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Database: UniProt
Entry: R4YV53_OLEAN
LinkDB: R4YV53_OLEAN
Original site: R4YV53_OLEAN 
ID   R4YV53_OLEAN            Unreviewed;       134 AA.
AC   R4YV53;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=OLEAN_C34230 {ECO:0000313|EMBL:CCK77599.1};
OS   Oleispira antarctica RB-8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oleispira.
OX   NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK77599.1, ECO:0000313|Proteomes:UP000032749};
RN   [1] {ECO:0000313|EMBL:CCK77599.1, ECO:0000313|Proteomes:UP000032749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23877221; DOI=10.1038/ncomms3156;
RA   Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA   Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., Langer I.,
RA   Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., Ciordia S.,
RA   Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., Kim Y.,
RA   Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., Reva O.N.,
RA   Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., Yakunin A.F.,
RA   Yakimov M.M., Golyshina O.V., Reinhardt R., Golyshin P.N.;
RT   "Genome sequence and functional genomic analysis of the oil-degrading
RT   bacterium Oleispira antarctica.";
RL   Nat. Commun. 4:2156-2156(2013).
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}.
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DR   EMBL; FO203512; CCK77599.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4YV53; -.
DR   STRING; 698738.OLEAN_C34230; -.
DR   KEGG; oai:OLEAN_C34230; -.
DR   HOGENOM; CLU_146776_0_0_6; -.
DR   OrthoDB; 5298508at2; -.
DR   Proteomes; UP000032749; 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:UP000032749}.
FT   DOMAIN          11..113
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
SQ   SEQUENCE   134 AA;  15117 MW;  1FBFF41940491C27 CRC64;
     MSDQNLENTH ENRRFRRISF VEAVQVVSED VDGAEACSWE AQCIDISMLG MLLAVPEGFP
     LVIGTPFEVQ LILAEDVMIE MPCTLVHIEG HRAGFRSEMM SIDSLTNLRR LLELNLADNI
     EVERELAELI KQSS
//
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