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Database: UniProt
Entry: G8QG88_DECSP
LinkDB: G8QG88_DECSP
Original site: G8QG88_DECSP 
ID   G8QG88_DECSP            Unreviewed;       270 AA.
AC   G8QG88;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUL-2017, entry version 37.
DE   RecName: Full=Flagellar brake protein YcgR {ECO:0000256|HAMAP-Rule:MF_01457};
DE   AltName: Full=Cyclic di-GMP binding protein YcgR {ECO:0000256|HAMAP-Rule:MF_01457};
GN   Name=ycgR {ECO:0000256|HAMAP-Rule:MF_01457};
GN   OrderedLocusNames=Dsui_1776 {ECO:0000313|EMBL:AEV26161.1};
OS   Dechlorosoma suillum (strain ATCC BAA-33 / DSM 13638 / PS) (Azospira
OS   oryzae).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azospira.
OX   NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV26161.1, ECO:0000313|Proteomes:UP000005633};
RN   [1] {ECO:0000313|EMBL:AEV26161.1, ECO:0000313|Proteomes:UP000005633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC   {ECO:0000313|Proteomes:UP000005633};
RX   PubMed=22535943; DOI=10.1128/JB.00124-12;
RA   Byrne-Bailey K.G., Coates J.D.;
RT   "Complete genome sequence of the anaerobic perchlorate-reducing
RT   bacterium Azospira suillum strain PS.";
RL   J. Bacteriol. 194:2767-2768(2012).
CC   -!- FUNCTION: Acts as a flagellar brake, regulating swimming and
CC       swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-
CC       dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing
CC       levels of c-di-GMP lead to decreased motility. {ECO:0000256|HAMAP-
CC       Rule:MF_01457}.
CC   -!- SUBUNIT: Monomer. Interacts with the flagellar basal bodies.
CC       {ECO:0000256|HAMAP-Rule:MF_01457}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|HAMAP-Rule:MF_01457}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000256|HAMAP-
CC       Rule:MF_01457}.
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DR   EMBL; CP003153; AEV26161.1; -; Genomic_DNA.
DR   RefSeq; WP_014236860.1; NC_016616.1.
DR   STRING; 640081.Dsui_1776; -.
DR   EnsemblBacteria; AEV26161; AEV26161; Dsui_1776.
DR   KEGG; dsu:Dsui_1776; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   OMA; RYIFRID; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000005633; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.30.110.10; -; 1.
DR   HAMAP; MF_01457; YcgR; 1.
DR   InterPro; IPR009875; PilZ_domain.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR023787; T3SS_YcgR.
DR   InterPro; IPR009926; T3SS_YcgR_N.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF07317; YcgR; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|HAMAP-Rule:MF_01457};
KW   c-di-GMP {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005633};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005633};
KW   Transferase {ECO:0000313|EMBL:AEV26161.1}.
FT   DOMAIN       31    137       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      139    256       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   270 AA;  30139 MW;  888D7A9578B43AD2 CRC64;
     MTDKASEPLE PEAHPVPHHL DVEDDDNYSR YLLYSKAEIL FVLKALVQKG VMITVYFDGG
     NSFLLTSLNH IGADGNSLIF DYGSDDEMNR RALQADKLVF TTTLDKVKIQ FSLKGLTQTT
     FEGRTAFGGK LPETLLRLQR REYYRLTTPI ANPIKVSVDV ILADGTKTTI EANMLDISGG
     GIGLMLPLSM GETFAIGNVF RDCKFTLPEE GQLVTALSVR NSFPVTTKTG SQYLRIGCEY
     VDLPGTRLTM IQRYITRIER ERKARISGLE
//
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