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Database: UniProt
Entry: YCGR_NITEC
LinkDB: YCGR_NITEC
Original site: YCGR_NITEC 
ID   YCGR_NITEC              Reviewed;         269 AA.
AC   Q0AI13;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   05-JUL-2017, entry version 64.
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=Neut_0749;
OS   Nitrosomonas eutropha (strain C91).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C91;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M.,
RA   Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium,
RT   Nitrosomonas eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59019.1; -; Genomic_DNA.
DR   RefSeq; WP_011633844.1; NC_008344.1.
DR   ProteinModelPortal; Q0AI13; -.
DR   SMR; Q0AI13; -.
DR   STRING; 335283.Neut_0749; -.
DR   EnsemblBacteria; ABI59019; ABI59019; Neut_0749.
DR   KEGG; net:Neut_0749; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000118572; -.
DR   OMA; YVQRREY; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000001966; 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    269       Flagellar brake protein YcgR.
FT                                /FTId=PRO_0000395279.
FT   DOMAIN      134    254       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   269 AA;  30105 MW;  1EA4C6DA316BB518 CRC64;
     MAILQTFSEQ TISSARASDI KEPDYSVNSR PEICFFLNGI MEEKSLISLY LARDSHSAIL
     SSILAVDPQQ KLLIMDYGIN ETLNQIALKR GYLRCITSHN QIRIEFDCDN LQRVQFEGRH
     AFSADIPESL KRLQRRNFYR VTTSITNPAV CTIPLLRAAD EAPVVYSLLD ISCGGMALID
     QPDADTLLKA GTTLEHCRID LPGDGNLFSS IEASIQIAYV GTVILNNGNT CPRIGCEFIN
     LPEKSRLLIQ RYITKLEQQA RKLETESGF
//
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