TTR_PSEAJ
ID TTR_PSEAJ Reviewed; 177 AA.
AC P16966;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acetyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Tabtoxin resistance protein;
GN Name=ttr;
OS Pseudomonas amygdali pv. tabaci (Pseudomonas syringae pv. tabaci).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali.
OX NCBI_TaxID=322;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF03-01075;
RX PubMed=2336364; DOI=10.1093/nar/18.7.1890;
RA Anzai H., Yoneyama K., Yamaguchi I.;
RT "The nucleotide sequence of tabtoxin resistance gene (ttr) of Pseudomonas
RT syringae pv. tabaci.";
RL Nucleic Acids Res. 18:1890-1890(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ACETYL-COA, AND
RP FUNCTION.
RX PubMed=12527305; DOI=10.1016/s0022-2836(02)01284-6;
RA He H., Ding Y., Bartlam M., Sun F., Le Y., Qin X., Tang H., Zhang R.,
RA Joachimiak A., Liu J., Zhao N., Rao Z.;
RT "Crystal structure of tabtoxin resistance protein complexed with acetyl
RT coenzyme A reveals the mechanism for beta-lactam acetylation.";
RL J. Mol. Biol. 325:1019-1030(2003).
CC -!- FUNCTION: Renders tabtoxin-producing pathogens tolerant to their own
CC phytotoxins. {ECO:0000269|PubMed:12527305}.
CC -!- MISCELLANEOUS: Tabtoxin causes wildfire disease of tobacco.
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DR EMBL; X17150; CAA35037.1; -; Genomic_DNA.
DR PIR; S09214; S09214.
DR RefSeq; WP_002555402.1; NZ_RBSE01000043.1.
DR PDB; 1GHE; X-ray; 1.55 A; A/B=1-177.
DR PDB; 1J4J; X-ray; 2.55 A; A/B=1-177.
DR PDBsum; 1GHE; -.
DR PDBsum; 1J4J; -.
DR AlphaFoldDB; P16966; -.
DR SMR; P16966; -.
DR GeneID; 61872015; -.
DR KEGG; ag:CAA35037; -.
DR BioCyc; MetaCyc:MON-20391; -.
DR EvolutionaryTrace; P16966; -.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13673; Acetyltransf_10; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Transferase.
FT CHAIN 1..177
FT /note="Acetyltransferase"
FT /id="PRO_0000065680"
FT DOMAIN 4..174
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 27
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:12527305"
FT BINDING 96..98
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 104..109
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 130..131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 141
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:12527305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1GHE"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1GHE"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:1GHE"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:1GHE"
SQ SEQUENCE 177 AA; 19235 MW; 8D278EC9AB27E9DF CRC64;
MNHAQLRRVT AESFAHYRHG LAQLLFETVH GGASVGFMAD LDMQQAYAWC DGLKADIAAG
SLLLWVVAED DNVLASAQLS LCQKPNGLNR AEVQKLMVLP SARGRGLGRQ LMDEVEQVAV
KHKRGLLHLD TEAGSVAEAF YSALAYTRVG ELPGYCATPD GRLHPTAIYF KTLGQPT