CDGBP_PSEAE
ID CDGBP_PSEAE Reviewed; 125 AA.
AC Q9HVI1;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cyclic diguanosine monophosphate-binding protein PA4608 {ECO:0000303|PubMed:17096419, ECO:0000303|PubMed:21280119, ECO:0000303|PubMed:21310957};
DE Short=c-di-GMP-binding protein PA4608 {ECO:0000303|PubMed:17096419, ECO:0000303|PubMed:21280119, ECO:0000303|PubMed:21310957};
DE AltName: Full=Pilz domain-containing protein PA4608 {ECO:0000303|PubMed:17096419, ECO:0000303|PubMed:21280119, ECO:0000303|PubMed:21310957};
GN OrderedLocusNames=PA4608;
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] {ECO:0000312|EMBL:AAG07996.1}
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] {ECO:0000305, ECO:0000312|PDB:1YWU}
RP STRUCTURE BY NMR (APO-FORM), FUNCTION, SUBUNIT, DOMAIN, AND C-DI-GMP
RP BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:17096419};
RX PubMed=17096419; DOI=10.1002/prot.21199;
RA Ramelot T.A., Yee A., Cort J.R., Semesi A., Arrowsmith C.H., Kennedy M.A.;
RT "NMR structure and binding studies confirm that PA4608 from Pseudomonas
RT aeruginosa is a PilZ domain and a c-di-GMP binding protein.";
RL Proteins 66:266-271(2007).
RN [3] {ECO:0000305, ECO:0000312|PDB:2L74}
RP STRUCTURE BY NMR IN COMPLEX WITH C-DI-GMP (HOLO-FORM), FUNCTION, SUBUNIT,
RP DOMAIN, AND MOTIF.
RX PubMed=21310957; DOI=10.1074/jbc.m110.209007;
RA Habazettl J., Allan M.G., Jenal U., Grzesiek S.;
RT "Solution structure of the PilZ domain protein PA4608 complex with cyclic
RT di-GMP identifies charge clustering as molecular readout.";
RL J. Biol. Chem. 286:14304-14314(2011).
RN [4] {ECO:0000305}
RP STRUCTURE BY NMR, FUNCTION, SUBUNIT, DOMAIN, MOTIF, SITE, AND MUTAGENESIS
RP OF ARG-9; ARG-13 AND GLY-40.
RX PubMed=21280119; DOI=10.1002/pro.557;
RA Shin J.S., Ryu K.S., Ko J., Lee A., Choi B.S.;
RT "Structural characterization reveals that a PilZ domain protein undergoes
RT substantial conformational change upon binding to cyclic dimeric guanosine
RT monophosphate.";
RL Protein Sci. 20:270-277(2011).
CC -!- FUNCTION: Binds the second messenger bis-(3'-5') cyclic dimeric
CC guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per
CC monomer. May play a role in bacterial second-messenger regulated
CC processes. Binding to c-di-GMP induces a conformational change of the
CC C- and N-termini resulting in the exposure of a highly negative surface
CC on one side of the protein to a possible effector protein.
CC {ECO:0000269|PubMed:17096419, ECO:0000269|PubMed:21280119,
CC ECO:0000269|PubMed:21310957}.
CC -!- SUBUNIT: Monomer in both c-di-GMP-bound and free forms.
CC {ECO:0000269|PubMed:17096419, ECO:0000269|PubMed:21280119,
CC ECO:0000269|PubMed:21310957}.
CC -!- DOMAIN: Consists of a six-stranded anti-parallel beta-barrel core
CC structure with an unstructured N-terminus in apo-form and a C-terminal
CC alpha helix. In the holo-form the C-terminal helix is displaced by the
CC ligand, thereby opening one side of the beta-barrel as a binding site,
CC and the N-terminus containing the RXXXR motif wraps around the ligand
CC and in turn ties the C-terminal helix in a loose conformation. The
CC structural rearrangement upon ligand binding creates a significant
CC change in surface charge distribution. {ECO:0000269|PubMed:17096419,
CC ECO:0000269|PubMed:21280119, ECO:0000269|PubMed:21310957}.
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DR EMBL; AE004091; AAG07996.1; -; Genomic_DNA.
DR PIR; H83068; H83068.
DR RefSeq; NP_253298.1; NC_002516.2.
DR RefSeq; WP_003094864.1; NZ_QZGE01000004.1.
DR PDB; 1YWU; NMR; -; A=1-125.
DR PDB; 2L74; NMR; -; A=1-125.
DR PDB; 5XLY; X-ray; 1.76 A; B=1-125.
DR PDB; 5Y4R; X-ray; 2.30 A; C/D=2-125.
DR PDBsum; 1YWU; -.
DR PDBsum; 2L74; -.
DR PDBsum; 5XLY; -.
DR PDBsum; 5Y4R; -.
DR AlphaFoldDB; Q9HVI1; -.
DR BMRB; Q9HVI1; -.
DR SMR; Q9HVI1; -.
DR STRING; 287.DR97_1914; -.
DR PaxDb; Q9HVI1; -.
DR PRIDE; Q9HVI1; -.
DR DNASU; 881102; -.
DR EnsemblBacteria; AAG07996; AAG07996; PA4608.
DR GeneID; 881102; -.
DR KEGG; pae:PA4608; -.
DR PATRIC; fig|208964.12.peg.4823; -.
DR PseudoCAP; PA4608; -.
DR HOGENOM; CLU_146776_0_1_6; -.
DR OMA; LGFVCRH; -.
DR PhylomeDB; Q9HVI1; -.
DR BioCyc; PAER208964:G1FZ6-4702-MON; -.
DR EvolutionaryTrace; Q9HVI1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IDA:UniProtKB.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IDA:UniProtKB.
DR InterPro; IPR027021; C-di-GMP_BP_PA4608.
DR InterPro; IPR009875; PilZ_domain.
DR Pfam; PF07238; PilZ; 1.
DR PIRSF; PIRSF028141; C-di-GMP_BP_PA4608; 1.
PE 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Nucleotide-binding; Reference proteome.
FT CHAIN 1..125
FT /note="Cyclic diguanosine monophosphate-binding protein
FT PA4608"
FT /id="PRO_0000423181"
FT DOMAIN 7..103
FT /note="PilZ"
FT /evidence="ECO:0000255"
FT MOTIF 9..13
FT /note="RXXXR motif; surrounds the surface of the c-di-GMP
FT binding site"
FT /evidence="ECO:0000269|PubMed:21280119,
FT ECO:0000269|PubMed:21310957"
FT MOTIF 35..40
FT /note="DXSXXG motif; surrounds the surface of the c-di-GMP
FT binding site"
FT /evidence="ECO:0000269|PubMed:21280119,
FT ECO:0000269|PubMed:21310957"
FT BINDING 6..13
FT /ligand="cyclic di-3',5'-guanylate"
FT /ligand_id="ChEBI:CHEBI:58805"
FT /evidence="ECO:0000269|PubMed:21310957"
FT BINDING 77
FT /ligand="cyclic di-3',5'-guanylate"
FT /ligand_id="ChEBI:CHEBI:58805"
FT /evidence="ECO:0000269|PubMed:21310957"
FT SITE 40
FT /note="Important for c-di-GMP binding"
FT MUTAGEN 9
FT /note="R->A: Abolishes c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:21280119"
FT MUTAGEN 13
FT /note="R->A: Abolishes c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:21280119"
FT MUTAGEN 40
FT /note="G->A: Abolishes c-di-GMP binding."
FT /evidence="ECO:0000269|PubMed:21280119"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2L74"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2L74"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5XLY"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 67..79
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:5XLY"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5XLY"
SQ SEQUENCE 125 AA; 14573 MW; AB6D8110967348B0 CRC64;
MSDQHDERRR FHRIAFDADS EILQGERRWE VLLHDVSLHG ILVGQPQDWN GDPQRPFEAR
LYLGLDVLIR MEISLAWARD GLLGFECQHI DLDSISHLRR LVELNLGDEE LLERELALLV
SAHDD
