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Database: UniProt
Entry: A0A0N1JT37_9NEIS
LinkDB: A0A0N1JT37_9NEIS
Original site: A0A0N1JT37_9NEIS 
ID   A0A0N1JT37_9NEIS        Unreviewed;       253 AA.
AC   A0A0N1JT37;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   05-JUL-2017, entry version 13.
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_2 {ECO:0000313|EMBL:KPC53534.1};
GN   Synonyms=ycgR {ECO:0000256|HAMAP-Rule:MF_01457};
GN   ORFNames=WG78_08435 {ECO:0000313|EMBL:KPC53534.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC53534.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC53534.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC53534.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) 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}.
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:KPC53534.1}.
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DR   EMBL; LAQT01000006; KPC53534.1; -; Genomic_DNA.
DR   RefSeq; WP_053937352.1; NZ_LAQT01000006.1.
DR   EnsemblBacteria; KPC53534; KPC53534; WG78_08435.
DR   PATRIC; fig|857265.3.peg.1729; -.
DR   Proteomes; UP000037939; 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:KPC53534.1};
KW   Cilium {ECO:0000313|EMBL:KPC53534.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037939};
KW   Flagellum {ECO:0000313|EMBL:KPC53534.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037939}.
FT   DOMAIN       21    126       T3SS_YcgR_N. {ECO:0000259|Pfam:PF07317}.
FT   DOMAIN      129    242       PilZ. {ECO:0000259|Pfam:PF07238}.
SQ   SEQUENCE   253 AA;  27966 MW;  BEC762E455A5B9D5 CRC64;
     MSEPIEHPQT PVSEGEDIAP FQLTNPLEIG AVLRQLVLRG DNITIYFAQG RQLMLSRLLA
     VDIPKRELIL DVGGHAETNA ALLNSERNII VGTPDGVKIQ FVLSKIRSTR FDGSPAFVAS
     FPSDLIKLQR REFFRIETPL NRPYTCEMTL PDGKRAALEL HDLSLGGIGA WALPQVAVPL
     VPGTVLERAQ LELGPNGMLQ MDLEMRSKRV TVRGSGQEIY LVGFKFVNTS RAGEATLQRL
     MAQLERERKA LTG
//
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