YCGR_JANMA
ID YCGR_JANMA Reviewed; 252 AA.
AC A6SXY6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=mma_1443;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR90520.1; -; Genomic_DNA.
DR RefSeq; WP_012079299.1; NC_009659.1.
DR AlphaFoldDB; A6SXY6; -.
DR SMR; A6SXY6; -.
DR STRING; 375286.mma_1443; -.
DR EnsemblBacteria; ABR90520; ABR90520; mma_1443.
DR KEGG; mms:mma_1443; -.
DR eggNOG; COG5581; Bacteria.
DR HOGENOM; CLU_086025_0_0_4; -.
DR OMA; RYIFRID; -.
DR OrthoDB; 1084216at2; -.
DR BioCyc; JSP375286:MMA_RS07505-MON; -.
DR Proteomes; UP000006388; 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..252
FT /note="Flagellar brake protein YcgR"
FT /id="PRO_0000395274"
FT DOMAIN 123..238
FT /note="PilZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01457"
SQ SEQUENCE 252 AA; 27728 MW; 67AAC80A56A63A59 CRC64;
MTLVSDHEND DMNPFRVRSR REVIALLRSI GERNQLVRMV INHGADTIVT SILNIDETND
TVLLDCAPTA IMNQRVLDSN KLSFETVLEN IRILFNSPSA ESCMYENLPA FVIPLPTSVV
RLQRREFYRV PTPLTAPVSC TVPYTTEGVT IEVATTLHNI SGGGVSLVDE KKLLSTTIGL
TYQNCKIVLP GSGLITVALQ VRNVLELTLT NGKSINRIGC EFINPSNGTL ATVQKYITKI
EREQNAKATG LG