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YCGR_ERWT9
ID   YCGR_ERWT9              Reviewed;         249 AA.
AC   B2VDU2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=ETA_19350;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO96981.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2VDU2; -.
DR   SMR; B2VDU2; -.
DR   STRING; 465817.ETA_19350; -.
DR   EnsemblBacteria; CAO96981; CAO96981; ETA_19350.
DR   KEGG; eta:ETA_19350; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_1_0_6; -.
DR   OMA; REYFRVN; -.
DR   Proteomes; UP000001726; 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..249
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395273"
FT   DOMAIN          117..236
FT                   /note="PilZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ   SEQUENCE   249 AA;  27908 MW;  F941263CFEE7E3FB CRC64;
     MGADVEQDDT EQYLKQGTLA VLGVLRELLQ NQTPMRVSHP RGQFITRLLH VDKTNMVIDF
     GSNDYDNQLA QEANELHIVA DTRGARIELI LTSLQMSEYE GLPAFTAALP GQLKMIQRRE
     FFRVDAPLNP IFFCYVPWPD GTGEGRLRLQ DLSIGGIGML SEGTVPDALS CGDTIKKLRL
     EMGEYGRFVV DAQLISIGKH SVVGSKCETV VTPRLSLRFL SLNAAQEREL QQVIFSLERL
     ARDKAKRFQ
 
 
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