YIAC_ECOLI
ID YIAC_ECOLI Reviewed; 146 AA.
AC P37664; Q2M7L1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Peptidyl-lysine N-acetyltransferase YiaC {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30352934};
DE AltName: Full=KAT {ECO:0000303|PubMed:30352934};
GN Name=yiaC; OrderedLocusNames=b3550, JW3519;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2180922; DOI=10.1128/jb.172.4.2194-2198.1990;
RA Pierson D.E., Campbell A.;
RT "Cloning and nucleotide sequence of bisC, the structural gene for biotin
RT sulfoxide reductase in Escherichia coli.";
RL J. Bacteriol. 172:2194-2198(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PHE-70 AND TYR-115.
RC STRAIN=K12;
RX PubMed=30352934; DOI=10.1128/mbio.01905-18;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Identification of novel protein lysine acetyltransferases in Escherichia
RT coli.";
RL MBio 9:E01905-E01905(2018).
RN [6]
RP ERRATUM OF PUBMED:30352934.
RX PubMed=30967468; DOI=10.1128/mbio.00592-19;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Correction for Christensen et al., 'Identification of novel protein lysine
RT acetyltransferases in Escherichia coli'.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: N-epsilon-lysine acetyltransferase that catalyzes acetylation
CC of a large number of proteins. Overexpression inhibits motility.
CC {ECO:0000269|PubMed:30352934}.
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:30352934};
CC -!- DISRUPTION PHENOTYPE: Mutant shows the same motility as wild-type
CC strain. {ECO:0000269|PubMed:30352934}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M34827; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M34827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00039; AAB18527.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76574.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77745.1; -; Genomic_DNA.
DR PIR; S47771; S47771.
DR RefSeq; NP_418006.1; NC_000913.3.
DR RefSeq; WP_000617473.1; NZ_SSZK01000068.1.
DR AlphaFoldDB; P37664; -.
DR SMR; P37664; -.
DR BioGRID; 4261556; 5.
DR BioGRID; 850814; 1.
DR IntAct; P37664; 3.
DR STRING; 511145.b3550; -.
DR PaxDb; P37664; -.
DR PRIDE; P37664; -.
DR EnsemblBacteria; AAC76574; AAC76574; b3550.
DR EnsemblBacteria; BAE77745; BAE77745; BAE77745.
DR GeneID; 946460; -.
DR KEGG; ecj:JW3519; -.
DR KEGG; eco:b3550; -.
DR PATRIC; fig|1411691.4.peg.3164; -.
DR EchoBASE; EB2179; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_21_2_6; -.
DR InParanoid; P37664; -.
DR OMA; RAVNFYH; -.
DR PhylomeDB; P37664; -.
DR BioCyc; EcoCyc:EG12270-MON; -.
DR BioCyc; MetaCyc:EG12270-MON; -.
DR BRENDA; 2.3.1.286; 2026.
DR PRO; PR:P37664; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:EcoCyc.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..146
FT /note="Peptidyl-lysine N-acetyltransferase YiaC"
FT /id="PRO_0000074614"
FT DOMAIN 1..143
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 70
FT /note="F->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:30352934"
FT MUTAGEN 115
FT /note="Y->A: Loss of activity. Unable to inhibit motility."
FT /evidence="ECO:0000269|PubMed:30352934"
SQ SEQUENCE 146 AA; 17104 MW; A996E3003F07DFB4 CRC64;
MIREAQRSEL PAILELWLES TTWGHPFIKA NYWRDCIPLV RDAYLANAQN WVWEEDGKLL
GFVSIMEGRF LAAMFVAPKA VRRGIGKALM QYVQQRHPHL MLEVYQKNQP AINFYQAQGF
HIVDCAWQDE TQLPTWIMSW PVVQTL
