LYSAC_ECOLI
ID LYSAC_ECOLI Reviewed; 886 AA.
AC P76594; Q2MAF2; Q47320;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peptidyl-lysine N-acetyltransferase PatZ {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:21696463, ECO:0000269|PubMed:26251518, ECO:0000269|PubMed:26847092, ECO:0000269|PubMed:27484197, ECO:0000269|PubMed:30352934};
DE AltName: Full=Protein lysine acetyltransferase {ECO:0000303|PubMed:21981926};
GN Name=patZ {ECO:0000303|PubMed:22059728};
GN Synonyms=pka {ECO:0000303|PubMed:21981926}, yfiQ;
GN OrderedLocusNames=b2584, JW2568;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-612.
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=21703240; DOI=10.1016/j.bbrc.2011.06.076;
RA Ma Q., Wood T.K.;
RT "Protein acetylation in prokaryotes increases stress resistance.";
RL Biochem. Biophys. Res. Commun. 410:846-851(2011).
RN [5]
RP FUNCTION IN ACETYLATION OF RNASE R, AND GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21981926; DOI=10.1016/j.molcel.2011.06.037;
RA Liang W., Malhotra A., Deutscher M.P.;
RT "Acetylation regulates the stability of a bacterial protein: growth stage-
RT dependent modification of RNase R.";
RL Mol. Cell 44:160-166(2011).
RN [6]
RP FUNCTION IN ACETYLATION OF RNAP, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x;
RA Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R.,
RA Wolfe A.J.;
RT "Involvement of protein acetylation in glucose-induced transcription of a
RT stress-responsive promoter.";
RL Mol. Microbiol. 81:1190-1204(2011).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=22059728; DOI=10.1111/j.1365-2958.2011.07873.x;
RA Castano-Cerezo S., Bernal V., Blanco-Catala J., Iborra J.L., Canovas M.;
RT "cAMP-CRP co-ordinates the expression of the protein acetylation pathway
RT with central metabolism in Escherichia coli.";
RL Mol. Microbiol. 82:1110-1128(2011).
RN [8]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22124017; DOI=10.1261/rna.030213.111;
RA Liang W., Deutscher M.P.;
RT "Post-translational modification of RNase R is regulated by stress-
RT dependent reduction in the acetylating enzyme Pka (YfiQ).";
RL RNA 18:37-41(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP ACETYLATION, AND MUTAGENESIS OF GLU-809.
RX PubMed=26251518; DOI=10.1074/jbc.m115.649806;
RA de Diego Puente T., Gallego-Jara J., Castano-Cerezo S., Bernal Sanchez V.,
RA Fernandez Espin V., Garcia de la Torre J., Manjon Rubio A.,
RA Canovas Diaz M.;
RT "The protein acetyltransferase PatZ from Escherichia coli is regulated by
RT autoacetylation-induced oligomerization.";
RL J. Biol. Chem. 290:23077-23093(2015).
RN [10]
RP FUNCTION IN ACETYLATION OF RNASE II, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=26847092; DOI=10.1093/nar/gkw053;
RA Song L., Wang G., Malhotra A., Deutscher M.P., Liang W.;
RT "Reversible acetylation on Lys501 regulates the activity of RNase II.";
RL Nucleic Acids Res. 44:1979-1988(2016).
RN [11]
RP FUNCTION IN ACETYLATION OF DNAA, AND CATALYTIC ACTIVITY.
RX PubMed=27484197; DOI=10.1038/srep30837;
RA Zhang Q., Zhou A., Li S., Ni J., Tao J., Lu J., Wan B., Li S., Zhang J.,
RA Zhao S., Zhao G.P., Shao F., Yao Y.F.;
RT "Reversible lysine acetylation is involved in DNA replication initiation by
RT regulating activities of initiator DnaA in Escherichia coli.";
RL Sci. Rep. 6:30837-30837(2016).
RN [12]
RP FUNCTION, OVEREXPRESSION, AND CATALYTIC ACTIVITY.
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 [13]
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: Catalyzes the acetyl-CoA-dependent acetylation of lysine
CC residues of a large number of target proteins. Acetylates RNase R in
CC exponential phase cells and RNase II (PubMed:21981926, PubMed:22124017,
CC PubMed:26847092). Required for the glucose-dependent acetylation on
CC multiple lysines of alpha, beta and beta' RNAP subunits
CC (PubMed:21696463). Also acetylates acetyl-coenzyme A synthetase (Acs)
CC and the chromosomal replication initiator protein DnaA, and inhibits
CC their activity (PubMed:22059728, PubMed:26251518, PubMed:27484197).
CC Overexpression leads to the acetylation of a large number of additional
CC proteins and inhibits motility (PubMed:30352934).
CC {ECO:0000269|PubMed:21696463, ECO:0000269|PubMed:21981926,
CC ECO:0000269|PubMed:22059728, ECO:0000269|PubMed:22124017,
CC ECO:0000269|PubMed:26251518, ECO:0000269|PubMed:26847092,
CC ECO:0000269|PubMed:27484197, 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:21696463, ECO:0000269|PubMed:26251518,
CC ECO:0000269|PubMed:26847092, ECO:0000269|PubMed:27484197,
CC ECO:0000269|PubMed:30352934};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.78 uM for Acs {ECO:0000269|PubMed:26251518};
CC Note=kcat is 1.02 sec(-1) with acetyl-CoA as substrate. kcat is 1.19
CC sec(-1) with Acs as substrate. {ECO:0000269|PubMed:26251518};
CC -!- SUBUNIT: Stable tetramer in solution. Oligomerizes to an octomeric form
CC by autoacetylation. {ECO:0000269|PubMed:26251518}.
CC -!- INTERACTION:
CC P76594; P77802: ecpC; NbExp=4; IntAct=EBI-557388, EBI-561348;
CC P76594; P0A9W0: ulaR; NbExp=4; IntAct=EBI-557388, EBI-560926;
CC -!- INDUCTION: Positively regulated by cAMP-CRP. Up-regulated in the
CC presence of non-PTS carbon sources (PubMed:22059728). According to
CC PubMed:22059728, pka is up-regulated during the stationary phase
CC growth, while according to PubMed:22124017, it is absent from the late
CC exponential and stationary phase cells (PubMed:22059728,
CC PubMed:22124017). {ECO:0000269|PubMed:22059728,
CC ECO:0000269|PubMed:22124017}.
CC -!- PTM: Autoacetylated. Deacetylated by CobB.
CC {ECO:0000269|PubMed:26251518}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has decreased resistance to
CC oxidative and heat stress (PubMed:21703240). Mutant responds poorly to
CC glucose (PubMed:21696463). {ECO:0000269|PubMed:21696463,
CC ECO:0000269|PubMed:21703240}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA
CC ligase alpha subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the acetate CoA ligase
CC beta subunit family. {ECO:0000305}.
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DR EMBL; U00096; AAC75637.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76754.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10925.1; -; Genomic_DNA.
DR PIR; G65036; G65036.
DR RefSeq; NP_417079.1; NC_000913.3.
DR RefSeq; WP_000083005.1; NZ_LN832404.1.
DR AlphaFoldDB; P76594; -.
DR SMR; P76594; -.
DR BioGRID; 4260608; 12.
DR BioGRID; 851394; 3.
DR DIP; DIP-12068N; -.
DR IntAct; P76594; 30.
DR STRING; 511145.b2584; -.
DR jPOST; P76594; -.
DR PaxDb; P76594; -.
DR PRIDE; P76594; -.
DR EnsemblBacteria; AAC75637; AAC75637; b2584.
DR EnsemblBacteria; BAE76754; BAE76754; BAE76754.
DR GeneID; 947056; -.
DR KEGG; ecj:JW2568; -.
DR KEGG; eco:b2584; -.
DR PATRIC; fig|1411691.4.peg.4150; -.
DR EchoBASE; EB3976; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_007415_0_2_6; -.
DR InParanoid; P76594; -.
DR OMA; SFMSQSG; -.
DR PhylomeDB; P76594; -.
DR BioCyc; EcoCyc:G7350-MON; -.
DR BioCyc; MetaCyc:G7350-MON; -.
DR BRENDA; 2.3.1.286; 2026.
DR PRO; PR:P76594; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 2.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..886
FT /note="Peptidyl-lysine N-acetyltransferase PatZ"
FT /id="PRO_0000169272"
FT DOMAIN 487..523
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 726..881
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 809
FT /note="E->A: Decreases activity at low pH (5-7), but does
FT not change activity at high pH."
FT /evidence="ECO:0000269|PubMed:26251518"
FT CONFLICT 506..507
FT /note="ST -> YA (in Ref. 3; BAA10925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 97987 MW; 255944B9E2961251 CRC64;
MSQRGLEALL RPKSIAVIGA SMKPNRAGYL MMRNLLAGGF NGPVLPVTPA WKAVLGVLAW
PDIASLPFTP DLAVLCTNAS RNLALLEELG EKGCKTCIIL SAPASQHEDL RACALRHNMR
LLGPNSLGLL APWQGLNASF SPVPIKRGKL AFISQSAAVS NTILDWAQQR KMGFSYFIAL
GDSLDIDVDE LLDYLARDSK TSAILLYLEQ LSDARRFVSA ARSASRNKPI LVIKSGRSPA
AQRLLNTTAG MDPAWDAAIQ RAGLLRVQDT HELFSAVETL SHMRPLRGDR LMIISNGAAP
AALALDALWS RNGKLATLSE ETCQKLRDAL PEHVAISNPL DLRDDASSEH YIKTLDILLH
SQDFDALMVI HSPSAAAPAT ESAQVLIEAV KHHPRSKYVS LLTNWCGEHS SQEARRLFSE
AGLPTYRTPE GTITAFMHMV EYRRNQKQLR ETPALPSNLT SNTAEAHLLL QQAIAEGATS
LDTHEVQPIL QAYGMNTLPT WIASDSTEAV HIAEQIGYPV ALKLRSPDIP HKSEVQGVML
YLRTANEVQQ AANAIFDRVK MAWPQARVHG LLVQSMANRA GAQELRVVVE HDPVFGPLIM
LGEGGVEWRP EDQAVVALPP LNMNLARYLV IQGIKSKKIR ARSALRPLDV AGLSQLLVQV
SNLIVDCPEI QRLDIHPLLA SGSEFTALDV TLDISPFEGD NESRLAVRPY PHQLEEWVEL
KNGERCLFRP ILPEDEPQLQ QFISRVTKED LYYRYFSEIN EFTHEDLANM TQIDYDREMA
FVAVRRIDQT EEILGVTRAI SDPDNIDAEF AVLVRSDLKG LGLGRRLMEK LITYTRDHGL
QRLNGITMPN NRGMVALARK LGFNVDIQLE EGIVGLTLNL AQREES
