ID   YCGR_LEPCP              Reviewed;         251 AA.
AC   B1Y382;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=Lcho_1014;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001013; ACB33285.1; -; Genomic_DNA.
DR   RefSeq; WP_012346047.1; NC_010524.1.
DR   AlphaFoldDB; B1Y382; -.
DR   SMR; B1Y382; -.
DR   STRING; 395495.Lcho_1014; -.
DR   EnsemblBacteria; ACB33285; ACB33285; Lcho_1014.
DR   KEGG; lch:Lcho_1014; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_0_0_4; -.
DR   OMA; RYIFRID; -.
DR   OrthoDB; 1084216at2; -.
DR   Proteomes; UP000001693; 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; 2.30.110.10; -; 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; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395276"
FT   DOMAIN          127..239
FT                   /note="PilZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ   SEQUENCE   251 AA;  27517 MW;  963F664A4BBF8044 CRC64;
     MSTQPMPLSL TDAKPGQGEY RVRAGSEIRA LLRRFADEEL PITLATPDGV SYTTCLWADD
     PERAVLVLSA DAADARVQRL IEAEEAVAVG YLDSVKIQFD LNGLMLVHGR DASALHAQFP
     REIYRFQRRD GFRVRPVGHA CPELQLRVSG PTDTELTLRV LDLSHGGLAL FLPDDQPALP
     VGTSVRAARL ALDPLTQVQV ALRVVHVAPL KESAHGSRLG CEIEGLSGVA SRTLQRYIDQ
     TQKRRRLLAV S