PTI1_SOLLC
ID PTI1_SOLLC Reviewed; 354 AA.
AC Q41328;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pto-interacting protein 1;
DE Short=Pti1 {ECO:0000303|PubMed:8521516};
DE EC=2.7.11.1 {ECO:0000269|PubMed:8521516};
DE AltName: Full=Pto kinase interactor 1 {ECO:0000312|EMBL:AAC61805.1};
GN Name=PTI1 {ECO:0000312|EMBL:AAC61805.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC61805.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AUTOPHOSPHORYLATION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-96.
RC STRAIN=cv. Rio Grande {ECO:0000312|EMBL:AAC61805.1};
RX PubMed=8521516; DOI=10.1016/0092-8674(95)90208-2;
RA Zhou J., Loh Y.T., Bressan R.A., Martin G.B.;
RT "The tomato gene Pti1 encodes a serine/threonine kinase that is
RT phosphorylated by Pto and is involved in the hypersensitive response.";
RL Cell 83:925-935(1995).
RN [2] {ECO:0000312|EMBL:AAC61805.1}
RP SEQUENCE REVISION TO 283-292 AND C-TERMINUS.
RA Martin G.B.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A serine-threonine kinase involved in the hypersensitive
CC response (HR)-mediated signaling cascade. {ECO:0000269|PubMed:8521516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:8521516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:8521516};
CC -!- SUBUNIT: Interacts with PTO. {ECO:0000269|PubMed:8521516}.
CC -!- INTERACTION:
CC Q41328; Q40234: Pto; Xeno; NbExp=2; IntAct=EBI-8566160, EBI-8566124;
CC -!- PTM: Autophosphorylated at threonine residues and to a lesser extent at
CC serine residues. Phosphorylated in vitro by PTO at threonine residues
CC and to a lesser extent at serine residues.
CC {ECO:0000269|PubMed:8521516}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U28007; AAC61805.1; -; mRNA.
DR RefSeq; NP_001233803.1; NM_001246874.2.
DR RefSeq; XP_010314665.1; XM_010316363.2.
DR AlphaFoldDB; Q41328; -.
DR SMR; Q41328; -.
DR DIP; DIP-42654N; -.
DR IntAct; Q41328; 1.
DR MINT; Q41328; -.
DR STRING; 4081.Solyc12g098980.1.1; -.
DR iPTMnet; Q41328; -.
DR PaxDb; Q41328; -.
DR PRIDE; Q41328; -.
DR EnsemblPlants; Solyc12g098980.2.1; Solyc12g098980.2.1; Solyc12g098980.2.
DR GeneID; 544006; -.
DR Gramene; Solyc12g098980.2.1; Solyc12g098980.2.1; Solyc12g098980.2.
DR KEGG; sly:544006; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q41328; -.
DR OMA; NGPFMAH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q41328; -.
DR Proteomes; UP000004994; Chromosome 12.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hypersensitive response; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..354
FT /note="Pto-interacting protein 1"
FT /id="PRO_0000390698"
FT DOMAIN 68..348
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 96
FT /note="K->N: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:8521516"
SQ SEQUENCE 354 AA; 38540 MW; A6C5346175FCEE97 CRC64;
MSCFSCCDDD DMHRATDNGP FMAHNSAGNN GGQRATESAQ RETQTVNIQP IAVPSIAVDE
LKDITDNFGS KALIGEGSYG RVYHGVLKSG RAAAIKKLDS SKQPDREFLA QVSMVSRLKD
ENVVELLGYC VDGGFRVLAY EYAPNGSLHD ILHGRKGVKG AQPGPVLSWA QRVKIAVGAA
KGLEYLHEKA QPHIIHRDIK SSNILLFDDD VAKIADFDLS NQAPDMAARL HSTRVLGTFG
YHAPEYAMTG QLSSKSDVYS FGVVLLELLT GRKPVDHTLP RGQQSLVTWA TPRLSEDKVK
QCVDARLNTD YPPKAIAKMA AVAALCVQYE ADFRPNMSIV VKALQPLLPR PVPS
