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Database: UniProt
Entry: A0A085FCA9_9BURK
LinkDB: A0A085FCA9_9BURK
Original site: A0A085FCA9_9BURK 
ID   A0A085FCA9_9BURK        Unreviewed;       249 AA.
AC   A0A085FCA9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 24.
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   ECO:0000313|EMBL:KFC69104.1};
GN   ORFNames=FG94_02659 {ECO:0000313|EMBL:KFC69104.1};
OS   Massilia sp. LC238.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC69104.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC69104.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC69104.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) 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:KFC69104.1}.
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DR   EMBL; JNNN01000048; KFC69104.1; -; Genomic_DNA.
DR   RefSeq; WP_036212343.1; NZ_JNNN01000048.1.
DR   EnsemblBacteria; KFC69104; KFC69104; FG94_02659.
DR   PATRIC; fig|1502852.3.peg.2619; -.
DR   Proteomes; UP000028601; 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:UP000028601};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457}.
FT   DOMAIN       12    118       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      120    235       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   249 AA;  28035 MW;  FA66BCDDCA546A83 CRC64;
     MNDQELENWH DYEVESRREI VQLLRQIGEK HQLVRMLVKG EADVCVTTVL DVDADTNSLV
     LDRSIERMQN ERIVEAGKVR CETTLDKIRI LFTAENLRPT LFEGEAALRA DIPPSLIRLQ
     RREYYRMETP VSNPVRAILP LPLEAGAGTG VFPLHDISCG GIAVLDNKLQ LDTTIGAQLP
     NCRIELPEIG PVTVTLEVRN SLDLTLLNNK TNRRIGLQFV DMSRGGMAGV QRYITKLERE
     RNARLAGLA
//
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