RPFC_XANCP
ID RPFC_XANCP Reviewed; 726 AA.
AC P0C0F6; P49246;
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;
GN Name=rpfC; OrderedLocusNames=XCC1856;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2] {ECO:0007744|PDB:3M6M}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 449-590 IN COMPLEX WITH RPFF,
RP FUNCTION, INTERACTION WITH RPFF, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-495 AND VAL-529.
RC STRAIN=XC1;
RX PubMed=20826346; DOI=10.1016/j.str.2010.06.011;
RA Cheng Z., He Y.W., Lim S.C., Qamra R., Walsh M.A., Zhang L.H., Song H.;
RT "Structural basis of the sensor-synthase interaction in autoinduction of
RT the quorum sensing signal DSF biosynthesis.";
RL Structure 18:1199-1209(2010).
CC -!- FUNCTION: Hybrid sensor kinase that regulates diverse biological
CC functions through two distinct molecular mechanisms (By similarity). At
CC 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:20826346). Is also member of the two-component regulatory
CC system RpfG/RpfC, which is involved in the perception and response to
CC DSF, which is essential for cell-cell signaling (By similarity). At
CC high cell density, the level of extracellular DSF increases and binding
CC of DSF to the sensor region of RpfC causes autophosphorylation of RpfC,
CC which results in the release of RpfF and the activation of RpfG via a
CC four-step phosphorelay (By similarity). Activation of RpfG leads to the
CC positive regulation of biofilm dispersal and the production of
CC virulence factors (By similarity). {ECO:0000250|UniProtKB:P0C0F7,
CC ECO:0000269|PubMed:20826346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0C0F7};
CC -!- ACTIVITY REGULATION: Binding of DSF to the sensor region causes
CC allosteric change, which facilitates RpfC autophosphorylation.
CC {ECO:0000250|UniProtKB:P0C0F7}.
CC -!- SUBUNIT: At low DSF concentrations, interacts with RpfF.
CC {ECO:0000269|PubMed:20826346}.
CC -!- INTERACTION:
CC P0C0F6; Q7CLS3: rpfF; NbExp=5; IntAct=EBI-15876881, EBI-15876866;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes at the cell poles.
CC {ECO:0000250|UniProtKB:P0C0F7}.
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 (By similarity). The response regulatory
CC domain, but not the HPt domain, is required for repression of DSF
CC biosynthesis (PubMed:20826346). {ECO:0000250|UniProtKB:P0C0F7,
CC ECO:0000269|PubMed:20826346}.
CC -!- PTM: Autophosphorylated (By similarity). 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:0000250|UniProtKB:P0C0F7, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in overproduction of
CC DSF. {ECO:0000269|PubMed:20826346}.
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DR EMBL; AE008922; AAM41145.1; -; Genomic_DNA.
DR RefSeq; NP_637221.1; NC_003902.1.
DR RefSeq; WP_011037026.1; NC_003902.1.
DR PDB; 3M6M; X-ray; 2.50 A; D/E/F=449-590.
DR PDBsum; 3M6M; -.
DR AlphaFoldDB; P0C0F6; -.
DR SMR; P0C0F6; -.
DR DIP; DIP-59500N; -.
DR IntAct; P0C0F6; 1.
DR STRING; 340.xcc-b100_2144; -.
DR EnsemblBacteria; AAM41145; AAM41145; XCC1856.
DR KEGG; xcc:XCC1856; -.
DR PATRIC; fig|190485.4.peg.1980; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_104_10_6; -.
DR BRENDA; 2.7.13.3; 6708.
DR EvolutionaryTrace; P0C0F6; -.
DR Proteomes; UP000001010; 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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..726
FT /note="Sensory/regulatory protein RpfC"
FT /id="PRO_0000074862"
FT TRANSMEM 23..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
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 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 495
FT /note="E->A: Attenuates the inhibitory activity on DSF
FT production."
FT /evidence="ECO:0000269|PubMed:20826346"
FT MUTAGEN 529
FT /note="V->A: Attenuates the inhibitory activity on DSF
FT production."
FT /evidence="ECO:0000269|PubMed:20826346"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:3M6M"
FT HELIX 471..482
FT /evidence="ECO:0007829|PDB:3M6M"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:3M6M"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:3M6M"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:3M6M"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:3M6M"
FT HELIX 520..532
FT /evidence="ECO:0007829|PDB:3M6M"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:3M6M"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:3M6M"
FT STRAND 561..567
FT /evidence="ECO:0007829|PDB:3M6M"
FT HELIX 570..580
FT /evidence="ECO:0007829|PDB:3M6M"
SQ SEQUENCE 726 AA; 79792 MW; 36374CBF5C47BE3D 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 RAFLAKPVVA AKLLDTLADL AVSTRQLATP ATTVQVATSF
EGVLDSSVLD ELAALGMGEE FERQFVRQCL DDAQNCVGDI ERDGTCSDWE QLRESAHALR
GVASNLGLAQ VASSGGELMR MADWQLQAEW RLRLSTLREQ LKAGKDALDA RVQGVKDGEC
SPRSNE
