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Database: UniProt
Entry: YCGR_SERP5
LinkDB: YCGR_SERP5
Original site: YCGR_SERP5 
ID   YCGR_SERP5              Reviewed;         237 AA.
AC   A8GEX8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 51.
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};
GN   OrderedLocusNames=Spro_2567;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a flagellar brake, regulating swimming and
CC       swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-
CC       dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing
CC       levels of c-di-GMP lead to decreased motility. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000826; ABV41668.1; -; Genomic_DNA.
DR   RefSeq; WP_012145295.1; NC_009832.1.
DR   ProteinModelPortal; A8GEX8; -.
DR   SMR; A8GEX8; -.
DR   STRING; 399741.Spro_2567; -.
DR   EnsemblBacteria; ABV41668; ABV41668; Spro_2567.
DR   KEGG; spe:Spro_2567; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000265609; -.
DR   OMA; YVQRREY; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000007074; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:InterPro.
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_N.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF07317; YcgR; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; c-di-GMP; Complete proteome; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    237       Flagellar brake protein YcgR.
FT                                /FTId=PRO_0000395284.
FT   DOMAIN      108    225       PilZ. {ECO:0000255|HAMAP-Rule:MF_01457}.
SQ   SEQUENCE   237 AA;  27189 MW;  324593F2617C0C9C CRC64;
     MEQNDNGLFI KQERFEVLAI LREICKQRTP LKVVNDRQQF QSLLLSVGPD NIVFSGDEAD
     NRVDGECTIV IESHDAKIEF SVGQAEFTDH QGVNACSTRL PKELIYIQRR RQFRVTTPHW
     REFLCSGEYA DGSEYQLRIH DLSAGGVGLR VDGPLPENLQ PGFQFKKALL DLGSYGSFKV
     NMELVVINED HELDDDDNMV HFSRLSCRFM KLGLAMERKI QSAVFAFELD FNKKKKR
//
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