ID   DGCP_PSEAB              Reviewed;         671 AA.
AC   A0A0H2ZJS2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Diguanylate cyclase DgcP {ECO:0000303|PubMed:32080219};
DE            EC=2.7.7.65 {ECO:0000250|UniProtKB:Q9HT84};
GN   Name=dgcP; OrderedLocusNames=PA14_72420;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   FUNCTION, INTERACTION WITH FIMV, AND SUBCELLULAR LOCATION.
RX   PubMed=32080219; DOI=10.1038/s41598-020-59536-9;
RA   Nicastro G.G., Kaihami G.H., Pulschen A.A., Hernandez-Montelongo J.,
RA   Boechat A.L., de Oliveira Pereira T., Rosa C.G.T., Stefanello E.,
RA   Colepicolo P., Bordi C., Baldini R.L.;
RT   "c-di-GMP-related phenotypes are modulated by the interaction between a
RT   diguanylate cyclase and a polar hub protein.";
RL   Sci. Rep. 10:3077-3077(2020).
CC   -!- FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the
CC       condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger
CC       which controls cell surface-associated traits in bacteria (By
CC       similarity). Localizes at the cell poles through interaction with FimV
CC       where it increases the local pools of c-di-GMP (PubMed:32080219).
CC       {ECO:0000250|UniProtKB:Q9HT84, ECO:0000269|PubMed:32080219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC         Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58805; EC=2.7.7.65;
CC         Evidence={ECO:0000250|UniProtKB:Q9HT84};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P31129};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P31129};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC       {ECO:0000250|UniProtKB:P31129}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:32080219}. Note=Localizes at the cell poles in a
CC       FimV-dependent manner. {ECO:0000269|PubMed:32080219}.
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DR   EMBL; CP000438; ABJ14873.1; -; Genomic_DNA.
DR   RefSeq; WP_003142135.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZJS2; -.
DR   SMR; A0A0H2ZJS2; -.
DR   EnsemblBacteria; ABJ14873; ABJ14873; PA14_72420.
DR   KEGG; pau:PA14_72420; -.
DR   HOGENOM; CLU_025058_0_0_6; -.
DR   OMA; EACPFHF; -.
DR   BioCyc; PAER208963:G1G74-6093-MON; -.
DR   UniPathway; UPA00599; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01949; GGDEF; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   Pfam; PF00990; GGDEF; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   TIGRFAMs; TIGR00254; GGDEF; 1.
DR   PROSITE; PS50887; GGDEF; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; GTP-binding; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..671
FT                   /note="Diguanylate cyclase DgcP"
FT                   /id="PRO_0000450452"
FT   REGION          204..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   BINDING         549
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   BINDING         557
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   BINDING         562
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   BINDING         566
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   BINDING         592
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P31129"
FT   SITE            554
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   671 AA;  73937 MW;  7BD3A29861FF64B8 CRC64;
     MSRDDVQRWK DKYLENIEQQ ERLQRRWDAR IDLLRRGLVR SSLAAEGSDK AVDQCMKELR
     EILRRDDMDA GLSGLIPRLE KAVLDSEQRR QQRTQQNIDA LGELAQQLLA LDLPRELRKP
     LKQFARDIEE RARQSREIPI LLSELSRLQR QALAERKGGD AEDGRPSLLQ RLFGGKESET
     AAEPSASVPS VVAASNTPIQ PAAAAPSLPV AEHDEAPGGP PQPLPASRVA AIESAPAGWV
     GVAERGEPNQ ILLDEPREIW LDSLPLPAGL SFSETLEDAG AESPPAVPAD VESAPEAPAT
     PVDNLDGQAV DEAYELPPPI PEPGYSAVAP HIEASLLRLL DGLSLPSSHQ PQAEALRERI
     DGSLNWYELV PVLDDLAVLV LSLADSGQRD FEEYLRQLNE RLESFLGHLG DAHAGYTDVL
     DNARGFDQSL REQVSGLQAS VQQATDLNSL KLAVDSRLNG LLASMDEHQR EQAEHEQEVS
     GRLQALMERV NSMEQDAKAF HSHLEDQRQK ALTDPLTGLP NRAALSERLE QEVARRHRDG
     GDLLLAVLDI DHFKRINDDF GHLAGDKVLK IIAGELRKRL RQADFIARFG GEEFVVLLPA
     TSLEAGRQLL ERLRAAIAAC PFHFKGEPLS ITCSAGITAF EGNEAGEVVF ERADQALYRA
     KRAGRDRLEV A