ID Q8EHJ4_SHEON Unreviewed; 130 AA.
AC Q8EHJ4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=SO_1227 {ECO:0000313|EMBL:AAN54295.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54295.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN54295.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN54295.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014299; AAN54295.1; -; Genomic_DNA.
DR RefSeq; NP_716850.1; NC_004347.2.
DR AlphaFoldDB; Q8EHJ4; -.
DR STRING; 211586.SO_1227; -.
DR PaxDb; 211586-SO_1227; -.
DR KEGG; son:SO_1227; -.
DR PATRIC; fig|211586.12.peg.1178; -.
DR eggNOG; ENOG5032YUI; Bacteria.
DR HOGENOM; CLU_146776_0_1_6; -.
DR OrthoDB; 5298508at2; -.
DR PhylomeDB; Q8EHJ4; -.
DR BioCyc; SONE211586:G1GMP-1137-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
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:UP000008186}.
FT DOMAIN 10..106
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 130 AA; 14705 MW; 80656696C4BBE56A CRC64;
MKDKALVIDE RRHFSRILFA ASASIHQGEN QWQTTILDLS LNGALVEEPV RFSHTGEPIT
LSFTLQGSDI ELQMETELVH QRNHQLGLKC NIIDVDSISH LKRIVELNLG DASILNRELA
LFVEKHHSAD
//
