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Database: UniProt
Entry: F9ZLJ1_ACICS
LinkDB: F9ZLJ1_ACICS
Original site: F9ZLJ1_ACICS 
ID   F9ZLJ1_ACICS            Unreviewed;       442 AA.
AC   F9ZLJ1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=diguanylate cyclase {ECO:0000256|ARBA:ARBA00012528};
DE            EC=2.7.7.65 {ECO:0000256|ARBA:ARBA00012528};
GN   OrderedLocusNames=Atc_1092 {ECO:0000313|EMBL:AEK57741.1};
OS   Acidithiobacillus caldus (strain SM-1).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK57741.1, ECO:0000313|Proteomes:UP000006135};
RN   [1] {ECO:0000313|EMBL:AEK57741.1, ECO:0000313|Proteomes:UP000006135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:AEK57741.1,
RC   ECO:0000313|Proteomes:UP000006135};
RX   PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA   You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA   Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT   "Unraveling the Acidithiobacillus caldus complete genome and its central
RT   metabolisms for carbon assimilation.";
RL   J. Genet. Genomics 38:243-252(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 GTP = 3',3'-c-di-GMP + 2 diphosphate; Xref=Rhea:RHEA:24898,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58805; EC=2.7.7.65;
CC         Evidence={ECO:0000256|ARBA:ARBA00034247};
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DR   EMBL; CP002573; AEK57741.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9ZLJ1; -.
DR   STRING; 990288.Atc_1092; -.
DR   KEGG; acu:Atc_1092; -.
DR   HOGENOM; CLU_000445_11_4_6; -.
DR   OMA; GAHRNIH; -.
DR   OrthoDB; 5293332at2; -.
DR   Proteomes; UP000006135; Chromosome.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45138:SF9; DIGUANYLATE CYCLASE DGCM-RELATED; 1.
DR   PANTHER; PTHR45138; REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEM; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT   DOMAIN          143..209
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          214..266
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          298..432
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   442 AA;  49137 MW;  07635796944FC737 CRC64;
     MRTDGTPSEG SDYISALMNL GGLDVLRICP SPHVILNKRR IIFLNTAAMA LLDGSEAEEF
     LHKDIIEFVH PLDQELVLYR FSALTESHPK NAPTLIRLRT RTGAIRAVVV SSATTRVNGL
     RIDLASGTEV TELLKMDAAL KASEENFQRL FENMHDVFYR TNERQELVMV GPGSMRMLGY
     TVEEVLGRPA ADFYLVPEER SLVVEAIQKH GEIRDHPARL RHKDGRVVHV AITSRALKGA
     GGELLGVEGI FRDVTAEVEA KAALTRLATW DDLTDTLNRR AFLEQTGKYI RHLRRYPEES
     LLVIVDLDHF KAVNDRFGHL AGDKVLRTTA EIIRDVLRST DLFGRLGGDE FAIVFRKCCP
     EEGYDILGRI LSRICGTEVA LSGREHVCLS VSLGATPLLA EDQPTALALA RADRALYWAK
     AQGRGRCAFA PIDGEPFLPS YP
//
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