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Database: UniProt
Entry: A0A106BP56_THIDE
LinkDB: A0A106BP56_THIDE
Original site: A0A106BP56_THIDE 
ID   A0A106BP56_THIDE        Unreviewed;       254 AA.
AC   A0A106BP56;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   30-AUG-2017, entry version 11.
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   ORFNames=ABW22_08565 {ECO:0000313|EMBL:KVW96075.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW96075.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW96075.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW96075.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted,
RT   Subglacial Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KVW96075.1}.
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DR   EMBL; LDUG01000021; KVW96075.1; -; Genomic_DNA.
DR   RefSeq; WP_059754864.1; NZ_LDUG01000021.1.
DR   EnsemblBacteria; KVW96075; KVW96075; ABW22_08565.
DR   PATRIC; fig|36861.3.peg.1370; -.
DR   Proteomes; UP000064243; Unassembled WGS sequence.
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   Cell projection {ECO:0000313|EMBL:KVW96075.1};
KW   Cilium {ECO:0000313|EMBL:KVW96075.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000064243};
KW   Flagellum {ECO:0000313|EMBL:KVW96075.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064243}.
FT   DOMAIN       21    127       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      129    244       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   254 AA;  27927 MW;  EF37F5535082071B CRC64;
     MLSSPQHDPN PADHDDLLAR YTLHSRSEIL FQLRAIQKRK LLVNLDLLGS RQIIVTSVLM
     VNEAKNTLIL DSARGDALNQ ELMSGKGAEF VAQLDGVSIS FATGPVTWCK YEGLPALRIA
     LPMSLVRLQR REHFRVPMPI ANPVKCIVPS TADGDTDPIT THLVDISCGG VAIAETGGRL
     GPETGRILPN CRLLLPESDT ITTSLEVRNS AQIRLPNGAF QTRLGCKFID LPNDMAAKLQ
     RFVMDIERAR RNSL
//
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