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Database: UniProt
Entry: YCGR_SALTY
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Original site: YCGR_SALTY 
ID   YCGR_SALTY              Reviewed;         244 AA.
AC   Q8ZP19;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 73.
DE   RecName: Full=Flagellar brake protein YcgR;
DE   AltName: Full=Cyclic di-GMP binding protein YcgR;
GN   Name=ycgR; OrderedLocusNames=STM1798;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION IN MOTILITY, MUTAGENESIS OF ARG-118, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=16920715; DOI=10.1074/jbc.C600179200;
RA   Ryjenkov D.A., Simm R., Romling U., Gomelsky M.;
RT   "The PilZ domain is a receptor for the second messenger c-di-GMP: the
RT   PilZ domain protein YcgR controls motility in enterobacteria.";
RL   J. Biol. Chem. 281:30310-30314(2006).
RN   [3]
RP   MUTAGENESIS OF ARG-118 AND GLU-223, SUBCELLULAR LOCATION,
RP   OVEREXPRESSION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA   Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT   "The c-di-GMP binding protein YcgR controls flagellar motor direction
RT   and speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL   Mol. Cell 38:128-139(2010).
CC   -!- FUNCTION: Acts as a flagellar brake, regulating swimming and
CC       swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-
CC       dependent manner. Overexpression of this gene decreases swimming
CC       and swarming motility; those cells that are motile turn
CC       predominantly counterclockwise. The D-118 mutant is still able to
CC       bind FliM but no longer affects motility upon overexpression.
CC       Binds 1 c-di-GMP dimer per subunit. {ECO:0000269|PubMed:16920715}.
CC   -!- SUBUNIT: Monomer. Interacts with the flagellar basal bodies (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000269|PubMed:20346719}. Note=Localization lost in FliM
CC       mutants E-155 or E-160.
CC   -!- DOMAIN: The N-terminal domain is involved in FliG binding, the C-
CC       terminal domain is involved in FliM binding.
CC   -!- DISRUPTION PHENOTYPE: No visible motility phenotype. Disruption of
CC       this gene suppresses the reduced motility of a yhjH disruption,
CC       thus the double knockout is motile. Overexpression of this gene in
CC       a yhjH disruption has the converse effect, i.e. it reduces
CC       motility further. {ECO:0000269|PubMed:16920715,
CC       ECO:0000269|PubMed:20346719}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000305}.
DR   EMBL; AE006468; AAL20713.1; -; Genomic_DNA.
DR   RefSeq; NP_460754.1; NC_003197.2.
DR   RefSeq; WP_000017421.1; NC_003197.2.
DR   ProteinModelPortal; Q8ZP19; -.
DR   SMR; Q8ZP19; -.
DR   STRING; 99287.STM1798; -.
DR   PaxDb; Q8ZP19; -.
DR   PRIDE; Q8ZP19; -.
DR   DNASU; 1253317; -.
DR   EnsemblBacteria; AAL20713; AAL20713; STM1798.
DR   GeneID; 1253317; -.
DR   KEGG; stm:STM1798; -.
DR   PATRIC; fig|99287.12.peg.1897; -.
DR   eggNOG; ENOG4108T7K; Bacteria.
DR   eggNOG; COG5581; LUCA.
DR   HOGENOM; HOG000265609; -.
DR   KO; K21087; -.
DR   OMA; YVQRREY; -.
DR   PhylomeDB; Q8ZP19; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0071945; P:regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed; IGI:UniProtKB.
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_N.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF07317; YcgR; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum; c-di-GMP; Complete proteome; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    244       Flagellar brake protein YcgR.
FT                                /FTId=PRO_0000395283.
FT   DOMAIN      112    230       PilZ.
FT   MUTAGEN     118    118       R->D: Suppresses a yhjH disruption mutant
FT                                upon overexpression, binds FliM but no
FT                                longer affects motility in this assay.
FT                                {ECO:0000269|PubMed:16920715,
FT                                ECO:0000269|PubMed:20346719}.
FT   MUTAGEN     223    223       E->W: No localization with flagellar
FT                                basal body, thus no binding to FliM.
FT                                {ECO:0000269|PubMed:20346719}.
SQ   SEQUENCE   244 AA;  27668 MW;  53AFC4BFB4ADE28D CRC64;
     MSGYNEQFLK KNPLAILGVL RDLNKNQVPL RISWAHGQFI SKILAVDPEK LIVDYGSQEY
     ENSAVLRAGQ VAIIAETQGA KVEFTLPQLV TGEYQRLPAF ITPLPSSLWF VQRREYFRIG
     APLYPPYYGV TTLPDTRTLR FRLFDLSLGG MGALLESAIP DGLIEGARFS QVELNMGQWG
     IFHVDAQLIS ISERKVIDGK NETITTPRLS FRFLNVSPAV ERELQRIIFS LEREARERAN
     KVRE
//
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