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Protein

Polyphosphate kinase

Gene

ppk

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

Functioni

Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG) synthesis and autophosphorylation.2 Publications

Catalytic activityi

ATP + (phosphate)(n) = ADP + (phosphate)(n+1).UniRule annotation3 Publications

Cofactori

Mg2+UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45ATPUniRule annotationCombined sources1
Metal bindingi375MagnesiumUniRule annotationCombined sources1
Metal bindingi405MagnesiumUniRule annotationCombined sources1
Active sitei435Phosphohistidine intermediateUniRule annotation1 Publication1 Publication1
Binding sitei468ATPUniRule annotationCombined sources1
Binding sitei564ATPUniRule annotationCombined sources1
Binding sitei592ATPUniRule annotationCombined sources1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • diphosphotransferase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • phosphotransferase activity, phosphate group as acceptor Source: EcoCyc
  • polyphosphate:AMP phosphotransferase activity Source: EcoCyc
  • polyphosphate kinase activity Source: EcoCyc

GO - Biological processi

  • ATP generation from ADP Source: EcoCyc
  • polyphosphate biosynthetic process Source: EcoCyc
  • protein autophosphorylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PPK-MONOMER.
ECOL316407:JW2486-MONOMER.
MetaCyc:PPK-MONOMER.
BRENDAi2.7.4.1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphosphate kinaseUniRule annotation (EC:2.7.4.1UniRule annotation3 Publications)
Alternative name(s):
ATP-polyphosphate phosphotransferaseUniRule annotation
Polyphosphoric acid kinaseUniRule annotation
Gene namesi
Name:ppkUniRule annotation
Ordered Locus Names:b2501, JW2486
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11510. ppk.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Associated with the outer membrane in overproducing cells.1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • periplasmic side of cell outer membrane Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
  • polyphosphate kinase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi375R → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi380S → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi424H → Q: No effect on enzyme activity. 1 Publication1
Mutagenesisi435H → A or Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi454H → A or Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi488F → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi507P → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi564R → A: Loss of enzyme activity, but retains low autophosphorylation activity. 1 Publication1
Mutagenesisi592H → Q: Slightly reduced enzyme activity. 1 Publication1
Mutagenesisi621R → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi674Q → A: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001286402 – 688Polyphosphate kinaseAdd BLAST687

Post-translational modificationi

An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.UniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0A7B1.
PRIDEiP0A7B1.

Interactioni

Subunit structurei

Homotetramer (PubMed:1331061). Dimer of dimers (PubMed:10660553, PubMed:15947782). The diverse functions of this enzyme involve different subunit organizations and conformations (PubMed:10660553).3 Publications

Protein-protein interaction databases

BioGridi4261066. 17 interactors.
DIPiDIP-36218N.
IntActiP0A7B1. 29 interactors.
MINTiMINT-1244108.
STRINGi511145.b2501.

Structurei

Secondary structure

1688
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 26Combined sources17
Helixi32 – 51Combined sources20
Helixi53 – 67Combined sources15
Helixi73 – 103Combined sources31
Turni104 – 106Combined sources3
Beta strandi108 – 110Combined sources3
Helixi112 – 114Combined sources3
Helixi119 – 130Combined sources12
Helixi132 – 134Combined sources3
Turni146 – 149Combined sources4
Beta strandi155 – 163Combined sources9
Beta strandi166 – 173Combined sources8
Turni176 – 178Combined sources3
Beta strandi181 – 184Combined sources4
Beta strandi188 – 190Combined sources3
Beta strandi195 – 198Combined sources4
Helixi199 – 211Combined sources13
Turni212 – 214Combined sources3
Beta strandi218 – 229Combined sources12
Turni235 – 238Combined sources4
Beta strandi241 – 243Combined sources3
Turni253 – 255Combined sources3
Beta strandi260 – 264Combined sources5
Helixi270 – 279Combined sources10
Beta strandi284 – 290Combined sources7
Helixi297 – 302Combined sources6
Helixi309 – 311Combined sources3
Helixi322 – 325Combined sources4
Helixi332 – 338Combined sources7
Beta strandi341 – 345Combined sources5
Helixi351 – 362Combined sources12
Beta strandi366 – 375Combined sources10
Helixi381 – 391Combined sources11
Beta strandi395 – 400Combined sources6
Turni407 – 415Combined sources9
Helixi416 – 420Combined sources5
Beta strandi424 – 427Combined sources4
Beta strandi437 – 445Combined sources9
Beta strandi448 – 458Combined sources11
Helixi464 – 466Combined sources3
Beta strandi468 – 475Combined sources8
Helixi478 – 492Combined sources15
Beta strandi504 – 506Combined sources3
Helixi510 – 526Combined sources17
Beta strandi533 – 538Combined sources6
Helixi543 – 554Combined sources12
Beta strandi559 – 565Combined sources7
Turni574 – 576Combined sources3
Beta strandi580 – 585Combined sources6
Beta strandi587 – 591Combined sources5
Beta strandi595 – 598Combined sources4
Helixi600 – 602Combined sources3
Beta strandi605 – 610Combined sources6
Helixi615 – 619Combined sources5
Beta strandi620 – 627Combined sources8
Helixi631 – 645Combined sources15
Beta strandi649 – 653Combined sources5
Helixi673 – 684Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XDOX-ray3.00A/B2-688[»]
1XDPX-ray2.50A/B2-688[»]
ProteinModelPortaliP0A7B1.
SMRiP0A7B1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7B1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini430 – 464PLD phosphodiesteraseUniRule annotationAdd BLAST35

Sequence similaritiesi

Belongs to the polyphosphate kinase family.UniRule annotation
Contains 1 PLD phosphodiesterase domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CUU. Bacteria.
COG0855. LUCA.
HOGENOMiHOG000248949.
InParanoidiP0A7B1.
KOiK00937.
OMAiLSSMIHA.
PhylomeDBiP0A7B1.

Family and domain databases

Gene3Di3.30.1840.10. 1 hit.
HAMAPiMF_00347. Polyphosphate_kinase. 1 hit.
InterProiIPR001736. PLipase_D/transphosphatidylase.
IPR003414. PP_kinase.
IPR024953. PP_kinase_middle.
IPR025200. PPK_C_dom.
IPR025198. PPK_N_dom.
[Graphical view]
PfamiPF02503. PP_kinase. 1 hit.
PF13090. PP_kinase_C. 1 hit.
PF13089. PP_kinase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF015589. PP_kinase. 1 hit.
SUPFAMiSSF140356. SSF140356. 1 hit.
TIGRFAMsiTIGR03705. poly_P_kin. 1 hit.
PROSITEiPS50035. PLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7B1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQEKLYIEK ELSWLSFNER VLQEAADKSN PLIERMRFLG IYSNNLDEFY
60 70 80 90 100
KVRFAELKRR IIISEEQGSN SHSRHLLGKI QSRVLKADQE FDGLYNELLL
110 120 130 140 150
EMARNQIFLI NERQLSVNQQ NWLRHYFKQY LRQHITPILI NPDTDLVQFL
160 170 180 190 200
KDDYTYLAVE IIRGDTIRYA LLEIPSDKVP RFVNLPPEAP RRRKPMILLD
210 220 230 240 250
NILRYCLDDI FKGFFDYDAL NAYSMKMTRD AEYDLVHEME ASLMELMSSS
260 270 280 290 300
LKQRLTAEPV RFVYQRDMPN ALVEVLREKL TISRYDSIVP GGRYHNFKDF
310 320 330 340 350
INFPNVGKAN LVNKPLPRLR HIWFDKAQFR NGFDAIRERD VLLYYPYHTF
360 370 380 390 400
EHVLELLRQA SFDPSVLAIK INIYRVAKDS RIIDSMIHAA HNGKKVTVVV
410 420 430 440 450
ELQARFDEEA NIHWAKRLTE AGVHVIFSAP GLKIHAKLFL ISRKENGEVV
460 470 480 490 500
RYAHIGTGNF NEKTARLYTD YSLLTADARI TNEVRRVFNF IENPYRPVTF
510 520 530 540 550
DYLMVSPQNS RRLLYEMVDR EIANAQQGLP SGITLKLNNL VDKGLVDRLY
560 570 580 590 600
AASSSGVPVN LLVRGMCSLI PNLEGISDNI RAISIVDRYL EHDRVYIFEN
610 620 630 640 650
GGDKKVYLSS ADWMTRNIDY RIEVATPLLD PRLKQRVLDI IDILFSDTVK
660 670 680
ARYIDKELSN RYVPRGNRRK VRAQLAIYDY IKSLEQPE
Length:688
Mass (Da):80,432
Last modified:January 23, 2007 - v2
Checksum:iE1EA6C53432E6935
GO

Sequence cautioni

The sequence AAA83900 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03719 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75554.1.
AP009048 Genomic DNA. Translation: BAA16389.1.
M13747 Genomic DNA. Translation: AAA83900.1. Different initiation.
L06129 Genomic DNA. No translation available.
PIRiA44306.
RefSeqiNP_416996.1. NC_000913.3.
WP_000529576.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75554; AAC75554; b2501.
BAA16389; BAA16389; BAA16389.
GeneIDi946971.
KEGGiecj:JW2486.
eco:b2501.
PATRICi32120391. VBIEscCol129921_2598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03719 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75554.1.
AP009048 Genomic DNA. Translation: BAA16389.1.
M13747 Genomic DNA. Translation: AAA83900.1. Different initiation.
L06129 Genomic DNA. No translation available.
PIRiA44306.
RefSeqiNP_416996.1. NC_000913.3.
WP_000529576.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XDOX-ray3.00A/B2-688[»]
1XDPX-ray2.50A/B2-688[»]
ProteinModelPortaliP0A7B1.
SMRiP0A7B1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261066. 17 interactors.
DIPiDIP-36218N.
IntActiP0A7B1. 29 interactors.
MINTiMINT-1244108.
STRINGi511145.b2501.

Proteomic databases

PaxDbiP0A7B1.
PRIDEiP0A7B1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75554; AAC75554; b2501.
BAA16389; BAA16389; BAA16389.
GeneIDi946971.
KEGGiecj:JW2486.
eco:b2501.
PATRICi32120391. VBIEscCol129921_2598.

Organism-specific databases

EchoBASEiEB1472.
EcoGeneiEG11510. ppk.

Phylogenomic databases

eggNOGiENOG4105CUU. Bacteria.
COG0855. LUCA.
HOGENOMiHOG000248949.
InParanoidiP0A7B1.
KOiK00937.
OMAiLSSMIHA.
PhylomeDBiP0A7B1.

Enzyme and pathway databases

BioCyciEcoCyc:PPK-MONOMER.
ECOL316407:JW2486-MONOMER.
MetaCyc:PPK-MONOMER.
BRENDAi2.7.4.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A7B1.
PROiP0A7B1.

Family and domain databases

Gene3Di3.30.1840.10. 1 hit.
HAMAPiMF_00347. Polyphosphate_kinase. 1 hit.
InterProiIPR001736. PLipase_D/transphosphatidylase.
IPR003414. PP_kinase.
IPR024953. PP_kinase_middle.
IPR025200. PPK_C_dom.
IPR025198. PPK_N_dom.
[Graphical view]
PfamiPF02503. PP_kinase. 1 hit.
PF13090. PP_kinase_C. 1 hit.
PF13089. PP_kinase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF015589. PP_kinase. 1 hit.
SUPFAMiSSF140356. SSF140356. 1 hit.
TIGRFAMsiTIGR03705. poly_P_kin. 1 hit.
PROSITEiPS50035. PLD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPK_ECOLI
AccessioniPrimary (citable) accession number: P0A7B1
Secondary accession number(s): P28688, Q47549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.