(data stored in ACNUC7421 zone)

SWISSPROT: YCGR2_PARPJ

ID   YCGR2_PARPJ             Reviewed;         257 AA.
AC   B2TD41;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   RecName: Full=Flagellar brake protein YcgR 2 {ECO:0000255|HAMAP-Rule:MF_01457};
DE   AltName: Full=Cyclic di-GMP binding protein YcgR 2 {ECO:0000255|HAMAP-Rule:MF_01457};
GN   Name=ycgR2 {ECO:0000255|HAMAP-Rule:MF_01457};
GN   OrderedLocusNames=Bphyt_4582;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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:0000255|HAMAP-
CC       Rule:MF_01457}.
CC   -!- SUBUNIT: Monomer. Interacts with the flagellar basal bodies.
CC       {ECO:0000255|HAMAP-Rule:MF_01457}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000255|HAMAP-Rule:MF_01457}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000255|HAMAP-
CC       Rule:MF_01457}.
DR   EMBL; CP001053; ACD18955.1; -; Genomic_DNA.
DR   RefSeq; WP_012426469.1; NC_010676.1.
DR   SMR; B2TD41; -.
DR   STRING; 398527.Bphyt_4582; -.
DR   EnsemblBacteria; ACD18955; ACD18955; Bphyt_4582.
DR   KEGG; bpy:Bphyt_4582; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000265609; -.
DR   OMA; RYIFRID; -.
DR   OrthoDB; 1084216at2; -.
DR   Proteomes; UP000001739; Chromosome 2.
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;
DR   PRODOM; B2TD41.
DR   SWISS-2DPAGE; B2TD41.
KW   Bacterial flagellum; c-di-GMP; Complete proteome; Nucleotide-binding.
FT   CHAIN         1    257       Flagellar brake protein YcgR 2.
FT                                /FTId=PRO_0000395268.
FT   DOMAIN      131    244       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   257 AA;  28281 MW;  F365DCCCF690BEE6 CRC64;
     MIADLSLDAD VAEQTQQTLG ADSNFAQRHP LQIAVCLRQL VAGQDFVTVE FGGRQIVTQI
     LDVDSRNARF VFDAGSVADD NDALPSARQL TFRSLPGGIR TEFTTFDATP TQFDGLPAFE
     APLPTVLHYV QRREFFRVQT PVLDPYIASG RYADGGSFRL ELLDLSLGGI ALKTADERFG
     SLERGTVLRD VALQLGGFGM LRLDLEIVAP RQVSTAKGDR RFVIGCKFVA TPGPAERTLQ
     RVVTQLETRR QALTPRR
//

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