ID A0A0R0CNQ7_9GAMM Unreviewed; 259 AA.
AC A0A0R0CNQ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 {ECO:0000256|HAMAP-Rule:MF_01457};
GN ORFNames=ABB29_04195 {ECO:0000313|EMBL:KRG71030.1};
OS Pseudoxanthomonas dokdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG71030.1, ECO:0000313|Proteomes:UP000052052};
RN [1] {ECO:0000313|EMBL:KRG71030.1, ECO:0000313|Proteomes:UP000052052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG71030.1,
RC ECO:0000313|Proteomes:UP000052052};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:0000256|HAMAP-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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG71030.1}.
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DR EMBL; LDJL01000004; KRG71030.1; -; Genomic_DNA.
DR RefSeq; WP_057657355.1; NZ_LDJL01000004.1.
DR AlphaFoldDB; A0A0R0CNQ7; -.
DR STRING; 344882.ABB29_04195; -.
DR PATRIC; fig|344882.3.peg.2170; -.
DR Proteomes; UP000052052; Unassembled WGS sequence.
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; 2.40.10.220; predicted glycosyltransferase like domains; 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; PilZN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_01457};
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636, ECO:0000256|HAMAP-Rule:MF_01457};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01457}; Reference proteome {ECO:0000313|Proteomes:UP000052052}.
FT DOMAIN 21..126
FT /note="Type III secretion system flagellar brake protein
FT YcgR PilZN"
FT /evidence="ECO:0000259|Pfam:PF07317"
FT DOMAIN 129..246
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 259 AA; 28949 MW; 337650EA208A8944 CRC64;
MSESAVSANP PPVRYEEDEK YLLRGQRKVG PVLNALIERQ ALISAWISPR NLSFPTALLE
YSADTGSVVI DASVNEALNS AVQQCSHLTC VSQLDKVHVQ FRLQGLRLQT LAGQPAFVAA
APSQLLQLQR REYYRLPVPL TQPLTCTVDF SDRHGVISRR DLRVLDISAG GIAVVAPDDQ
PGFRPLNAFE SCSLQLPDSE PLPIQLQVRN LFRQKLANGQ ESWRAGCAFL RLPHGADRLI
QRYIFRMERL RTARRQGLV
//
