ID   A0A081G2P7_9GAMM        Unreviewed;       124 AA.
AC   A0A081G2P7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Cyclic diguanosine monophosphate-binding protein {ECO:0000256|PIRNR:PIRNR028141};
DE            Short=c-di-GMP-binding protein {ECO:0000256|PIRNR:PIRNR028141};
DE   AltName: Full=Pilz domain-containing protein {ECO:0000256|PIRNR:PIRNR028141};
GN   ORFNames=ADIMK_0754 {ECO:0000313|EMBL:KEA65052.1};
OS   Marinobacterium lacunae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA65052.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA65052.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA65052.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR028141}.
CC   -!- SUBUNIT: Monomer in both c-di-GMP-bound and free forms.
CC       {ECO:0000256|PIRNR:PIRNR028141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEA65052.1}.
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DR   EMBL; JMQN01000013; KEA65052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081G2P7; -.
DR   STRING; 1232683.ADIMK_0754; -.
DR   PATRIC; fig|1232683.4.peg.746; -.
DR   eggNOG; ENOG5032YUI; Bacteria.
DR   Proteomes; UP000028252; Unassembled WGS sequence.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
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.
DR   SUPFAM; SSF141371; PilZ domain-like; 1.
PE   4: Predicted;
KW   c-di-GMP {ECO:0000256|PIRNR:PIRNR028141};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR028141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028252}.
FT   DOMAIN          7..103
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
SQ   SEQUENCE   124 AA;  13762 MW;  059161D92874754C CRC64;
     MTATQDERRR FSRIRFDAGC ELHTDAGPVE VQLVDISLRG ALIESTQPLA LGLDGKAELH
     IYLASDILIR MPGSVTHLSG TQYGFRAGDM DIESISHLRR LVELNLGDEA MLERELEALF
     PPNT
//