YCGR1_PARPJ
ID YCGR1_PARPJ Reviewed; 257 AA.
AC B2T792;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Flagellar brake protein YcgR 1 {ECO:0000255|HAMAP-Rule:MF_01457};
DE AltName: Full=Cyclic di-GMP binding protein YcgR 1 {ECO:0000255|HAMAP-Rule:MF_01457};
GN Name=ycgR1 {ECO:0000255|HAMAP-Rule:MF_01457}; OrderedLocusNames=Bphyt_3785;
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., 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 swarming
CC in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner.
CC Binds 1 c-di-GMP dimer per subunit. Increasing levels of c-di-GMP lead
CC to decreased motility. {ECO:0000255|HAMAP-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}.
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DR EMBL; CP001052; ACD18173.1; -; Genomic_DNA.
DR RefSeq; WP_012434699.1; NC_010681.1.
DR AlphaFoldDB; B2T792; -.
DR SMR; B2T792; -.
DR STRING; 398527.Bphyt_3785; -.
DR EnsemblBacteria; ACD18173; ACD18173; Bphyt_3785.
DR KEGG; bpy:Bphyt_3785; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_086025_0_0_4; -.
DR OMA; REYFRVN; -.
DR OrthoDB; 1084216at2; -.
DR Proteomes; UP000001739; Chromosome 1.
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 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_PilZN.
DR Pfam; PF07238; PilZ; 1.
DR Pfam; PF07317; YcgR; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; c-di-GMP; Nucleotide-binding.
FT CHAIN 1..257
FT /note="Flagellar brake protein YcgR 1"
FT /id="PRO_0000395267"
FT DOMAIN 133..246
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 28787 MW; 3E7F475CF6FCC36D CRC64;
MDTTQSNGQT DTQGQLHAQT AEGGNDFGRR NPLEIGVQLR NLVNRGDFLT VQYAGGQLVT
RLLEVDVRGR TFTFDWGALS DQNRGLLGAP RCQFHAQPDG VRVEFATATP RETRFEGLPA
FEADFPEVLF YVQRREYFRV DAPILDPYVC SGRLPEGDTF RFEVHDLSLG GVGMRTADER
VAELPMGTRL LDCELVLGAL GRLSLDLQLV SHRSTALPNG TQRYQLGFRF LTLPGSAENT
LQRLITQLEM KRRSLVR