UniProtKB - P76594 (LYSAC_ECOLI)
Protein
Peptidyl-lysine N-acetyltransferase PatZ
Gene
patZ
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II (PubMed:21981926, PubMed:22124017, PubMed:26847092). Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits (PubMed:21696463). Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity (PubMed:22059728, PubMed:26251518, PubMed:27484197). Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility (PubMed:30352934).8 Publications
Catalytic activityi
Kineticsi
kcat is 1.02 sec(-1) with acetyl-CoA as substrate. kcat is 1.19 sec(-1) with Acs as substrate.1 Publication
- KM=14.78 µM for Acs1 Publication
GO - Molecular functioni
- ATP binding Source: InterPro
- identical protein binding Source: EcoCyc
- metal ion binding Source: InterPro
- peptide-lysine-N-acetyltransferase activity Source: EcoCyc
- peptidyl-lysine acetyltransferase activity Source: EcoliWiki
GO - Biological processi
- internal peptidyl-lysine acetylation Source: EcoCyc
- regulation of protein homooligomerization Source: EcoCyc
- response to heat Source: EcoCyc
- response to oxidative stress Source: EcoCyc
Keywordsi
Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BioCyci | EcoCyc:G7350-MONOMER MetaCyc:G7350-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Peptidyl-lysine N-acetyltransferase PatZCurated (EC:2.3.1.-5 Publications)Alternative name(s): Protein lysine acetyltransferase1 Publication |
Gene namesi | Name:patZ1 Publication Synonyms:pka1 Publication, yfiQ Ordered Locus Names:b2584, JW2568 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Deletion mutant has decreased resistance to oxidative and heat stress (PubMed:21703240). Mutant responds poorly to glucose (PubMed:21696463).2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 809 | E → A: Decreases activity at low pH (5-7), but does not change activity at high pH. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000169272 | 1 – 886 | Peptidyl-lysine N-acetyltransferase PatZAdd BLAST | 886 |
Post-translational modificationi
Autoacetylated. Deacetylated by CobB.1 Publication
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P76594 |
PaxDbi | P76594 |
PRIDEi | P76594 |
Expressioni
Inductioni
Positively regulated by cAMP-CRP. Up-regulated in the presence of non-PTS carbon sources (PubMed:22059728). According to PubMed:22059728, pka is up-regulated during the stationary phase growth, while according to PubMed:22124017, it is absent from the late exponential and stationary phase cells (PubMed:22059728, PubMed:22124017).2 Publications
Interactioni
Subunit structurei
Stable tetramer in solution. Oligomerizes to an octomeric form by autoacetylation.
1 PublicationBinary interactionsi
Hide detailsGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4260608, 12 interactors 851394, 3 interactors |
DIPi | DIP-12068N |
IntActi | P76594, 30 interactors |
STRINGi | 511145.b2584 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 487 – 523 | ATP-graspPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 726 – 881 | N-acetyltransferasePROSITE-ProRule annotationAdd BLAST | 156 |
Sequence similaritiesi
In the N-terminal section; belongs to the acetate CoA ligase alpha subunit family.Curated
In the central section; belongs to the acetate CoA ligase beta subunit family.Curated
Phylogenomic databases
eggNOGi | COG0045, Bacteria COG1042, Bacteria COG1670, Bacteria |
HOGENOMi | CLU_007415_0_2_6 |
InParanoidi | P76594 |
PhylomeDBi | P76594 |
Family and domain databases
Gene3Di | 3.30.1490.20, 1 hit 3.40.50.261, 2 hits |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR003781, CoA-bd IPR000182, GNAT_dom IPR036291, NAD(P)-bd_dom_sf IPR032875, Succ_CoA_lig_flav_dom IPR016102, Succinyl-CoA_synth-like |
Pfami | View protein in Pfam PF00583, Acetyltransf_1, 1 hit PF13380, CoA_binding_2, 1 hit PF13607, Succ_CoA_lig, 1 hit |
SMARTi | View protein in SMART SM00881, CoA_binding, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF52210, SSF52210, 2 hits SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 1 hit PS51186, GNAT, 1 hit |
i Sequence
Sequence statusi: Complete.
P76594-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSQRGLEALL RPKSIAVIGA SMKPNRAGYL MMRNLLAGGF NGPVLPVTPA
60 70 80 90 100
WKAVLGVLAW PDIASLPFTP DLAVLCTNAS RNLALLEELG EKGCKTCIIL
110 120 130 140 150
SAPASQHEDL RACALRHNMR LLGPNSLGLL APWQGLNASF SPVPIKRGKL
160 170 180 190 200
AFISQSAAVS NTILDWAQQR KMGFSYFIAL GDSLDIDVDE LLDYLARDSK
210 220 230 240 250
TSAILLYLEQ LSDARRFVSA ARSASRNKPI LVIKSGRSPA AQRLLNTTAG
260 270 280 290 300
MDPAWDAAIQ RAGLLRVQDT HELFSAVETL SHMRPLRGDR LMIISNGAAP
310 320 330 340 350
AALALDALWS RNGKLATLSE ETCQKLRDAL PEHVAISNPL DLRDDASSEH
360 370 380 390 400
YIKTLDILLH SQDFDALMVI HSPSAAAPAT ESAQVLIEAV KHHPRSKYVS
410 420 430 440 450
LLTNWCGEHS SQEARRLFSE AGLPTYRTPE GTITAFMHMV EYRRNQKQLR
460 470 480 490 500
ETPALPSNLT SNTAEAHLLL QQAIAEGATS LDTHEVQPIL QAYGMNTLPT
510 520 530 540 550
WIASDSTEAV HIAEQIGYPV ALKLRSPDIP HKSEVQGVML YLRTANEVQQ
560 570 580 590 600
AANAIFDRVK MAWPQARVHG LLVQSMANRA GAQELRVVVE HDPVFGPLIM
610 620 630 640 650
LGEGGVEWRP EDQAVVALPP LNMNLARYLV IQGIKSKKIR ARSALRPLDV
660 670 680 690 700
AGLSQLLVQV SNLIVDCPEI QRLDIHPLLA SGSEFTALDV TLDISPFEGD
710 720 730 740 750
NESRLAVRPY PHQLEEWVEL KNGERCLFRP ILPEDEPQLQ QFISRVTKED
760 770 780 790 800
LYYRYFSEIN EFTHEDLANM TQIDYDREMA FVAVRRIDQT EEILGVTRAI
810 820 830 840 850
SDPDNIDAEF AVLVRSDLKG LGLGRRLMEK LITYTRDHGL QRLNGITMPN
860 870 880
NRGMVALARK LGFNVDIQLE EGIVGLTLNL AQREES
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 506 – 507 | ST → YA in BAA10925 (Ref. 3) Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75637.1 AP009048 Genomic DNA Translation: BAE76754.1 D64044 Genomic DNA Translation: BAA10925.1 |
PIRi | G65036 |
RefSeqi | NP_417079.1, NC_000913.3 WP_000083005.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75637; AAC75637; b2584 BAE76754; BAE76754; BAE76754 |
GeneIDi | 57732313 947056 |
KEGGi | ecj:JW2568 eco:b2584 |
PATRICi | fig|1411691.4.peg.4150 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75637.1 AP009048 Genomic DNA Translation: BAE76754.1 D64044 Genomic DNA Translation: BAA10925.1 |
PIRi | G65036 |
RefSeqi | NP_417079.1, NC_000913.3 WP_000083005.1, NZ_LN832404.1 |
3D structure databases
SMRi | P76594 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4260608, 12 interactors 851394, 3 interactors |
DIPi | DIP-12068N |
IntActi | P76594, 30 interactors |
STRINGi | 511145.b2584 |
Proteomic databases
jPOSTi | P76594 |
PaxDbi | P76594 |
PRIDEi | P76594 |
Genome annotation databases
EnsemblBacteriai | AAC75637; AAC75637; b2584 BAE76754; BAE76754; BAE76754 |
GeneIDi | 57732313 947056 |
KEGGi | ecj:JW2568 eco:b2584 |
PATRICi | fig|1411691.4.peg.4150 |
Organism-specific databases
EchoBASEi | EB3976 |
Phylogenomic databases
eggNOGi | COG0045, Bacteria COG1042, Bacteria COG1670, Bacteria |
HOGENOMi | CLU_007415_0_2_6 |
InParanoidi | P76594 |
PhylomeDBi | P76594 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7350-MONOMER MetaCyc:G7350-MONOMER |
Miscellaneous databases
PROi | PR:P76594 |
Family and domain databases
Gene3Di | 3.30.1490.20, 1 hit 3.40.50.261, 2 hits |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR003781, CoA-bd IPR000182, GNAT_dom IPR036291, NAD(P)-bd_dom_sf IPR032875, Succ_CoA_lig_flav_dom IPR016102, Succinyl-CoA_synth-like |
Pfami | View protein in Pfam PF00583, Acetyltransf_1, 1 hit PF13380, CoA_binding_2, 1 hit PF13607, Succ_CoA_lig, 1 hit |
SMARTi | View protein in SMART SM00881, CoA_binding, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF52210, SSF52210, 2 hits SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 1 hit PS51186, GNAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LYSAC_ECOLI | |
Accessioni | P76594Primary (citable) accession number: P76594 Secondary accession number(s): Q2MAF2, Q47320 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | February 1, 1997 | |
Last modified: | February 10, 2021 | |
This is version 146 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families