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Database: UniProt
Entry: A0A0X8GQE3_9BURK
LinkDB: A0A0X8GQE3_9BURK
Original site: A0A0X8GQE3_9BURK 
ID   A0A0X8GQE3_9BURK        Unreviewed;       247 AA.
AC   A0A0X8GQE3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-MAR-2018, entry version 12.
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=VN23_19210 {ECO:0000313|EMBL:AMC36565.1};
OS   Janthinobacterium sp. B9-8.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36565.1, ECO:0000313|Proteomes:UP000069577};
RN   [1] {ECO:0000313|EMBL:AMC36565.1, ECO:0000313|Proteomes:UP000069577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-8 {ECO:0000313|EMBL:AMC36565.1,
RC   ECO:0000313|Proteomes:UP000069577};
RA   Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT   "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT   isolated from low temperature sewage.";
RL   Submitted (JAN-2016) 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; CP014222; AMC36565.1; -; Genomic_DNA.
DR   RefSeq; WP_046351755.1; NZ_CP014222.1.
DR   EnsemblBacteria; AMC36565; AMC36565; VN23_19210.
DR   KEGG; jab:VN23_19210; -.
DR   Proteomes; UP000069577; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01457; YcgR; 1.
DR   InterPro; IPR009875; PilZ_domain.
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:UP000069577};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069577}.
FT   DOMAIN       18    116       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      125    237       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   247 AA;  27497 MW;  0328F8E21A3FE519 CRC64;
     MQQPPTLEPV FVSDTGPYLV SASIEIKYLL KQLLENGEII CLYPAGKREP FAISTLLSIN
     DNELLFDASN DIVTNAALIK DARMLLVGVV NKVKVQFELP DATLVAYEGR TAIRSGGPVQ
     TLRMQRRDFY RLDIPMSQKV DCVVPLGDGR QTELLVTDIS LGGLSLLGVS PDLPMVVGDT
     LHNCQIQLLD VGVIEIDMQV CIVIDVTLRN GVKTQRIGCR FFDLPGKMQT LIQRFINKIE
     RQRISRE
//
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