ID   DGCP_PSEAE              Reviewed;         671 AA.
AC   Q9HT84;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Diguanylate cyclase DgcP {ECO:0000303|PubMed:25118352};
DE            EC=2.7.7.65 {ECO:0000269|PubMed:25809128};
GN   Name=dgcP; OrderedLocusNames=PA5487;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PAK;
RX   PubMed=25118352; DOI=10.1111/1462-2920.12422;
RA   Nicastro G.G., Kaihami G.H., Pereira T.O., Meireles D.A., Groleau M.C.,
RA   Deziel E., Baldini R.L.;
RT   "Cyclic-di-GMP levels affect Pseudomonas aeruginosa fitness in the presence
RT   of imipenem.";
RL   Environ. Microbiol. 16:1321-1333(2014).
RN   [3]
RP   FUNCTION AS A DIGUANYLATE CYCLASE, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND DOMAIN.
RC   STRAIN=PAK;
RX   PubMed=25809128; DOI=10.1111/1462-2920.12856;
RA   Aragon I.M., Perez-Mendoza D., Moscoso J.A., Faure E., Guery B.,
RA   Gallegos M.T., Filloux A., Ramos C.;
RT   "Diguanylate cyclase DgcP is involved in plant and human Pseudomonas spp.
RT   infections.";
RL   Environ. Microbiol. 17:4332-4351(2015).
CC   -!- FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the
CC       condensation of 2 GTP molecules (PubMed:25809128). Cyclic-di-GMP is a
CC       second messenger which controls cell surface-associated traits in
CC       bacteria (PubMed:25118352). Localizes at the cell poles through
CC       interaction with FimV where it increases the local pools of c-di-GMP
CC       (By similarity). {ECO:0000250|UniProtKB:A0A0H2ZJS2,
CC       ECO:0000269|PubMed:25118352, ECO:0000269|PubMed:25809128}.
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:0000269|PubMed:25809128};
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31129}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:A0A0H2ZJS2}. Note=Localizes at the cell poles in
CC       a FimV-dependent manner. {ECO:0000250|UniProtKB:A0A0H2ZJS2}.
CC   -!- DOMAIN: The GGEEF domain is required for function.
CC       {ECO:0000269|PubMed:25809128}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant leads to a reduction in virulence
CC       that is reflected by decreased bacterial dissemination, enhanced
CC       bacterial clearance and reduced host lung injury. It also results in
CC       increased swimming motility of approximatly 1.5-fold increase, and a 2-
CC       fold decrease in biofilm formation. {ECO:0000269|PubMed:25809128}.
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DR   EMBL; AE004091; AAG08872.1; -; Genomic_DNA.
DR   PIR; F82960; F82960.
DR   RefSeq; NP_254174.1; NC_002516.2.
DR   RefSeq; WP_003114121.1; NZ_QZGE01000012.1.
DR   AlphaFoldDB; Q9HT84; -.
DR   SMR; Q9HT84; -.
DR   STRING; 287.DR97_2865; -.
DR   PaxDb; Q9HT84; -.
DR   PRIDE; Q9HT84; -.
DR   EnsemblBacteria; AAG08872; AAG08872; PA5487.
DR   GeneID; 877705; -.
DR   KEGG; pae:PA5487; -.
DR   PATRIC; fig|208964.12.peg.5752; -.
DR   PseudoCAP; PA5487; -.
DR   HOGENOM; CLU_025058_0_0_6; -.
DR   OMA; EACPFHF; -.
DR   PhylomeDB; Q9HT84; -.
DR   BioCyc; PAER208964:G1FZ6-5614-MON; -.
DR   BRENDA; 2.7.7.65; 5087.
DR   UniPathway; UPA00599; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0052621; F:diguanylate cyclase activity; IDA:PseudoCAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR   GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..671
FT                   /note="Diguanylate cyclase DgcP"
FT                   /id="PRO_0000450451"
FT   REGION          204..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..298
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;  73999 MW;  3C99919EA2CAD743 CRC64;
     MSRDDVQRWK DKYLENIEQQ ERLQRRWDAR IDLLRRGLVR SSLAAEGSDK AVDQCMKELR
     EILRRDDMDA GLSGLIPRLE KAVLDSEQRR QQRTQQNIDA LGELAQQLLA LDLPRELRKP
     LKQFARDIEE RARQSREIPI LLSELSRLQR QALAERKGGD AEDGRPSLLQ RLFGGKESET
     TAEPSASVPS VVAASNTPIQ PAAAAPSLPV AEHDEAPGGP PQPLPARTVA AIESAPAGWV
     GVAERGEPNQ ILLDEPREIW LDSLPLPAGL SFSETLEEAG AEPSPAMPAD 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 EGNEAGEAVF ERADQALYRA
     KRAGRDRLEV A