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Database: UniProt
Entry: A0A0L0MF11_9BURK
LinkDB: A0A0L0MF11_9BURK
Original site: A0A0L0MF11_9BURK 
ID   A0A0L0MF11_9BURK        Unreviewed;       255 AA.
AC   A0A0L0MF11;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 10.
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=BVER_00970c {ECO:0000313|EMBL:KND60870.1};
OS   Candidatus Burkholderia verschuerenii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=242163 {ECO:0000313|EMBL:KND60870.1, ECO:0000313|Proteomes:UP000036959};
RN   [1] {ECO:0000313|Proteomes:UP000036959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KND60870.1}.
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DR   EMBL; LFJJ01000041; KND60870.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND60870; KND60870; BVER_00970c.
DR   PATRIC; fig|242163.4.peg.5012; -.
DR   Proteomes; UP000036959; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000036959};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036959}.
FT   DOMAIN       25    128       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      131    245       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   255 AA;  28471 MW;  3A6835F3B70420A3 CRC64;
     MNLASTMNSN HNNDAADDDA PQVDFGRRNP LEVGVSLRNL ANRGDFLTAQ YGDAQIVTRI
     LDVDVTAHTF IFDWGGVPEH NSYVLAAQKL FFSAAPEGVR LEFTTGTPRQ TTFDGRPAFE
     MEFPPVLYYM QRREYFRVEA PVLDPYICSG SLPDGERFCF EVHDLSLGGV ALRTSDERVA
     ALELGSVIQD AELHFTTTGR VTLDIKLVSH RESKSSKGER RFTLGFKSAS MPGSAENTLQ
     RLITQLEMKR RSLSK
//
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