RPFC_XANC8
ID RPFC_XANC8 Reviewed; 726 AA.
AC P0C0F7; Q4UU87; Q9L431;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Sensory/regulatory protein RpfC;
DE EC=2.7.13.3 {ECO:0000305|PubMed:28369120};
GN Name=rpfC; OrderedLocusNames=XC_2333;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-726, AND MUTAGENESIS.
RX PubMed=1645442; DOI=10.1007/bf00260653;
RA Tang J.-L., Liu Y.-N., Barber C.E., Dow J.M., Wootton J.C., Daniels M.J.;
RT "Genetic and molecular analysis of a cluster of rpf genes involved in
RT positive regulation of synthesis of extracellular enzymes and
RT polysaccharide in Xanthomonas campestris pathovar campestris.";
RL Mol. Gen. Genet. 226:409-417(1991).
RN [4]
RP FUNCTION.
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 [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, INTERACTION WITH RPFF, DOMAIN, AND MUTAGENESIS OF HIS-198;
RP GLN-496; GLU-504; ASP-512; ILE-552 AND HIS-657.
RX PubMed=16940295; DOI=10.1074/jbc.m606571200;
RA He Y.W., Wang C., Zhou L., Song H., Dow J.M., Zhang L.H.;
RT "Dual signaling functions of the hybrid sensor kinase RpfC of Xanthomonas
RT campestris involve either phosphorelay or receiver domain-protein
RT interaction.";
RL J. Biol. Chem. 281:33414-33421(2006).
RN [8]
RP SUBCELLULAR LOCATION.
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).
RN [9]
RP FUNCTION, KINASE ACTIVITY, ACTIVITY REGULATION, DOMAIN,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF ARG-15; ASP-17; SER-18; GLU-19;
RP GLN-22; LEU-172; ALA-178; ASP-512 AND HIS-657.
RC STRAIN=8004;
RX PubMed=28369120; DOI=10.1371/journal.ppat.1006304;
RA Cai Z., Yuan Z.H., Zhang H., Pan Y., Wu Y., Tian X.Q., Wang F.F., Wang L.,
RA Qian W.;
RT "Fatty acid DSF binds and allosterically activates histidine kinase RpfC of
RT phytopathogenic bacterium Xanthomonas campestris pv. campestris to regulate
RT quorum-sensing and virulence.";
RL PLoS Pathog. 13:e1006304-e1006304(2017).
CC -!- FUNCTION: Hybrid sensor kinase that regulates diverse biological
CC functions through two distinct molecular mechanisms (PubMed:16940295).
CC At low cell density, the extracellular concentration of the diffusible
CC signaling factor (DSF) is below a threshold, and unphosphorylated RpfC
CC is involved in the negative regulation of DSF synthesis, via direct
CC interaction with the DSF synthase RpfF. Interaction prevents synthesis
CC of DSF, which remains at a basal level. This activity does not involve
CC the phosphorelay mechanism and is not dependent on RpfG
CC (PubMed:11123673, PubMed:16940295). Is also member of the two-component
CC regulatory system RpfG/RpfC, which is involved in the perception and
CC response to DSF, which is essential for cell-cell signaling
CC (PubMed:11123673, PubMed:12960398). At high cell density, the level of
CC extracellular DSF increases and binding of DSF to the sensor region of
CC RpfC causes autophosphorylation of RpfC, which results in the release
CC of RpfF and the activation of RpfG via a four-step phosphorelay
CC (PubMed:16940295, PubMed:28369120). Activation of RpfG leads to the
CC positive regulation of biofilm dispersal and the production of
CC virulence factors (PubMed:12960398). {ECO:0000269|PubMed:11123673,
CC ECO:0000269|PubMed:12960398, ECO:0000269|PubMed:16940295,
CC ECO:0000269|PubMed:28369120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:28369120};
CC -!- ACTIVITY REGULATION: Binding of DSF to the sensor region causes
CC allosteric change, which facilitates RpfC autophosphorylation.
CC {ECO:0000269|PubMed:28369120}.
CC -!- SUBUNIT: At low DSF concentrations, interacts with RpfF.
CC {ECO:0000269|PubMed:16940295}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:28369120}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes at the cell poles.
CC {ECO:0000269|PubMed:20231439}.
CC -!- DOMAIN: The N-terminal input region plays an essential role in DSF
CC perception. DSF binds with high affinity to a 22-amino acid sensor
CC region at the N-terminus (PubMed:28369120). The response regulatory
CC domain, but not the HPt domain, is required for repression of DSF
CC biosynthesis (PubMed:16940295). {ECO:0000269|PubMed:16940295,
CC ECO:0000269|PubMed:28369120}.
CC -!- PTM: Autophosphorylated (PubMed:28369120). Activation may require a
CC sequential transfer of a phosphate group from a His in the primary
CC transmitter domain, to an Asp in the receiver domain and to a His in
CC the secondary transmitter domain (Probable).
CC {ECO:0000269|PubMed:28369120, ECO:0000305}.
CC -!- CAUTION: The article describing the function has been retracted due to
CC duplications and irregularities in some figures, but repeated
CC experiments using the original strains support the findings.
CC {ECO:0000305|PubMed:16611728, ECO:0000305|PubMed:28784774}.
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DR EMBL; AJ251547; CAB89845.1; -; Genomic_DNA.
DR EMBL; CP000050; AAY49386.1; -; Genomic_DNA.
DR PIR; S16003; S16003.
DR RefSeq; WP_011269804.1; NC_007086.1.
DR AlphaFoldDB; P0C0F7; -.
DR SMR; P0C0F7; -.
DR EnsemblBacteria; AAY49386; AAY49386; XC_2333.
DR KEGG; xcb:XC_2333; -.
DR HOGENOM; CLU_000445_104_10_6; -.
DR OMA; QRECLNT; -.
DR OrthoDB; 1755994at2; -.
DR PHI-base; PHI:7059; -.
DR PHI-base; PHI:8361; -.
DR PHI-base; PHI:8453; -.
DR Proteomes; UP000000420; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..726
FT /note="Sensory/regulatory protein RpfC"
FT /id="PRO_0000074863"
FT TOPO_DOM 1..22
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT TRANSMEM 23..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..94
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..151
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28369120"
FT DOMAIN 195..417
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 463..581
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 618..711
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT REGION 1..22
FT /note="Sensor"
FT /evidence="ECO:0000305|PubMed:28369120"
FT MOD_RES 198
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 512
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 657
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MUTAGEN 15
FT /note="R->A: Cannot interact with DSF. Significant decrease
FT in EXP and EPS production, as well as in biofilm formation.
FT Substantial attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 17
FT /note="D->A: Cannot interact with DSF. Significant decrease
FT in EXP and EPS production, as well as in biofilm formation.
FT Substantial attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 18
FT /note="S->A: Cannot interact with DSF. Significant decrease
FT in EXP and EPS production, as well as in biofilm formation.
FT Substantial attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 18
FT /note="S->T: Has similar or increased levels in EXP
FT activity, EPS production and biofilm formation. Does not
FT affect virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 19
FT /note="E->A: Cannot interact with DSF. Significant decrease
FT in EXP and EPS production, as well as in biofilm formation.
FT Substantial attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 22
FT /note="Q->A: Cannot interact with DSF. Significant decrease
FT in EXP and EPS production, as well as in biofilm formation.
FT Substantial attenuation in virulence."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 172
FT /note="L->A: Constitutive activation of kinase activity."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 178
FT /note="A->D: Constitutive activation of kinase activity."
FT /evidence="ECO:0000269|PubMed:28369120"
FT MUTAGEN 198
FT /note="H->A: Decreased production of EPS and reduced
FT activity of cellulase and protease. No change in DSF
FT production."
FT /evidence="ECO:0000269|PubMed:16940295"
FT MUTAGEN 496
FT /note="Q->A: Decreases repressor activity of the response
FT regulatory domain."
FT /evidence="ECO:0000269|PubMed:16940295"
FT MUTAGEN 504
FT /note="E->A: Decreases repressor activity of the response
FT regulatory domain."
FT /evidence="ECO:0000269|PubMed:16940295"
FT MUTAGEN 512
FT /note="D->V: Decreased production of EPS and reduced
FT activity of cellulase and protease. No change in DSF
FT production. Does not affect the DSF-dependent autokinase
FT activity."
FT /evidence="ECO:0000269|PubMed:16940295,
FT ECO:0000269|PubMed:28369120"
FT MUTAGEN 552
FT /note="I->A: Decreases repressor activity of the response
FT regulatory domain."
FT /evidence="ECO:0000269|PubMed:16940295"
FT MUTAGEN 657
FT /note="H->A: Decreased production of EPS and reduced
FT activity of cellulase and protease. No change in DSF
FT production. Does not affect the DSF-dependent autokinase
FT activity."
FT /evidence="ECO:0000269|PubMed:16940295,
FT ECO:0000269|PubMed:28369120"
FT CONFLICT 226
FT /note="C -> G (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..590
FT /note="TLADLAVSTRQLATP -> NPGRSGSEHPAVGDA (in Ref. 3; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 79806 MW; 5B7CACABE30340D7 CRC64;
MKSPLPWLKR RLSGRADSEH AQNLIRIIIT TLFISYLGWR YQHTHGDTLM ATWLILVGEL
LVSLGLMVAI LLRPQVSHTR RLIGMLLDYT CTGAIMAIQG EPASPLYAVC MWVTIGNGLR
YGSNYLRAAT AMGSLCFLGA ILISPYWKAN PYLSWGLLLG LIAVPLYFDS LLRAMTRAVR
EARHANQAKS RFLANMSHEF RTPLNGLSGM TEVLATTRLD AEQKECLNTI QASARSLLSL
VEEVLDISAI EAGKIRIDRR DFSLREMIGS VNLILQPQAR GRRLEYGTQV ADDVPDLLKG
DTAHLRQVLL NLVGNAVKFT EHGHVLLRVT RVSGSAEDAV RLRFDVEDTG IGVPMDMRPR
LFEAFEQADV GLSRRYEGTG LGTTIAKGLV EAMGGSIGFK ENQPSGSVFW FELPMAIGEP
LKSSTVRVPT GALVDAPEEL ESSNIIAFSN PFLRHRARVR SMRMLVADDH EANRMVLQRL
LEKAGHKVLC VNGAEQVLDA MAEEDYDAVI VDLHMPGMNG LDMLKQLRVM QASGMRYTPV
VVLSADVTPE AIRACEQAGA RAFLAKPVLA AKLLDTLADL AVSTRQLATP ATTVQVATSF
EGVLDSSVLD ELAALGMGEE FERQFVRQCL DDAQNCVGDI ERDGTCSDWE QLRESAHALR
GVASNLGLAQ VASSGGELMR MADWQLQAEW RLRLSTLREQ LKAGKDALDA RVQGVKDGEC
SPRSNE
