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Database: UniProt
Entry: Q1LAQ0_CUPMC
LinkDB: Q1LAQ0_CUPMC
Original site: Q1LAQ0_CUPMC 
ID   Q1LAQ0_CUPMC            Unreviewed;       264 AA.
AC   Q1LAQ0;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Flagellar brake protein YcgR {ECO:0000256|HAMAP-Rule:MF_01457};
DE   AltName: Full=Cyclic di-GMP binding protein YcgR {ECO:0000256|HAMAP-Rule:MF_01457};
GN   Name=ycgR {ECO:0000256|HAMAP-Rule:MF_01457};
GN   OrderedLocusNames=Rmet_5917 {ECO:0000313|EMBL:ABF12776.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF12776.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RC   PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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:0000256|HAMAP-Rule:MF_01457}.
CC   -!- SUBUNIT: Monomer. Interacts with the flagellar basal bodies.
CC       {ECO:0000256|HAMAP-Rule:MF_01457}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|HAMAP-Rule:MF_01457}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000256|HAMAP-
CC       Rule:MF_01457}.
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DR   EMBL; CP000353; ABF12776.1; -; Genomic_DNA.
DR   RefSeq; WP_011518126.1; NC_007974.2.
DR   AlphaFoldDB; Q1LAQ0; -.
DR   KEGG; rme:Rmet_5917; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_0_0_4; -.
DR   Proteomes; UP000002429; Plasmid megaplasmid CH34.
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 {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW   Rule:MF_01457};
KW   c-di-GMP {ECO:0000256|ARBA:ARBA00022636, ECO:0000256|HAMAP-Rule:MF_01457};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01457}; Plasmid {ECO:0000313|EMBL:ABF12776.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   DOMAIN          35..140
FT                   /note="Type III secretion system flagellar brake protein
FT                   YcgR PilZN"
FT                   /evidence="ECO:0000259|Pfam:PF07317"
FT   DOMAIN          142..257
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  29557 MW;  0177F9BFB33310C6 CRC64;
     MSLQEPIGSK LAQSQSQVDG EADERDAAAQ SDERYRLTHS SQIGTVLRDM AWQKCLLNVR
     SKGGSEIVTS ILHVDPANKT FIFDWCRADG ERQALMSSEQ NAFSGLLRGV PVNFIVGTPG
     ATRFEGGPAF IADFPEKLYH FQRRRHFRAR TLLTKGYRCE LRIPETEKQA LQLDIADLSL
     SGVGLRSRAV GADQLPVGTV IKRCLLDFAE LGRLELDMQV VGHWLVGFDD NTVHHYGCAF
     LNPDGRMENF LQRLVFQLEL AHRG
//
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