ID   YCGR_PECCP              Reviewed;         255 AA.
AC   C6DF90;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 50.
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=PC1_1758;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT12799.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6DF90; -.
DR   SMR; C6DF90; -.
DR   STRING; 561230.PC1_1758; -.
DR   EnsemblBacteria; ACT12799; ACT12799; PC1_1758.
DR   KEGG; pct:PC1_1758; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_0_0_6; -.
DR   OMA; REYFRVN; -.
DR   Proteomes; UP000002736; 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.
FT   CHAIN           1..255
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395281"
FT   DOMAIN          122..240
FT                   /note="PilZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ   SEQUENCE   255 AA;  28979 MW;  CB44F7222F7033EF CRC64;
     MMVEMKAVNE NLKEQFVKRN KLAICATLRE LKKNDTSLMV HHSHGQFISK ILDVVPDNNL
     FVFDLGGIER ENNRALYAGS LSFVAEPAGA KVEFNAEIAK TVTYDGLPAF SAQIPELLYL
     IQRRTYFRIN TPLWPPLTCR GELPDESVFL FTIKDLSLGG LSLYTDRDTT GLLTEGDIIK
     SVEMDLADHG FFCVDLQFVG QAMVKVVDNK GEVQLTQRLS FKFPSLNAAQ ERDLQQVIFE
     LERLQNEKKK RFQEL