ID   YCGR_AZOSB              Reviewed;         259 AA.
AC   A1K922;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=azo2711;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95327.1; -; Genomic_DNA.
DR   RefSeq; WP_011766437.1; NC_008702.1.
DR   AlphaFoldDB; A1K922; -.
DR   SMR; A1K922; -.
DR   STRING; 62928.azo2711; -.
DR   EnsemblBacteria; CAL95327; CAL95327; azo2711.
DR   KEGG; aoa:dqs_2846; -.
DR   KEGG; azo:azo2711; -.
DR   eggNOG; COG5581; Bacteria.
DR   HOGENOM; CLU_086025_0_0_4; -.
DR   OMA; REYFRVN; -.
DR   OrthoDB; 1084216at2; -.
DR   Proteomes; UP000002588; 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..259
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395266"
FT   DOMAIN          129..246
FT                   /note="PilZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ   SEQUENCE   259 AA;  29235 MW;  9F527576D681CCFE CRC64;
     MSNQNDDTRV DLLGSDDFEK YLLYGSREIR QILQGLIDHH ALITAQTVPG HQSFLTTVVA
     LPDDGASIII DAGPDEHINQ RVGNAERLVC MSQLDKIRIQ FDLSAPALTR YENRPAFRAP
     VPAQLLRLQR REFYRLQTPV THTVTCRIPL PQPDGRTLEL ETRVIDISGG GIAVVVPPDN
     VPFGADMEFE NCKLTLPELG TIPVRLKVRN LFRLTNRNGV EMLRAGCEFV DLPRSADNAI
     QRYIFKVERD RSARERGRL