XOPAC_XANC8
ID XOPAC_XANC8 Reviewed; 536 AA.
AC Q4UWF4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Uridine 5'-monophosphate transferase {ECO:0000303|PubMed:22504181};
DE Short=UMP transferase {ECO:0000303|PubMed:22504181};
DE EC=2.7.7.- {ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:26355215};
DE AltName: Full=Type III effector XopAC/AvrAC {ECO:0000305};
DE AltName: Full=Uridylyl transferase {ECO:0000303|PubMed:22504181};
GN Name=xopAC {ECO:0000303|PubMed:23736288};
GN Synonyms=AvrAC {ECO:0000303|PubMed:17951377};
GN OrderedLocusNames=XC_1553 {ECO:0000312|EMBL:AAY48619.1};
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8004;
RX PubMed=23736288; DOI=10.1128/mbio.00538-12;
RA Guy E., Genissel A., Hajri A., Chabannes M., David P., Carrere S.,
RA Lautier M., Roux B., Boureau T., Arlat M., Poussier S., Noel L.D.;
RT "Natural genetic variation of Xanthomonas campestris pv. campestris
RT pathogenicity on Arabidopsis revealed by association and reverse
RT genetics.";
RL MBio 4:e00538-e00538(2013).
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 AS BOTH A VIRULENCE AND AN AVIRULENCE GENE, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8004;
RX PubMed=17951377; DOI=10.1128/jb.00978-07;
RA Xu R.Q., Blanvillain S., Feng J.X., Jiang B.L., Li X.Z., Wei H.Y., Kroj T.,
RA Lauber E., Roby D., Chen B., He Y.Q., Lu G.T., Tang D.J., Vasse J.,
RA Arlat M., Tang J.L.;
RT "AvrAC(Xcc8004), a type III effector with a leucine-rich repeat domain from
RT Xanthomonas campestris pathovar campestris confers avirulence in vascular
RT tissues of Arabidopsis thaliana ecotype Col-0.";
RL J. Bacteriol. 190:343-355(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-469.
RX PubMed=22504181; DOI=10.1038/nature10962;
RA Feng F., Yang F., Rong W., Wu X., Zhang J., Chen S., He C., Zhou J.M.;
RT "A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune
RT kinases.";
RL Nature 485:114-118(2012).
RN [5]
RP FUNCTION, INTERACTION WITH RLCK, SUBCELLULAR LOCATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
CC -!- FUNCTION: Functions as both a virulence and an avirulence gene in
CC Arabidopsis (PubMed:17951377, PubMed:23736288). Causes disease on the
CC Kashmir (Kas) ecotype, but not on Columbia (Col-0) ecotype
CC (PubMed:17951377). Acts by directly uridylylating the conserved
CC phosphorylation sites in the activation loop of a number of host
CC receptor-like cytoplasmic protein kinases (RLCK), including BIK1, RIPK,
CC PBL1 and PBL2, preventing the activation of these kinases and
CC subsequent signal transduction (PubMed:22504181, PubMed:26355215). In
CC susceptible Arabidopsis plants, uridylylation of BIK1 inhibits the
CC PAMP-triggered immunity (PTI) signaling cascade and thereby promotes
CC bacterial virulence (PubMed:22504181). It also inhibits RPM1-dependent
CC effector-triggered immunity (ETI) in mesophyll tissues by targeting
CC RIPK (PubMed:22504181). In contrast, in the resistant ecotype Col-0,
CC xopAC is a major avirulence gene (PubMed:23951354, PubMed:26355215).
CC Uridylylation of PBL2 triggers the PBL2-RKS1 interaction and thus the
CC assembly of the PBL2-RKS1-ZAR1 complex, which, in turn, activates
CC effector-triggered immunity (ETI) against X.campestris
CC (PubMed:26355215). {ECO:0000269|PubMed:17951377,
CC ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:23736288,
CC ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:26355215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UTP = diphosphate + uridylyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:64604, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:16635, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:156051; Evidence={ECO:0000269|PubMed:22504181,
CC ECO:0000269|PubMed:26355215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UTP = diphosphate + uridylyl-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:64608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:16636, ChEBI:CHEBI:30013, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:156052;
CC Evidence={ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:26355215};
CC -!- SUBUNIT: Interacts with several members of the Arabidopsis RLCK VIIa
CC subfamily. {ECO:0000269|PubMed:23951354}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17951377}. Host cell
CC {ECO:0000269|PubMed:17951377}. Host cell membrane
CC {ECO:0000269|PubMed:23951354}. Note=Secreted via the type III secretion
CC system (TTSS) (Probable). Localization to the host plasma membrane
CC requires the LRR domain (PubMed:23951354).
CC {ECO:0000269|PubMed:23951354, ECO:0000305|PubMed:17951377}.
CC -!- INDUCTION: Transcriptionally regulated by HrpG and HrpX.
CC {ECO:0000269|PubMed:17951377}.
CC -!- DOMAIN: The LRR domain, the Fic/Fido domain and the uridylylation
CC activity are required for avirulence function on Col-0.
CC {ECO:0000269|PubMed:23951354}.
CC -!- DISRUPTION PHENOTYPE: Mutant becomes virulent on Col-0 plants
CC (PubMed:17951377, PubMed:23736288, PubMed:23951354). Mutant still
CC induces disease on the Kashmir ecotype (PubMed:17951377,
CC PubMed:23951354). {ECO:0000269|PubMed:17951377,
CC ECO:0000269|PubMed:23736288, ECO:0000269|PubMed:23951354}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the fic family.
CC {ECO:0000305}.
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DR EMBL; JX453139; AFP74845.1; -; Genomic_DNA.
DR EMBL; CP000050; AAY48619.1; -; Genomic_DNA.
DR RefSeq; WP_011269629.1; NC_007086.1.
DR AlphaFoldDB; Q4UWF4; -.
DR SMR; Q4UWF4; -.
DR EnsemblBacteria; AAY48619; AAY48619; XC_1553.
DR KEGG; xcb:XC_1553; -.
DR HOGENOM; CLU_508005_0_0_6; -.
DR OMA; MERIMRC; -.
DR OrthoDB; 1232677at2; -.
DR PHI-base; PHI:6574; -.
DR PHI-base; PHI:6575; -.
DR Proteomes; UP000000420; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3290.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF02661; Fic; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SUPFAM; SSF140931; SSF140931; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 1: Evidence at protein level;
KW Host cell membrane; Host membrane; Leucine-rich repeat; Membrane;
KW Nucleotidyltransferase; Repeat; Secreted; Transferase; Virulence.
FT CHAIN 1..536
FT /note="Uridine 5'-monophosphate transferase"
FT /id="PRO_0000451250"
FT REPEAT 140..164
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 165..189
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 191..211
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 212..234
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 236..257
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 258..282
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 377..533
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT REGION 22..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 469
FT /note="H->A: Lack of uridylyl transferase activity."
FT /evidence="ECO:0000269|PubMed:22504181"
SQ SEQUENCE 536 AA; 59041 MW; 4B671548C817AA59 CRC64;
MDKNLNLWDM STFIQQYGAL TADHPTHTPE DSPQTVPSPR SSSAHSPEIQ ELRSLQETRP
ARLGARSQSR SSKHGLQQCS SSPSDESFRL HAELAAWCER VETKPSLLAK LGCCAAPPVV
GDHREQRREA MERIMRCLDA GQAGTQLTLR DLNLSQLPPG LHRLAHLRDL DVADNVNLTR
LPEDLSLCKH LERINADGCS IAALPSKIGA LKNLSEISLA FNELRTLPDS IGQCSSLTTI
VVPGCKINKL PASLANLTQL KKLDVAANIE LSELSPHMNL DDVAVHSTQT RLGLMHRIFK
APTFDPETRQ RLSYQASALR DRWAALSHHL SPQARARVDQ MREGASTTLS SQDHKASTAW
KTATEKVSSW AEEGAPITLD RIFKLNQLLL PEGDDDNDPI GGQLRKVGIQ AAPSNTWTEC
RYPPPETLKD EMAKFSGWLE HSEQQAHARD ALGHIEFAAQ LHQRLVSLHP FDDANGRTAR
LAMDWALQRH GLPPAPPVGE ASRLPASFLG GKRVSPEKVV LETLEGIATV MNQVHQ
