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Database: UniProt
Entry: B2VJH3_ERWT9
LinkDB: B2VJH3_ERWT9
Original site: B2VJH3_ERWT9 
ID   B2VJH3_ERWT9            Unreviewed;       396 AA.
AC   B2VJH3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Virulence/avirulence effector protein homolog {ECO:0000313|EMBL:CAO95585.1};
GN   OrderedLocusNames=ETA_05390 {ECO:0000313|EMBL:CAO95585.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO95585.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO95585.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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:0000256|ARBA:ARBA00023671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC         Evidence={ECO:0000256|ARBA:ARBA00023671};
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:0000256|ARBA:ARBA00023676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC         Evidence={ECO:0000256|ARBA:ARBA00023676};
CC   -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC       {ECO:0000256|ARBA:ARBA00023785}.
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DR   EMBL; CU468135; CAO95585.1; -; Genomic_DNA.
DR   RefSeq; WP_012440293.1; NC_010694.1.
DR   AlphaFoldDB; B2VJH3; -.
DR   STRING; 465817.ETA_05390; -.
DR   KEGG; eta:ETA_05390; -.
DR   eggNOG; ENOG5032VKN; Bacteria.
DR   HOGENOM; CLU_058396_0_0_6; -.
DR   OrthoDB; 8888419at2; -.
DR   Proteomes; UP000001726; Chromosome.
DR   InterPro; IPR005083; Ser/Thr_AcTrfase.
DR   Pfam; PF03421; Acetyltransf_14; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001726};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  43785 MW;  C3680971738C4D4F CRC64;
     MNISGLRAGQ GSPSQQTDRA ASSSTQASPA PAGRRLQRQD ALPTNTRYQA SQMPATPERA
     RVAARNSAGA SSSAAHAQPS LSLSRQNAHR EDPALARFHH QMQQSTKMSR ADPLPEKPQV
     VPKRLQEKID AINLPRLKKL DNNLHEYGKM ATELAKEGSG SSSALTRMDK KVLPLLADAE
     NARHPGLNLH VYKKGEECYQ AIKDQHKSVQ QSGQPKTMRA LYPPFKGMPD HHIALDIQLR
     PGHRPSIVGF ESALGHMVEH LKQGIAEGVR GAKVHMVGNT IQNSQWDCTM YSLSNALKSF
     KHHDEYTARL HKGEKVPVPA EFFKHAQSKS SVEGKPHQDA VVTKDKGGLH AETLLHRNLA
     YRADRFDRAY STSIEGFRMQ EIQRAGEHLA AKKHKS
//
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