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Protein

Protein lysine acetyltransferase Pka

Gene

pka

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates RNase R in exponential phase cells. Also required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. May acetylate Acs and inhibit its activity.4 Publications

GO - Molecular functioni

  • ATP binding Source: InterPro
  • cofactor binding Source: InterPro
  • metal ion binding Source: InterPro
  • peptide-lysine-N-acetyltransferase activity Source: EcoCyc
  • peptidyl-lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: EcoliWiki

GO - Biological processi

  • internal peptidyl-lysine acetylation Source: EcoCyc
  • protein homotetramerization Source: EcoCyc
  • regulation of protein homooligomerization Source: EcoCyc
  • response to heat Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:G7350-MONOMER.
ECOL316407:JW2568-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lysine acetyltransferase Pka (EC:2.3.1.-)
Gene namesi
Name:pka
Synonyms:patZ, yfiQ
Ordered Locus Names:b2584, JW2568
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14224. pka.

Pathology & Biotechi

Disruption phenotypei

Deletion mutant has decreased resistance to oxidative and heat stress. Mutant responds poorly to glucose.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 886886Protein lysine acetyltransferase PkaPRO_0000169272Add
BLAST

Proteomic databases

EPDiP76594.
PaxDbiP76594.
PRIDEiP76594.

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.2 Publications

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ecpCP778024EBI-557388,EBI-561348

Protein-protein interaction databases

BioGridi4260608. 9 interactions.
DIPiDIP-12068N.
IntActiP76594. 29 interactions.
MINTiMINT-1243710.
STRINGi511145.b2584.

Structurei

3D structure databases

ProteinModelPortaliP76594.
SMRiP76594. Positions 6-445, 465-679, 718-862.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini487 – 52337ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini726 – 881156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

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
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CD5. Bacteria.
COG0454. LUCA.
COG1042. LUCA.
HOGENOMiHOG000220090.
InParanoidiP76594.
KOiK09181.
OMAiIVIYMES.
OrthoDBiEOG6FFS5B.
PhylomeDBiP76594.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR003781. CoA-bd.
IPR000182. GNAT_dom.
IPR016040. NAD(P)-bd_dom.
IPR032875. Succ_CoA_lig_flav_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF13380. CoA_binding_2. 1 hit.
PF13607. Succ_CoA_lig. 1 hit.
[Graphical view]
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 2 hits.
SSF55729. SSF55729. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76594-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:886
Mass (Da):97,987
Last modified:February 1, 1997 - v1
Checksum:i255944B9E2961251
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti506 – 5072ST → YA in BAA10925 (Ref. 3) Curated

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.
PIRiG65036.
RefSeqiNP_417079.1. NC_000913.3.
WP_000083005.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75637; AAC75637; b2584.
BAE76754; BAE76754; BAE76754.
GeneIDi947056.
KEGGiecj:JW2568.
eco:b2584.
PATRICi32120569. VBIEscCol129921_2687.

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.
PIRiG65036.
RefSeqiNP_417079.1. NC_000913.3.
WP_000083005.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76594.
SMRiP76594. Positions 6-445, 465-679, 718-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260608. 9 interactions.
DIPiDIP-12068N.
IntActiP76594. 29 interactions.
MINTiMINT-1243710.
STRINGi511145.b2584.

Proteomic databases

EPDiP76594.
PaxDbiP76594.
PRIDEiP76594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75637; AAC75637; b2584.
BAE76754; BAE76754; BAE76754.
GeneIDi947056.
KEGGiecj:JW2568.
eco:b2584.
PATRICi32120569. VBIEscCol129921_2687.

Organism-specific databases

EchoBASEiEB3976.
EcoGeneiEG14224. pka.

Phylogenomic databases

eggNOGiENOG4105CD5. Bacteria.
COG0454. LUCA.
COG1042. LUCA.
HOGENOMiHOG000220090.
InParanoidiP76594.
KOiK09181.
OMAiIVIYMES.
OrthoDBiEOG6FFS5B.
PhylomeDBiP76594.

Enzyme and pathway databases

BioCyciEcoCyc:G7350-MONOMER.
ECOL316407:JW2568-MONOMER.

Miscellaneous databases

PROiP76594.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR003781. CoA-bd.
IPR000182. GNAT_dom.
IPR016040. NAD(P)-bd_dom.
IPR032875. Succ_CoA_lig_flav_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF13380. CoA_binding_2. 1 hit.
PF13607. Succ_CoA_lig. 1 hit.
[Graphical view]
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 2 hits.
SSF55729. SSF55729. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Nashimoto H., Saito N.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-612.
    Strain: K12.
  4. "Protein acetylation in prokaryotes increases stress resistance."
    Ma Q., Wood T.K.
    Biochem. Biophys. Res. Commun. 410:846-851(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  5. "Acetylation regulates the stability of a bacterial protein: growth stage-dependent modification of RNase R."
    Liang W., Malhotra A., Deutscher M.P.
    Mol. Cell 44:160-166(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLATION OF RNASE R, GENE NAME.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter."
    Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., Wolfe A.J.
    Mol. Microbiol. 81:1190-1204(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLATION OF RNAP, DISRUPTION PHENOTYPE.
  7. "cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli."
    Castano-Cerezo S., Bernal V., Blanco-Catala J., Iborra J.L., Canovas M.
    Mol. Microbiol. 82:1110-1128(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: K12 / BW25113.
  8. "Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)."
    Liang W., Deutscher M.P.
    RNA 18:37-41(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiPKA_ECOLI
AccessioniPrimary (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: March 16, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.