ID   YCGR_NITMU              Reviewed;         258 AA.
AC   Q2Y8L4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Nmul_A1606;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) 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; CP000103; ABB74907.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2Y8L4; -.
DR   SMR; Q2Y8L4; -.
DR   STRING; 323848.Nmul_A1606; -.
DR   KEGG; nmu:Nmul_A1606; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_0_0_4; -.
DR   OrthoDB; 5572581at2; -.
DR   Proteomes; UP000002718; 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..258
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395280"
FT   DOMAIN          131..248
FT                   /note="PilZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ   SEQUENCE   258 AA;  28797 MW;  9981D3B1A0E499BB CRC64;
     MSRTWIDIMA DSKPDLPDNN KKYRISSKSG ILSVLRVMIR NNSQATCYFG DAGSFFPTAL
     LNLDSQRGEM VLDYGPNEEI NQQALQVEKW NVVAFPNQVK VQFSCQQIGK TEFEGRNAFL
     AQIPTSLLRM QKREYYRVAT PTTAPVKCVI PLLLGKSPST VEVLLQDLSC GGMAVIDSNG
     RSNFEEGSVY ENCCIVLPDI GTVNVSMRII RVEPADTGFV HDLQSQRVSC EFADAGENAL
     SLIQRYITRL ELEQKRAS
//