RPFG_XANC8
ID RPFG_XANC8 Reviewed; 378 AA.
AC Q4UU85; Q9L433;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cyclic di-GMP phosphodiesterase response regulator RpfG;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q9WY30};
GN Name=rpfG; OrderedLocusNames=XC_2335;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=8004;
RX PubMed=11123673; DOI=10.1046/j.1365-2958.2000.02196.x;
RA Slater H., Alvarez-Morales A., Barber C.E., Daniels M.J., Dow J.M.;
RT "A two-component system involving an HD-GYP domain protein links cell-cell
RT signalling to pathogenicity gene expression in Xanthomonas campestris.";
RL Mol. Microbiol. 38:986-1003(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
RN [3]
RP FUNCTION.
RC STRAIN=8004;
RX PubMed=12960398; DOI=10.1073/pnas.1833360100;
RA Dow J.M., Crossman L., Findlay K., He Y.Q., Feng J.X., Tang J.L.;
RT "Biofilm dispersal in Xanthomonas campestris is controlled by cell-cell
RT signaling and is required for full virulence to plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10995-11000(2003).
RN [4]
RP FUNCTION, AND REVIEW.
RX PubMed=15158198; DOI=10.1016/j.micinf.2004.01.013;
RA Crossman L., Dow J.M.;
RT "Biofilm formation and dispersal in Xanthomonas campestris.";
RL Microbes Infect. 6:623-629(2004).
RN [5]
RP RETRACTED PAPER.
RC STRAIN=8004;
RX PubMed=16611728; DOI=10.1073/pnas.0600345103;
RA Ryan R.P., Fouhy Y., Lucey J.F., Crossman L.C., Spiro S., He Y.W.,
RA Zhang L.H., Heeb S., Camara M., Williams P., Dow J.M.;
RT "Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain
RT protein that functions in cyclic di-GMP turnover.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6712-6717(2006).
RN [6]
RP RETRACTION NOTICE OF PUBMED:16611728.
RX PubMed=28784774; DOI=10.1073/pnas.1712524114;
RA Ryan R.P., Fouhy Y., Lucey J.F., Crossman L.C., Spiro S., He Y.W.,
RA Zhang L.H., Heeb S., Camara M., Williams P., Dow J.M.;
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7031-E7031(2017).
RN [7]
RP FUNCTION.
RC STRAIN=Xc1;
RX PubMed=17378922; DOI=10.1111/j.1365-2958.2007.05670.x;
RA He Y.W., Ng A.Y., Xu M., Lin K., Wang L.H., Dong Y.H., Zhang L.H.;
RT "Xanthomonas campestris cell-cell communication involves a putative
RT nucleotide receptor protein Clp and a hierarchical signalling network.";
RL Mol. Microbiol. 64:281-292(2007).
RN [8]
RP FUNCTION, INTERACTION WITH GGDEF DOMAIN, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF HIS-231; ASP-232; GLY-294; TYR-295 AND PRO-296.
RC STRAIN=8004;
RX PubMed=20231439; DOI=10.1073/pnas.0912839107;
RA Ryan R.P., McCarthy Y., Andrade M., Farah C.S., Armitage J.P., Dow J.M.;
RT "Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF
RT domain proteins mediate virulence in Xanthomonas campestris.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5989-5994(2010).
CC -!- FUNCTION: Member of the two-component regulatory system RpfG/RpfC,
CC which is involved in the perception and response to the diffusible
CC signaling factor (DSF), which is essential for cell-cell signaling
CC (PubMed:11123673, PubMed:12960398). Detection of DSF leads to the
CC positive regulation of biofilm dispersal and the production of
CC virulence factors (PubMed:12960398). Activated RpfG degrades cyclic di-
CC GMP to GMP, leading to the activation of Clp, a global transcriptional
CC regulator that regulates a large set of genes in DSF pathway. May also
CC directly control genes involved in biofilm dispersal (PubMed:15158198,
CC PubMed:17378922, PubMed:20231439). {ECO:0000269|PubMed:11123673,
CC ECO:0000269|PubMed:12960398, ECO:0000269|PubMed:15158198,
CC ECO:0000269|PubMed:17378922, ECO:0000269|PubMed:20231439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclic di-3',5'-guanylate + 2 H2O = 2 GMP + 2 H(+);
CC Xref=Rhea:RHEA:52928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58805;
CC Evidence={ECO:0000250|UniProtKB:Q9WY30};
CC -!- SUBUNIT: Interacts with a subset of GGDEF domain-containing proteins.
CC {ECO:0000269|PubMed:20231439}.
CC -!- INTERACTION:
CC Q4UU85; A0A0H2X359: XC_0249; NbExp=5; IntAct=EBI-16222292, EBI-16222374;
CC Q4UU85; A0A0H2X3K2: XC_0420; NbExp=4; IntAct=EBI-16222292, EBI-16222336;
CC Q4UU85; A0A0H2X560: XC_0613; NbExp=3; IntAct=EBI-16222292, EBI-16222310;
CC Q4UU85; A0A0H2X5F3: XC_0675; NbExp=2; IntAct=EBI-16222292, EBI-16222750;
CC Q4UU85; A0A0H2X6P1: XC_1803; NbExp=3; IntAct=EBI-16222292, EBI-16222575;
CC Q4UU85; A0A0H2X9F2: XC_2866; NbExp=2; IntAct=EBI-16222292, EBI-16222601;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Localizes
CC predominantly at the cell poles. {ECO:0000269|PubMed:20231439}.
CC -!- DOMAIN: Contains a C-terminal HD-GYP (modified HD) domain, which is
CC involved in degradation of cyclic di-GMP. The GYP motif is required for
CC interaction with GGDEF domain-containing proteins.
CC {ECO:0000269|PubMed:20231439}.
CC -!- PTM: Phosphorylated and activated by RpfC.
CC {ECO:0000305|PubMed:12960398}.
CC -!- CAUTION: The article describing the function and the phosphodiesterase
CC activity has been retracted due to duplications and irregularities in
CC some figures, but repeated experiments using the original strains
CC support the findings. {ECO:0000305|PubMed:16611728,
CC ECO:0000305|PubMed:28784774}.
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DR EMBL; AJ251547; CAB89843.1; -; Genomic_DNA.
DR EMBL; CP000050; AAY49388.1; -; Genomic_DNA.
DR RefSeq; WP_011037024.1; NC_007086.1.
DR AlphaFoldDB; Q4UU85; -.
DR SMR; Q4UU85; -.
DR DIP; DIP-58626N; -.
DR IntAct; Q4UU85; 10.
DR EnsemblBacteria; AAY49388; AAY49388; XC_2335.
DR GeneID; 58013597; -.
DR KEGG; xcb:XC_2335; -.
DR HOGENOM; CLU_000445_92_10_6; -.
DR OMA; RCANTQF; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000000420; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProt.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW c-di-GMP; Cytoplasm; Hydrolase; Phosphoprotein; Transducer;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..378
FT /note="Cyclic di-GMP phosphodiesterase response regulator
FT RpfG"
FT /id="PRO_0000081219"
FT DOMAIN 29..147
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 174..371
FT /note="HD-GYP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01176"
FT MOD_RES 80
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 231
FT /note="H->A: Does not affect interaction with GGDEF
FT domain."
FT /evidence="ECO:0000269|PubMed:20231439"
FT MUTAGEN 232
FT /note="D->A: Does not affect interaction with GGDEF
FT domain."
FT /evidence="ECO:0000269|PubMed:20231439"
FT MUTAGEN 294
FT /note="G->A: Decreases interaction with GGDEF domain."
FT /evidence="ECO:0000269|PubMed:20231439"
FT MUTAGEN 295
FT /note="Y->A: Decreases interaction with GGDEF domain."
FT /evidence="ECO:0000269|PubMed:20231439"
FT MUTAGEN 296
FT /note="P->A: Decreases interaction with GGDEF domain."
FT /evidence="ECO:0000269|PubMed:20231439"
SQ SEQUENCE 378 AA; 42173 MW; D360BCFEFD52D3A1 CRC64;
MQDVLGNPAG VSSAETWGSW SEKADLGLNI VIVDDQMSAR TMLRHVIEDI APELKVYDFG
DPLDALSWCE AGRVDLLLLD YRMPGMDGLE FARRLRRLPS HRDIPIILIT IVGDEPIRQA
ALEAGVIDFL VKPIRPRELR ARCSNLLQLR QQSESVKQRA LSLEQRLLAS MNEVEERERE
TLSRLARAIE YRDGGTSAFL ERMSHVAGLV AEQLGLSEEE VRIIEMAAPL HDMGKIAIPD
SVLLKPGKLT EDEMNVMKRH PRIGYELLSG SQNRFIQVGA LIALRHHERY DGSGYPDGLV
GEAIPLEARI VAVADVFDAL LSARPYKEAW TMDAALAYLY AQRGRLFDPR CVDALLRGRA
QLEQICGQFS TASARPGV
