO:0000259|PROSITE:PS51794}.
SQ   SEQUENCE   270 AA;  30394 MW;  196076F93C2B0995 CRC64;
     MLILPKRQGL DFLNFLDFKI TDIIDIILVA VLLYYIYKLV RGSVAINIFI GIVIIWGFWK
     LTELLEMEMI SSMVGGFMQV GLIALIIVFQ QEIRKFLLMI GSTNFANKRN FIKRFRFLKT
     DGIGTNIDVD AILGACEIMG ESKTGAILVI KRNNSLDFVK SSGDQMYVEV NQPILGSIFY
     KNSPLHDGAA VIEDNYVTAT RVILPVSNER NIPLRFGLRH RAAVGITERT DALALVVSEE
     TGNISYIKNG EFVLFKDLTE LGNMMKEDLI
//

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