ID I2DR57_9BURK Unreviewed; 251 AA.
AC I2DR57;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=MYA_2773 {ECO:0000313|EMBL:AFJ87133.1};
OS Burkholderia sp. KJ006.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ87133.1, ECO:0000313|Proteomes:UP000010108};
RN [1] {ECO:0000313|EMBL:AFJ87133.1, ECO:0000313|Proteomes:UP000010108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ87133.1,
RC ECO:0000313|Proteomes:UP000010108};
RX PubMed=22843575; DOI=10.1128/JB.00821-12;
RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT Strain KJ006.";
RL J. Bacteriol. 194:4432-4433(2012).
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:0000256|HAMAP-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; CP003514; AFJ87133.1; -; Genomic_DNA.
DR RefSeq; WP_014723810.1; NC_017920.1.
DR AlphaFoldDB; I2DR57; -.
DR GeneID; 69524277; -.
DR KEGG; buk:MYA_2773; -.
DR PATRIC; fig|416344.3.peg.2819; -.
DR HOGENOM; CLU_086025_0_0_4; -.
DR Proteomes; UP000010108; 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; 2.40.10.220; predicted glycosyltransferase like domains; 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; PilZN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_01457};
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636, ECO:0000256|HAMAP-Rule:MF_01457};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01457}.
FT DOMAIN 20..123
FT /note="Type III secretion system flagellar brake protein
FT YcgR PilZN"
FT /evidence="ECO:0000259|Pfam:PF07317"
FT DOMAIN 126..239
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 27810 MW; B95691B366FC5360 CRC64;
MNIETSTDPS LDAGHSGPDY ARRNPLEIGV QLRNLVNRGD FLTVQYPGGQ LVTRLLDVDV
GARTFTFDWG ALAEQNAGIL AASHCTFAAA PDGVRVEFTT GTPRETRYEG LPAFVAEFPE
VLMCIQRREY FRVDAPVVDP FQCRGKLPDG EGFVFEVQNL SLGGVGLRTI DERVETLEVG
TLLPEVELEL NGHGKLSLDL RLVSQRSTQL PNGSRRYQLG FRFMSLPGSA ENTLQRLITQ
LEMKRRSLAR A
//