YCGR_THASP
ID YCGR_THASP Reviewed; 263 AA.
AC C4KAR8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=Tmz1t_2895;
OS Thauera sp. (strain MZ1T).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=85643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001281; ACR01494.1; -; Genomic_DNA.
DR RefSeq; WP_004321902.1; NC_011662.2.
DR AlphaFoldDB; C4KAR8; -.
DR SMR; C4KAR8; -.
DR STRING; 85643.Tmz1t_2895; -.
DR EnsemblBacteria; ACR01494; ACR01494; Tmz1t_2895.
DR KEGG; tmz:Tmz1t_2895; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_086025_0_0_4; -.
DR OMA; REYFRVN; -.
DR OrthoDB; 1084216at2; -.
DR Proteomes; UP000002186; 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..263
FT /note="Flagellar brake protein YcgR"
FT /id="PRO_0000395286"
FT DOMAIN 133..250
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 28517 MW; DB65BE9C344E849A CRC64;
MAELSTPSPA SPAPLDGGRG DELEKFTLRG ARQILQLLQD LITHRGLITA HTGGGHSFMT
AVLKVDEERG RVVLDPSPDP QANRRALAAP RLTCVTQLDG IRIQFPLVGL GEGQDKGRPA
LFAPLPAEML RLQRREFYRL QVPLAHELSC LLKAEDLARK PVEVSARVID IGAGGVAVVV
PTGAAEFVIG GTLPACRLAL PDGEPIELDL EVRNLNRQTQ RNGTEQLRVG LRFAALPRAA
DTRIQRYIFK TERALNAKAR GGL