YCGR_THISH
ID YCGR_THISH Reviewed; 246 AA.
AC B8GQA2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
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=Tgr7_1211;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL72297.1; -; Genomic_DNA.
DR RefSeq; WP_012637780.1; NC_011901.1.
DR AlphaFoldDB; B8GQA2; -.
DR SMR; B8GQA2; -.
DR STRING; 396588.Tgr7_1211; -.
DR EnsemblBacteria; ACL72297; ACL72297; Tgr7_1211.
DR KEGG; tgr:Tgr7_1211; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_1174300_0_0_6; -.
DR OMA; VERFVYQ; -.
DR OrthoDB; 1600481at2; -.
DR Proteomes; UP000002383; 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..246
FT /note="Flagellar brake protein YcgR"
FT /id="PRO_0000395287"
FT DOMAIN 128..232
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ SEQUENCE 246 AA; 27441 MW; D08799C144B0E1F1 CRC64;
MNETPAVPPS PEVEGSLNEQ ISHRRRILAV LDAMKDGRAL LSARIENQRG YFNTTLLKID
AEKGYVFLDE LAPADGHEKI AVGQTLHLYG FYNNLPAHFA IEVIHVGEHE GIAFYAGPLP
KLIHYQQKRA HFRAYVGLGK ELKVRLRKGD GAQISGRLQD ISLGGFGALM PADSVFEDLE
IVEVEALELP DHHAIACSAE IRHSHPTQGR VHIGARFTQL APQAERQLLQ AIVELEREQL
RKQSRD