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Database: UniProt
Entry: YCGR_THASP
LinkDB: YCGR_THASP
Original site: YCGR_THASP 
ID   YCGR_THASP              Reviewed;         263 AA.
AC   C4KAR8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 46.
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=Tmz1t_2895;
OS   Thauera sp. (strain MZ1T).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Thauera.
OX   NCBI_TaxID=85643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001281; ACR01494.1; -; Genomic_DNA.
DR   RefSeq; WP_004321902.1; NC_011662.2.
DR   ProteinModelPortal; C4KAR8; -.
DR   SMR; C4KAR8; -.
DR   STRING; 85643.Tmz1t_2895; -.
DR   EnsemblBacteria; ACR01494; ACR01494; Tmz1t_2895.
DR   KEGG; tmz:Tmz1t_2895; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000220069; -.
DR   OMA; YVQRREY; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000002186; 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    263       Flagellar brake protein YcgR.
FT                                /FTId=PRO_0000395286.
FT   DOMAIN      133    250       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   263 AA;  28517 MW;  DB65BE9C344E849A CRC64;
     MAELSTPSPA SPAPLDGGRG DELEKFTLRG ARQILQLLQD LITHRGLITA HTGGGHSFMT
     AVLKVDEERG RVVLDPSPDP QANRRALAAP RLTCVTQLDG IRIQFPLVGL GEGQDKGRPA
     LFAPLPAEML RLQRREFYRL QVPLAHELSC LLKAEDLARK PVEVSARVID IGAGGVAVVV
     PTGAAEFVIG GTLPACRLAL PDGEPIELDL EVRNLNRQTQ RNGTEQLRVG LRFAALPRAA
     DTRIQRYIFK TERALNAKAR GGL
//
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