YCGR_METML
ID YCGR_METML Reviewed; 253 AA.
AC C6WX20;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
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=Mmol_1565;
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540;
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., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
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; CP001672; ACT48469.1; -; Genomic_DNA.
DR RefSeq; WP_015832504.1; NC_012968.1.
DR AlphaFoldDB; C6WX20; -.
DR SMR; C6WX20; -.
DR STRING; 583345.Mmol_1565; -.
DR EnsemblBacteria; ACT48469; ACT48469; Mmol_1565.
DR KEGG; mmb:Mmol_1565; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_086025_0_0_4; -.
DR OMA; RYIFRID; -.
DR OrthoDB; 1084216at2; -.
DR Proteomes; UP000002742; 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..253
FT /note="Flagellar brake protein YcgR"
FT /id="PRO_0000395278"
FT DOMAIN 120..239
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ SEQUENCE 253 AA; 27949 MW; 53939C4DC47B6A64 CRC64;
MEHAAFVHNE EQYIVHNPKE VTQIINDLIK HKSMIKVTFN HGADVYLTSI ISIDAKTGAV
YLDVGVDDEF NRRLLASNHV VFIKEDGVKI KWTSAHIAGV ELKDGKAIKI ALPKDMVRLQ
RRDFYRFATP VANPVVCKIP VPDVLNPAEE TILELSLVDV SLGGIGTLVA APLNPALVLG
QAFNGCKIGF PDVGETNLTL KVKNITEIHV QDVMTKYRVG FEYVEPSRGN EGLINRYVYI
LERQAIALAH GAA