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Database: UniProt
Entry: D5CN17_SIDLE
LinkDB: D5CN17_SIDLE
Original site: D5CN17_SIDLE 
ID   D5CN17_SIDLE            Unreviewed;       255 AA.
AC   D5CN17;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 41.
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=Slit_0613 {ECO:0000313|EMBL:ADE10853.1};
OS   Sideroxydans lithotrophicus (strain ES-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Sideroxydans.
OX   NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE10853.1, ECO:0000313|Proteomes:UP000001625};
RN   [1] {ECO:0000313|EMBL:ADE10853.1, ECO:0000313|Proteomes:UP000001625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-1 {ECO:0000313|EMBL:ADE10853.1,
RC   ECO:0000313|Proteomes:UP000001625};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT   "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL   Submitted (MAR-2010) 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:0000256|HAMAP-
CC       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; CP001965; ADE10853.1; -; Genomic_DNA.
DR   RefSeq; WP_013028752.1; NC_013959.1.
DR   STRING; 580332.Slit_0613; -.
DR   EnsemblBacteria; ADE10853; ADE10853; Slit_0613.
DR   KEGG; slt:Slit_0613; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000220069; -.
DR   OMA; RYIFRID; -.
DR   OrthoDB; POG091H0NAE; -.
DR   Proteomes; UP000001625; 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:UniProtKB-HAMAP.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IEA:UniProtKB-HAMAP.
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 {ECO:0000256|HAMAP-Rule:MF_01457};
KW   c-di-GMP {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001625};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001625}.
FT   DOMAIN       21    125       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      127    243       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   255 AA;  28751 MW;  3F40A69873E972A8 CRC64;
     MRTKEIPLKI EMFSADEEND YLVSNPKEIV SILQTIAQRK SRVALYYNEG NSMVLTMILA
     VDDHGVWVDA ASNPHDNRLI ERSKRIIFVT THNQAKVQFV AGDVVLGTYE DAAAFSLALP
     RKLLRLQRRD YYRLVTPEHG ALKCIIRPVA SQAHIQHEVT VMDISIGGVA LVCEASGIEL
     QPGMVYEHCQ IELPEVGKLE ATIEVKNTFE ITDRNGKVKR RAGCVFVKPD GKTTMQLQRY
     VAQMQQRMAA VKSER
//
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