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Database: UniProt
Entry: A0A177P5V1_9GAMM
LinkDB: A0A177P5V1_9GAMM
Original site: A0A177P5V1_9GAMM 
ID   A0A177P5V1_9GAMM        Unreviewed;       251 AA.
AC   A0A177P5V1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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=A1356_13480 {ECO:0000313|EMBL:OAI25472.1};
OS   Methylomonas koyamae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=702114 {ECO:0000313|EMBL:OAI25472.1, ECO:0000313|Proteomes:UP000077734};
RN   [1] {ECO:0000313|EMBL:OAI25472.1, ECO:0000313|Proteomes:UP000077734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-49807 {ECO:0000313|EMBL:OAI25472.1,
RC   ECO:0000313|Proteomes:UP000077734};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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:OAI25472.1}.
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DR   EMBL; LUUL01000081; OAI25472.1; -; Genomic_DNA.
DR   RefSeq; WP_064027725.1; NZ_LUUL01000081.1.
DR   EnsemblBacteria; OAI25472; OAI25472; A1356_13480.
DR   Proteomes; UP000077734; 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-HAMAP.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:UniProtKB-HAMAP.
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:UP000077734};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457}.
FT   DOMAIN        7    111       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      115    239       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   251 AA;  28663 MW;  F898776CC82F75BB CRC64;
     MEKESDYLVR NAKLVYGHLT DLVKKKCIIS AHFGEHNQSF LTTIIDLDQK ANLLTLDVAP
     TELLNKQLLN SPKVLFRTEF DGIKVSFRGK SIKKSQSDGH PVFAMPIPDA IFWMQRRQFY
     RIKIPLSHIN SVCQIEFTAP RDPDNAEPVT SKGVFRLVDL SISGFAFLNP DPQFDKFLNP
     EDKHEGCMIY LHDGGQAKIS FEIKEITKVR ATMTATQLRI GCRFTDIPQA FESNIQRYMQ
     DIEIQQKNLA G
//
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