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Database: UniProt
Entry: YCGR2_DECAR
LinkDB: YCGR2_DECAR
Original site: YCGR2_DECAR 
ID   YCGR2_DECAR             Reviewed;         247 AA.
AC   Q47AR4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   30-AUG-2017, entry version 62.
DE   RecName: Full=Flagellar brake protein YcgR 2 {ECO:0000255|HAMAP-Rule:MF_01457};
DE   AltName: Full=Cyclic di-GMP binding protein YcgR 2 {ECO:0000255|HAMAP-Rule:MF_01457};
GN   Name=ycgR2 {ECO:0000255|HAMAP-Rule:MF_01457};
GN   OrderedLocusNames=Daro_3338;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Azonexaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str.
RT   RCB: indications of a surprisingly complex life-style and cryptic
RT   anaerobic pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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; CP000089; AAZ48067.1; -; Genomic_DNA.
DR   RefSeq; WP_011289063.1; NC_007298.1.
DR   ProteinModelPortal; Q47AR4; -.
DR   SMR; Q47AR4; -.
DR   STRING; 159087.Daro_3338; -.
DR   EnsemblBacteria; AAZ48067; AAZ48067; Daro_3338.
DR   KEGG; dar:Daro_3338; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000133745; -.
DR   OMA; YVQRREY; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000000550; 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    247       Flagellar brake protein YcgR 2.
FT                                /FTId=PRO_0000395272.
FT   DOMAIN      124    237       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   247 AA;  27499 MW;  C0C2DAA623BDAA70 CRC64;
     MTQIAQLSEA EIEARFRVMG TKPVAFLIAG FAKEREPFSV HFGAGGEMFL TTPLAVEPEK
     GLLIFDCSGS VESNQRFLRS DRNIFIGRPG GVHVQFTTGA AREVAHEGGK AFAVALPQYI
     VRLQRREYFR VETPRVNPLE FFGRLADGSL LKLPVHDISI SGLGVDAAVL PEGVMPGVVL
     PNCHFSLPGD GKDMFFSATI RNTLELERRS GARHWRIGMQ FNDLSSGDET RIQRYIARIE
     RERHELS
//
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