ID   Y4LO_SINFN              Reviewed;         260 AA.
AC   P55555;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Serine/threonine-protein acetyltransferase NGR_a02610;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:O68718};
GN   OrderedLocusNames=NGR_a02610; ORFNames=y4lO;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Serine/threonine-protein acetyltransferase translocated into
CC       infected cells, which mediates acetylation of serine and threonine
CC       residues of host target proteins. {ECO:0000250|UniProtKB:O68718}.
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   -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC       {ECO:0000305}.
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DR   EMBL; U00090; AAB92459.1; -; Genomic_DNA.
DR   RefSeq; NP_443964.1; NC_000914.2.
DR   RefSeq; WP_010875286.1; NC_000914.2.
DR   AlphaFoldDB; P55555; -.
DR   SMR; P55555; -.
DR   EnsemblBacteria; AAB92459; AAB92459; NGR_a02610.
DR   KEGG; rhi:NGR_a02610; -.
DR   eggNOG; ENOG5032VKN; Bacteria.
DR   HOGENOM; CLU_1069097_0_0_5; -.
DR   OrthoDB; 1550728at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005083; Ser/Thr_AcTrfase.
DR   Pfam; PF03421; Acetyltransf_14; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Plasmid; Reference proteome; Transferase.
FT   CHAIN           1..260
FT                   /note="Serine/threonine-protein acetyltransferase
FT                   NGR_a02610"
FT                   /id="PRO_0000200908"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   BINDING         123
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   BINDING         180..181
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
SQ   SEQUENCE   260 AA;  29079 MW;  96E2FA32A2FA87C4 CRC64;
     MQLSRRAEIG NPSSRNLSPR INEKVELLGQ ALEHARRAGM SSSLMEYGRQ VARHLSANVQ
     PDEKILSLDI RNLPLLAASY NRRYPDLDLR HMDSPARFFD ALNDRSSDGA WRAVVRLADG
     EQHHVAADVR TRAGAAPTII VMEGANFYTF VASYFKLRGD SFRQLGTQAK WAFIEVGAQK
     SAADCVMFGV QFALAAYREL PTFDAWHDNL HHHGTIAHEG DYSSDYMPRR HAGICANKPF
     SWGEVPPSDL LQALSLQQCN