ID YCGR_THIDA Reviewed; 255 AA.
AC Q3SIH8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Flagellar brake protein YcgR {ECO:0000255|HAMAP-Rule:MF_01457};
DE AltName: Full=Cyclic di-GMP binding protein YcgR {ECO:0000255|HAMAP-Rule:MF_01457};
GN Name=ycgR {ECO:0000255|HAMAP-Rule:MF_01457}; OrderedLocusNames=Tbd_1597;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97550.1; -; Genomic_DNA.
DR RefSeq; WP_011312109.1; NC_007404.1.
DR AlphaFoldDB; Q3SIH8; -.
DR SMR; Q3SIH8; -.
DR STRING; 292415.Tbd_1597; -.
DR DNASU; 3672982; -.
DR KEGG; tbd:Tbd_1597; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_086025_0_0_4; -.
DR OrthoDB; 5572581at2; -.
DR Proteomes; UP000008291; Chromosome.
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; c-di-GMP; Nucleotide-binding; Reference proteome.
FT CHAIN 1..255
FT /note="Flagellar brake protein YcgR"
FT /id="PRO_0000395288"
FT DOMAIN 130..245
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ SEQUENCE 255 AA; 28229 MW; 89C25AE785744456 CRC64;
MSSSPPQHDL GHCDGDDFLA RYTLHSRAEI LFQLRALQKR KVLVNLDLSE SRQIIVTSVL
AVNEADNTVV LDSARGDALN NELMSGKGAE FVAQLDGVSI SFSIGAVSLC EYEKLPALRI
PVPTSLIRLQ RREHFRVPLP IANPVKCIVP SPWEESKEQI TTHLVDIGCG GVALTDIGAR
LGTESGRLLR GCRLLLPETD VVVTTLEIRN SAQIRLQNGS FQTRLGCKFV DLPNDMAAHL
QRFVMNIERA RRNRL
//
