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Database: UniProt
Entry: A0A1B1KRT3_SERPL
LinkDB: A0A1B1KRT3_SERPL
Original site: A0A1B1KRT3_SERPL 
ID   A0A1B1KRT3_SERPL        Unreviewed;       237 AA.
AC   A0A1B1KRT3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUL-2017, entry version 7.
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:ANS43153.1};
GN   ORFNames=Q5A_013500 {ECO:0000313|EMBL:ANS43153.1};
OS   Serratia plymuthica PRI-2C.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1154756 {ECO:0000313|EMBL:ANS43153.1, ECO:0000313|Proteomes:UP000013567};
RN   [1] {ECO:0000313|EMBL:ANS43153.1, ECO:0000313|Proteomes:UP000013567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Serratia sp. PRI-2C {ECO:0000313|Proteomes:UP000013567};
RX   PubMed=22815440; DOI=10.1128/JB.00679-12;
RA   Garbeva P., van Elsas J.D., de Boer W.;
RT   "Draft genome sequence of the antagonistic rhizosphere bacterium
RT   Serratia plymuthica strain PRI-2C.";
RL   J. Bacteriol. 194:4119-4120(2012).
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; CP015613; ANS43153.1; -; Genomic_DNA.
DR   RefSeq; WP_006319632.1; NZ_CP015613.1.
DR   EnsemblBacteria; ANS43153; ANS43153; Q5A_013500.
DR   KEGG; sply:Q5A_013500; -.
DR   KO; K21087; -.
DR   Proteomes; UP000013567; 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-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   Cell projection {ECO:0000313|EMBL:ANS43153.1};
KW   Cilium {ECO:0000313|EMBL:ANS43153.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013567};
KW   Flagellum {ECO:0000313|EMBL:ANS43153.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457}.
FT   DOMAIN        9    105       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      108    225       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   237 AA;  27085 MW;  3E1B50BEDA57E3A4 CRC64;
     MEHNDNGLFI KRERFEVLAI LREICKQRTP LRVVNQQQQF QSLLLSVGPD NIVFSGDKAD
     SVADGEFTVV IESHDAKIEF TVGQPKFTDQ LGVQVCSTCL PKELVYIQRR RQFRVTTPHW
     RQFLCSGEYA DGTAYQLRIH DLSAGGVGLR FDGPLPDKLQ PGILFKKALL DLGSYGSFKV
     NMELMVINED QELDEDDKPV HFSRLSCRFI NLGLAMERKI QSAVFAFELD FNKKKKR
//
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