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Database: UniProt
Entry: YCGR_THIDA
LinkDB: YCGR_THIDA
Original site: YCGR_THIDA 
ID   YCGR_THIDA              Reviewed;         255 AA.
AC   Q3SIH8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   30-AUG-2017, entry version 69.
DE   RecName: Full=Flagellar brake protein YcgR {ECO:0000255|HAMAP-Rule:MF_01457};
DE   AltName: Full=Cyclic di-GMP binding protein YcgR {ECO:0000255|HAMAP-Rule:MF_01457};
GN   Name=ycgR {ECO:0000255|HAMAP-Rule:MF_01457};
GN   OrderedLocusNames=Tbd_1597;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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:0000255|HAMAP-
CC       Rule:MF_01457}.
CC   -!- SUBUNIT: Monomer. Interacts with the flagellar basal bodies.
CC       {ECO:0000255|HAMAP-Rule:MF_01457}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000255|HAMAP-Rule:MF_01457}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000255|HAMAP-
CC       Rule:MF_01457}.
DR   EMBL; CP000116; AAZ97550.1; -; Genomic_DNA.
DR   RefSeq; WP_011312109.1; NC_007404.1.
DR   ProteinModelPortal; Q3SIH8; -.
DR   SMR; Q3SIH8; -.
DR   STRING; 292415.Tbd_1597; -.
DR   DNASU; 3672982; -.
DR   EnsemblBacteria; AAZ97550; AAZ97550; Tbd_1597.
DR   KEGG; tbd:Tbd_1597; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   OMA; RYIFRID; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000008291; 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:InterPro.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:InterPro.
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; c-di-GMP; Complete proteome; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    255       Flagellar brake protein YcgR.
FT                                /FTId=PRO_0000395288.
FT   DOMAIN      130    245       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   255 AA;  28229 MW;  89C25AE785744456 CRC64;
     MSSSPPQHDL GHCDGDDFLA RYTLHSRAEI LFQLRALQKR KVLVNLDLSE SRQIIVTSVL
     AVNEADNTVV LDSARGDALN NELMSGKGAE FVAQLDGVSI SFSIGAVSLC EYEKLPALRI
     PVPTSLIRLQ RREHFRVPLP IANPVKCIVP SPWEESKEQI TTHLVDIGCG GVALTDIGAR
     LGTESGRLLR GCRLLLPETD VVVTTLEIRN SAQIRLQNGS FQTRLGCKFV DLPNDMAAHL
     QRFVMNIERA RRNRL
//
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