HOZ1A_PSESY
ID HOZ1A_PSESY Reviewed; 369 AA.
AC Q6VE93;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Serine/threonine-protein acetyltransferase HopZ1a {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22319451};
DE AltName: Full=Protein orf34 {ECO:0000303|PubMed:14634868};
GN Name=hopZ1a {ECO:0000303|PubMed:20636323};
GN ORFNames=ALP25_03258 {ECO:0000312|EMBL:RMU63652.1};
OS Pseudomonas syringae pv. syringae.
OG Plasmid pPSR1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2;
RX PubMed=14634868; DOI=10.1007/s00438-003-0945-9;
RA Sundin G.W., Mayfield C.T., Zhao Y., Gunasekera T.S., Foster G.L.,
RA Ullrich M.S.;
RT "Complete nucleotide sequence and analysis of pPSR1 (72,601 bp), a pPT23A-
RT family plasmid from Pseudomonas syringae pv. syringae A2.";
RL Mol. Genet. Genomics 270:462-476(2004).
RN [2] {ECO:0000312|Proteomes:UP000272344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 4917;
RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT "Recombination of ecologically and evolutionarily significant loci
RT maintains genetic cohesion in the Pseudomonas syringae species complex.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=20636323; DOI=10.1111/j.1469-8137.2010.03381.x;
RA Macho A.P., Guevara C.M., Tornero P., Ruiz-Albert J., Beuzon C.R.;
RT "The Pseudomonas syringae effector protein HopZ1a suppresses effector-
RT triggered immunity.";
RL New Phytol. 187:1018-1033(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP ACETYLATION AT LYS-289, AND MUTAGENESIS OF CYS-216 AND LYS-289.
RX PubMed=22319451; DOI=10.1371/journal.ppat.1002523;
RA Lee A.H., Hurley B., Felsensteiner C., Yea C., Ckurshumova W.,
RA Bartetzko V., Wang P.W., Quach V., Lewis J.D., Liu Y.C., Boernke F.,
RA Angers S., Wilde A., Guttman D.S., Desveaux D.;
RT "A bacterial acetyltransferase destroys plant microtubule networks and
RT blocks secretion.";
RL PLoS Pathog. 8:e1002523-e1002523(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-216,
RP INTERACTION WITH ARABIDOPSIS THALIANA TIFY10B/JAZ2; TIFY11A/JAZ5;
RP TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY3B/JAZ12 AND GLYCINE MAX JAZ1, AND
RP AUTOACETYLATION.
RX PubMed=24204266; DOI=10.1371/journal.ppat.1003715;
RA Jiang S., Yao J., Ma K.-W., Zhou H., Song J., He S.Y., Ma W.;
RT "Bacterial effector activates jasmonate signaling by directly targeting JAZ
RT transcriptional repressors.";
RL PLoS Pathog. 9:e1003715-e1003715(2013).
RN [6]
RP ACETYLATION AT LYS-289, AND MUTAGENESIS OF CYS-216 AND LYS-289.
RX PubMed=26217317; DOI=10.3389/fmicb.2015.00684;
RA Rufian J.S., Lucia A., Macho A.P., Orozco-Navarrete B., Arroyo-Mateos M.,
RA Bejarano E.R., Beuzon C.R., Ruiz-Albert J.;
RT "Auto-acetylation on K289 is not essential for HopZ1a-mediated plant
RT defense suppression.";
RL Front. Microbiol. 6:684-684(2015).
RN [7] {ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-369 IN COMPLEX WITH COENZYME A
RP AND 1D-MYO-INOSITOL HEXAKISPHOSPHATE, FUNCTION, ACTIVE SITES, COFACTOR,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-211; CYS-216; LYS-226; LYS-289;
RP THR-295; ARG-326 AND PHE-348.
RX PubMed=27525589; DOI=10.1038/nsmb.3279;
RA Zhang Z.M., Ma K.W., Yuan S., Luo Y., Jiang S., Hawara E., Pan S., Ma W.,
RA Song J.;
RT "Structure of a pathogen effector reveals the enzymatic mechanism of a
RT novel acetyltransferase family.";
RL Nat. Struct. Mol. Biol. 23:847-852(2016).
CC -!- FUNCTION: Serine/threonine-protein acetyltransferase translocated into
CC infected cells, which impairs host microtubule network and host
CC immunity by mediating acetylation of target proteins (PubMed:20636323,
CC PubMed:22319451, PubMed:24204266, PubMed:27525589). Blocks secretion in
CC host cells by mediating acetylation of host tubulin, thereby impairing
CC host microbubule network (PubMed:22319451). Impairs host cell immunity
CC by mediating acetylation of host TIFY/JAZ transcription repressors
CC (Arabidopsis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6,
CC TIFY5A/JAZ8, TIFY9/JAZ10 and TIFY3B/JAZ12), thereby activating host
CC jasmonate signaling (PubMed:24204266, PubMed:27525589).
CC {ECO:0000269|PubMed:20636323, ECO:0000269|PubMed:22319451,
CC ECO:0000269|PubMed:24204266, ECO:0000269|PubMed:27525589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-
CC [protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141025; Evidence={ECO:0000250|UniProtKB:O68718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC Evidence={ECO:0000250|UniProtKB:O68718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141128; Evidence={ECO:0000250|UniProtKB:O68718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000250|UniProtKB:O68718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:22319451};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000269|PubMed:27525589};
CC -!- ACTIVITY REGULATION: 1D-myo-inositol hexakisphosphate activates
CC protein-acetyltransferase activity via an allosteric mechanism: 1D-myo-
CC inositol hexakisphosphate-binding induces a conformational
CC rearrangement that stimulates the interaction with acetyl-CoA
CC (PubMed:27525589). Acetyltransferase activity is activated by phytic
CC acid (PubMed:22319451). {ECO:0000269|PubMed:22319451,
CC ECO:0000269|PubMed:27525589}.
CC -!- SUBUNIT: Interacts with host plant JAZ proteins (e.g. Glycine max JAZ1
CC and Arabidospis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6,
CC TIFY5A/JAZ8 and TIFY3B/JAZ12) and trigger their degradation.
CC {ECO:0000269|PubMed:24204266}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20636323}. Host cell
CC membrane {ECO:0000269|PubMed:24204266}. Host cytoplasm, host
CC cytoskeleton {ECO:0000269|PubMed:22319451}. Host nucleus
CC {ECO:0000305|PubMed:24204266}. Note=Secreted via type III secretion
CC system (TTSS). {ECO:0000305|PubMed:20636323}.
CC -!- PTM: Autoacetylated at Lys-289; while autoacetylation at Lys-289 is
CC required for virulence function to some extent, it is not essential.
CC {ECO:0000269|PubMed:22319451, ECO:0000269|PubMed:24204266,
CC ECO:0000269|PubMed:26217317}.
CC -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC {ECO:0000305}.
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DR EMBL; AY342395; AAR02168.1; -; Genomic_DNA.
DR EMBL; RBUE01000110; RMU63652.1; -; Genomic_DNA.
DR RefSeq; NP_940719.1; NC_005205.1.
DR RefSeq; WP_011152901.1; NZ_RBUE01000110.1.
DR PDB; 5KLP; X-ray; 2.00 A; A/B/C=29-369.
DR PDB; 5KLQ; X-ray; 3.40 A; A/B/C=29-369.
DR PDBsum; 5KLP; -.
DR PDBsum; 5KLQ; -.
DR AlphaFoldDB; Q6VE93; -.
DR SMR; Q6VE93; -.
DR EnsemblBacteria; RMU63652; RMU63652; ALP25_03258.
DR PATRIC; fig|321.63.peg.4110; -.
DR Proteomes; UP000272344; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0016413; F:O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005083; Ser/Thr_AcTrfase.
DR Pfam; PF03421; Acetyltransf_14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Allosteric enzyme;
KW Host cell membrane; Host cytoplasm; Host cytoskeleton; Host membrane;
KW Host nucleus; Membrane; Plasmid; Secreted; Transferase; Virulence.
FT CHAIN 1..369
FT /note="Serine/threonine-protein acetyltransferase HopZ1a"
FT /id="PRO_0000451626"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /evidence="ECO:0000269|PubMed:27525589"
FT ACT_SITE 170
FT /evidence="ECO:0000269|PubMed:27525589"
FT ACT_SITE 216
FT /evidence="ECO:0000269|PubMed:27525589,
FT ECO:0000305|PubMed:22319451"
FT BINDING 49
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP"
FT BINDING 53
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 106
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 150
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 177
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 211..212
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 222
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 226..229
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 289..290
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 292..295
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 314..317
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 326
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 331..334
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 344..348
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:5KLQ"
FT BINDING 358
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT BINDING 362
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007744|PDB:5KLP, ECO:0007744|PDB:5KLQ"
FT MOD_RES 289
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:22319451,
FT ECO:0000269|PubMed:26217317"
FT MUTAGEN 211
FT /note="K->A: Abolished ability to acetylate host
FT TIFY9/JAZ10; when associate with A-295 and A-348."
FT /evidence="ECO:0000269|PubMed:27525589"
FT MUTAGEN 216
FT /note="C->A: Abolished acetyltransferase activity. Reduced
FT ability to trigger host TIFY/JAZ proteins degradation and
FT altered host infection."
FT /evidence="ECO:0000269|PubMed:22319451,
FT ECO:0000269|PubMed:24204266, ECO:0000269|PubMed:26217317,
FT ECO:0000269|PubMed:27525589"
FT MUTAGEN 226
FT /note="K->E: Abolished binding to 1D-myo-inositol
FT hexakisphosphate and ability to acetylate host
FT TIFY9/JAZ10."
FT /evidence="ECO:0000269|PubMed:27525589"
FT MUTAGEN 289
FT /note="K->E: Abolished binding to 1D-myo-inositol
FT hexakisphosphate and ability to acetylate host
FT TIFY9/JAZ10."
FT /evidence="ECO:0000269|PubMed:27525589"
FT MUTAGEN 289
FT /note="K->R: Abolished autoacetylation and decreased
FT virulence. Virulence is however not abolished."
FT /evidence="ECO:0000269|PubMed:22319451,
FT ECO:0000269|PubMed:26217317"
FT MUTAGEN 295
FT /note="T->A: Abolished ability to acetylate host
FT TIFY9/JAZ10; when associate with A-211 and A-348."
FT /evidence="ECO:0000269|PubMed:27525589"
FT MUTAGEN 326
FT /note="R->E: Abolished binding to 1D-myo-inositol
FT hexakisphosphate and ability to acetylate host
FT TIFY9/JAZ10."
FT /evidence="ECO:0000269|PubMed:27525589"
FT MUTAGEN 348
FT /note="F->A: Abolished ability to acetylate host
FT TIFY9/JAZ10; when associate with A-211 and A-295."
FT /evidence="ECO:0000269|PubMed:27525589"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5KLQ"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:5KLP"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5KLP"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:5KLP"
FT HELIX 351..367
FT /evidence="ECO:0007829|PDB:5KLP"
SQ SEQUENCE 369 AA; 40949 MW; F82EC0225FFBF880 CRC64;
MGNVCVGGSR MSHQVYSPDR ADTPPRSERN TPDRRQRAAG DAERTQSMRL QQKINDLKPY
VRHARGPIKA YGQAALDRAS GKKTSVSFAE LDATHLDAMV YIENQRNPGL NLKHFRDHKE
LIQALQSDGP SAFRAIFPQT CPETGQTLKH HVMADVRLHQ GGAPTIIITE PAVIVGARYQ
QLQRHNLTLE DLSESGVPLS QVAIIETQAQ KTSDDCVMYS LNYAIKAHKN AAQFDDIHHG
LQHGTLSTES ESRARTTLGA LEASSSYSVM HEGAHAAFGA DVLPVDFYKH GASLTQAKQL
MKRPDGRMAG RVNSEGHSEA ENLVQRNQAF RVKRRELLDD ETPSNTQFSA SIDGFRLQEI
KRVLAEEQR
