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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   03-AUG-2022, entry version 88.
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., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION IN MOTILITY, MUTAGENESIS OF ARG-118, AND DISRUPTION 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 PilZ
RT   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, OVEREXPRESSION,
RP   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 and
RT   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 swarming
CC       in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner.
CC       Overexpression of this gene decreases swimming and swarming motility;
CC       those cells that are motile turn predominantly counterclockwise. The D-
CC       118 mutant is still able to bind FliM but no longer affects motility
CC       upon overexpression. Binds 1 c-di-GMP dimer per subunit.
CC       {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 mutants
CC       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 this
CC       gene suppresses the reduced motility of a yhjH disruption, thus the
CC       double knockout is motile. Overexpression of this gene in a yhjH
CC       disruption has the converse effect, i.e. it reduces motility further.
CC       {ECO:0000269|PubMed:16920715, ECO:0000269|PubMed:20346719}.
CC   -!- SIMILARITY: Belongs to the YcgR family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL20713.1; -; Genomic_DNA.
DR   RefSeq; NP_460754.1; NC_003197.2.
DR   RefSeq; WP_000017421.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZP19; -.
DR   SMR; Q8ZP19; -.
DR   STRING; 99287.STM1798; -.
DR   PaxDb; Q8ZP19; -.
DR   DNASU; 1253317; -.
DR   EnsemblBacteria; AAL20713; AAL20713; STM1798.
DR   GeneID; 1253317; -.
DR   KEGG; stm:STM1798; -.
DR   PATRIC; fig|99287.12.peg.1897; -.
DR   HOGENOM; CLU_086025_1_0_6; -.
DR   OMA; REYFRVN; -.
DR   PhylomeDB; Q8ZP19; -.
DR   BioCyc; SENT99287:STM1798-MON; -.
DR   Proteomes; UP000001014; 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; 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_PilZN.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF07317; YcgR; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum; c-di-GMP; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Flagellar brake protein YcgR"
FT                   /id="PRO_0000395283"
FT   DOMAIN          112..230
FT                   /note="PilZ"
FT   MUTAGEN         118
FT                   /note="R->D: Suppresses a yhjH disruption mutant upon
FT                   overexpression, binds FliM but no longer affects motility
FT                   in this assay."
FT                   /evidence="ECO:0000269|PubMed:16920715,
FT                   ECO:0000269|PubMed:20346719"
FT   MUTAGEN         223
FT                   /note="E->W: No localization with flagellar basal body,
FT                   thus no binding to FliM."
FT                   /evidence="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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