YJAB_ECOLI
ID YJAB_ECOLI Reviewed; 147 AA.
AC P09163; Q2M6U2; Q47614;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Peptidyl-lysine N-acetyltransferase YjaB {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30352934};
DE AltName: Full=KAT {ECO:0000303|PubMed:30352934};
GN Name=yjaB; OrderedLocusNames=b4012, JW3972;
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=2412207; DOI=10.1093/nar/13.15.5515;
RA Liebke H., Hatfull G.;
RT "The sequence of the distal end of the E. coli ribosomal RNA rrnE operon
RT indicates conserved features are shared by rrn operons.";
RL Nucleic Acids Res. 13:5515-5525(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-147.
RC STRAIN=K12;
RX PubMed=1709493; DOI=10.1093/nar/19.8.1845;
RA Albrechtsen B., Ross B.M., Squires C., Squires C.L.;
RT "Transcriptional termination sequence at the end of the Escherichia coli
RT ribosomal RNA G operon: complex terminators and antitermination.";
RL Nucleic Acids Res. 19:1845-1852(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-117.
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 [7]
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).
RN [8] {ECO:0007744|PDB:2KCW}
RP STRUCTURE BY NMR, AND ACETYL-COA-BINDING.
RX PubMed=19343803; DOI=10.1002/prot.22407;
RA Lu J., Wang X., Xia B., Jin C.;
RT "Solution structure of Apo-YjaB from Escherichia coli.";
RL Proteins 76:261-265(2009).
CC -!- FUNCTION: N-epsilon-lysine acetyltransferase that catalyzes acetylation
CC of a large number of proteins (PubMed:30352934). Binds acetyl-CoA
CC (PubMed:19343803). {ECO:0000269|PubMed:19343803,
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 -!- SIMILARITY: Belongs to the acetyltransferase family.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02800; CAA26570.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43106.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76982.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78014.1; -; Genomic_DNA.
DR EMBL; X56780; CAA40098.1; -; Genomic_DNA.
DR PIR; B24340; Q3ECE6.
DR RefSeq; NP_418436.1; NC_000913.3.
DR RefSeq; WP_000237004.1; NZ_SSZK01000049.1.
DR PDB; 2KCW; NMR; -; A=1-147.
DR PDBsum; 2KCW; -.
DR AlphaFoldDB; P09163; -.
DR BMRB; P09163; -.
DR SMR; P09163; -.
DR BioGRID; 4262085; 9.
DR IntAct; P09163; 1.
DR STRING; 511145.b4012; -.
DR PaxDb; P09163; -.
DR PRIDE; P09163; -.
DR EnsemblBacteria; AAC76982; AAC76982; b4012.
DR EnsemblBacteria; BAE78014; BAE78014; BAE78014.
DR GeneID; 948514; -.
DR KEGG; ecj:JW3972; -.
DR KEGG; eco:b4012; -.
DR PATRIC; fig|1411691.4.peg.2701; -.
DR EchoBASE; EB1192; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_21_0_6; -.
DR InParanoid; P09163; -.
DR OMA; KIEMLFI; -.
DR PhylomeDB; P09163; -.
DR BioCyc; EcoCyc:EG11207-MON; -.
DR BioCyc; MetaCyc:EG11207-MON; -.
DR BRENDA; 2.3.1.286; 2026.
DR EvolutionaryTrace; P09163; -.
DR PRO; PR:P09163; -.
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; PF13673; Acetyltransf_10; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..147
FT /note="Peptidyl-lysine N-acetyltransferase YjaB"
FT /id="PRO_0000074615"
FT DOMAIN 3..144
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 117
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30352934"
FT CONFLICT 128
FT /note="S -> M (in Ref. 5; CAA40098)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="DD -> GK (in Ref. 5; CAA40098)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> V (in Ref. 5; CAA40098)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2KCW"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:2KCW"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:2KCW"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2KCW"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2KCW"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2KCW"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2KCW"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2KCW"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2KCW"
SQ SEQUENCE 147 AA; 16447 MW; 9AABD7C5AFC3D61D CRC64;
MVISIRRSRH EEGEELVAIW CRSVDATHDF LSAEYRTELE DLVRSFLPEA PLWVAVNERD
QPVGFMLLSG QHMDALFIDP DVRGCGVGRV LVEHALSMAP ELTTNVNEQN EQAVGFYKKV
GFKVTGRSEV DDLGKPYPLL NLAYVGA
