YDIV_SALTY
ID YDIV_SALTY Reviewed; 237 AA.
AC Q8ZPS6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Anti-FlhC(2)FlhD(4) factor YdiV;
DE AltName: Full=EAL-like protein YdiV;
DE AltName: Full=c-di-GMP regulator CdgR;
GN Name=ydiV; Synonyms=cdgR; OrderedLocusNames=STM1344;
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 VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=14028;
RX PubMed=15882417; DOI=10.1111/j.1365-2958.2005.04632.x;
RA Hisert K.B., MacCoss M., Shiloh M.U., Darwin K.H., Singh S., Jones R.A.,
RA Ehrt S., Zhang Z., Gaffney B.L., Gandotra S., Holden D.W., Murray D.,
RA Nathan C.;
RT "A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls
RT bacterial survival in mice, antioxidant defence and killing of macrophages:
RT role of cyclic diGMP.";
RL Mol. Microbiol. 56:1234-1245(2005).
RN [3]
RP LACK OF C-DI-GMP PHOSPHODIESTERASE OR DIGUANYLATE CYCLASE ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=14028;
RX PubMed=19376870; DOI=10.1128/jb.00290-09;
RA Simm R., Remminghorst U., Ahmad I., Zakikhany K., Romling U.;
RT "A role for the EAL-like protein STM1344 in regulation of CsgD expression
RT and motility in Salmonella enterica serovar Typhimurium.";
RL J. Bacteriol. 191:3928-3937(2009).
RN [4]
RP FUNCTION IN REPRESSION OF MOTILITY, INTERACTION WITH FLHD, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-29.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=21278297; DOI=10.1128/jb.01494-10;
RA Wada T., Morizane T., Abo T., Tominaga A., Inoue-Tanaka K., Kutsukake K.;
RT "EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for
RT nutritional control of the flagellar regulon in Salmonella enterica Serovar
RT Typhimurium.";
RL J. Bacteriol. 193:1600-1611(2011).
CC -!- FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD,
CC decreasing its ability to bind DNA, and thus negatively regulates
CC expression of flagellar class II operons, decreasing motility in
CC nutrient-poor medium. Required for resistance to host phagocyte
CC oxidase. Suppresses killing of macrophages, while promoting resistance
CC to hydrogen peroxide. Data regarding c-di-GMP is controversial;
CC suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither
CC synthesizes nor degrades c-di-GMP (PubMed:19376870).
CC {ECO:0000269|PubMed:15882417, ECO:0000269|PubMed:19376870,
CC ECO:0000269|PubMed:21278297}.
CC -!- SUBUNIT: Interacts with FlhD in the FlhC(2)FlhD(4) heterohexamer,
CC inhibiting its ability to activate transcription.
CC {ECO:0000269|PubMed:21278297}.
CC -!- INTERACTION:
CC Q8ZPS6; P0A2R2: flhD; NbExp=2; IntAct=EBI-6413835, EBI-6413853;
CC -!- INDUCTION: Induced in nutrient-poor medium (at protein level).
CC {ECO:0000269|PubMed:21278297}.
CC -!- DISRUPTION PHENOTYPE: Decreased bacterial resistance to hydrogen
CC peroxide and accelerated bacterial killing of macrophages. increased
CC levels of c-di-GMP (PubMed:15882417). Down-regulation of rdar
CC morphology, 50% reduction in CsgD expression, cellulose and curli
CC fimbriae, increased swimming and swarming. Decrease in c-di-GMP levels
CC (PubMed:19376870). Derepresses transcription of flagellar class II
CC operons in nutrient-poor medium. {ECO:0000269|PubMed:15882417,
CC ECO:0000269|PubMed:19376870, ECO:0000269|PubMed:21278297}.
CC -!- MISCELLANEOUS: The multicellular rdar morphotype is characterized by
CC the expression of the adhesive extracellular matrix components
CC cellulose and curli fimbriae.
CC -!- SIMILARITY: Belongs to the YdiV family. {ECO:0000305}.
CC -!- CAUTION: Has been proposed to be involved in c-di-GMP turnover
CC (PubMed:15882417), but also not be involved in its turnover
CC (PubMed:19376870). Mutagenesis of Glu-29 in the EAL domain suggests if
CC this protein has c-di-GMP phosphdiesterase activity it is not involved
CC in motility regulation (PubMed:21278297). Note that (PubMed:15882417)
CC and (PubMed:19376870) experiments were done in strain 14028, which is
CC not an LT2 derivative. {ECO:0000305|PubMed:15882417,
CC ECO:0000305|PubMed:19376870, ECO:0000305|PubMed:21278297}.
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DR EMBL; AE006468; AAL20269.1; -; Genomic_DNA.
DR RefSeq; NP_460310.1; NC_003197.2.
DR RefSeq; WP_000562005.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPS6; -.
DR SMR; Q8ZPS6; -.
DR IntAct; Q8ZPS6; 2.
DR STRING; 99287.STM1344; -.
DR PaxDb; Q8ZPS6; -.
DR EnsemblBacteria; AAL20269; AAL20269; STM1344.
DR GeneID; 1252862; -.
DR KEGG; stm:STM1344; -.
DR PATRIC; fig|99287.12.peg.1427; -.
DR HOGENOM; CLU_089254_1_1_6; -.
DR OMA; SFEPFMR; -.
DR PhylomeDB; Q8ZPS6; -.
DR BioCyc; SENT99287:STM1344-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR Gene3D; 3.20.20.450; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR Pfam; PF00563; EAL; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Virulence.
FT CHAIN 1..237
FT /note="Anti-FlhC(2)FlhD(4) factor YdiV"
FT /id="PRO_0000346870"
FT DOMAIN 1..237
FT /note="EAL"
FT MUTAGEN 29
FT /note="E->A: No effect on motility."
FT /evidence="ECO:0000269|PubMed:21278297"
SQ SEQUENCE 237 AA; 26424 MW; 558A591D0B8AC895 CRC64;
MIASLDELYH SELFFLPVMD ENARLVGLEI IATFAAEDGA VRMPTELVAP RLSVEEQYCL
FVEKLALLET CQHFFIQHKL IAWLNLPPAI SDLLLLDSEL FSRAARFPFL ELAINENYPG
LNQGKNNETL ANLAMHFPLM LANFGAGEAS TKAIFDGLFK RVMLDKNFIQ QRAEMISFEP
FMHAIVAQIS SSCESLMIAG IDTEAMFARA APLGFSAFQG GLWPPVPVSQ LIKLVQR
