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Database: UniProt
Entry: A0A0G3BWS0_9BURK
LinkDB: A0A0G3BWS0_9BURK
Original site: A0A0G3BWS0_9BURK 
ID   A0A0G3BWS0_9BURK        Unreviewed;       262 AA.
AC   A0A0G3BWS0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
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   ORFNames=AAW51_4299 {ECO:0000313|EMBL:AKJ30990.1};
OS   [Polyangium] brachysporum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ30990.1, ECO:0000313|Proteomes:UP000035352};
RN   [1] {ECO:0000313|EMBL:AKJ30990.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ30990.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
RL   Submitted (MAY-2015) 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: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; CP011371; AKJ30990.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKJ30990; AKJ30990; AAW51_4299.
DR   KEGG; pbh:AAW51_4299; -.
DR   PATRIC; fig|413882.6.peg.4494; -.
DR   Proteomes; UP000035352; 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-UniRule.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-UniRule.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:UniProtKB-UniRule.
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   Cell projection {ECO:0000313|EMBL:AKJ30990.1};
KW   Cilium {ECO:0000313|EMBL:AKJ30990.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035352};
KW   Flagellum {ECO:0000313|EMBL:AKJ30990.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035352}.
FT   DOMAIN       27    134       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      136    249       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   262 AA;  29117 MW;  C6F7B5BB767D107A CRC64;
     MFHHAMATPS NPQAHDQAED AAKLDDFRIT GRFEIATLLQ QLVQQRALVT IATPEGACYT
     TNVWEVEPDK GVMRFSADRL DPQLQRVLDA GDAVAVAYLD SIKIQFDVEG LVQVHAGQTA
     ATTLNCVLPD ELFRFQRRTS FRVRPLLNSP PVASFRHPAI AEMRLELRVL DVSIGGIALF
     IPENVPVVEP GTQIGQVSVE LDAETRFNAT LRVAHASSML DNSKGMRIGC ELENLNGEAL
     RSLQRYIDQT QKRRRLMALD DA
//
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