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YDIV_SALT1
ID   YDIV_SALT1              Reviewed;         237 AA.
AC   D0ZW85;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=STM14_1632;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
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,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASN-85 AND PHE-168.
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.
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. Positively regulates expression of the
CC       multicellular rdar morphotype behavior, its major regulator CsgD and
CC       suppresses motility. Regulates the rdar morphotype and motility
CC       indirectly by affecting the expression of the c-di-GMP-dependent
CC       phosphodiesterases YciZ and YhjH. Required for resistance to host
CC       phagocyte oxidase. Suppresses killing of macrophages, while promoting
CC       resistance to hydrogen peroxide. Data regarding c-di-GMP is
CC       controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417)
CC       but neither 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. {ECO:0000250}.
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). {ECO:0000269|PubMed:15882417,
CC       ECO:0000269|PubMed:19376870}.
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:21278297)
CC       experiments were done in strain LT2, which is not a 14028 derivative.
CC       {ECO:0000305|PubMed:15882417, ECO:0000305|PubMed:19376870,
CC       ECO:0000305|PubMed:21278297}.
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DR   EMBL; CP001363; ACY88111.1; -; Genomic_DNA.
DR   RefSeq; WP_000562005.1; NZ_CP043402.1.
DR   AlphaFoldDB; D0ZW85; -.
DR   SMR; D0ZW85; -.
DR   EnsemblBacteria; ACY88111; ACY88111; STM14_1632.
DR   KEGG; seo:STM14_1632; -.
DR   PATRIC; fig|588858.6.peg.1573; -.
DR   HOGENOM; CLU_089254_1_1_6; -.
DR   OMA; SFEPFMR; -.
DR   BioCyc; SENT588858:STM14_RS07580-MON; -.
DR   Proteomes; UP000002695; 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   Repressor; Transcription; Transcription regulation; Virulence.
FT   CHAIN           1..237
FT                   /note="Anti-FlhC(2)FlhD(4) factor YdiV"
FT                   /id="PRO_0000417582"
FT   DOMAIN          1..237
FT                   /note="EAL"
FT   MUTAGEN         85
FT                   /note="N->A: Gain of function, increases CsgD expression in
FT                   disruption, represses swarming."
FT                   /evidence="ECO:0000269|PubMed:19376870"
FT   MUTAGEN         168
FT                   /note="F->A: Does not restore CsgD expression in
FT                   disruption."
FT                   /evidence="ECO:0000269|PubMed:19376870"
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
 
 
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