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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 also act in the reverse direction to form ATP in the presence of excess ADP. Can also use GTP instead of ATP; but the efficiency of GTP is 5% that of ATP.UniRule annotation1 Publication

Catalytic activityi

ATP + (phosphate)(n) = ADP + (phosphate)(n+1).UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei435 – 4351Phosphohistidine intermediate
Active sitei454 – 4541Phosphohistidine intermediate

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • diphosphotransferase activity Source: EcoCyc
  • 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, 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 annotation)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11510. ppk.

Subcellular locationi

  • Cell inner membrane 1 Publication; Peripheral membrane protein 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 inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 688687Polyphosphate kinasePRO_0000128640Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0A7B1.
PRIDEiP0A7B1.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
yafCP308641EBI-544152,EBI-548591
yfbVP0A8D91EBI-544152,EBI-1128326

Protein-protein interaction databases

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

Structurei

Secondary structure

1
688
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2617Combined sources
Helixi32 – 5120Combined sources
Helixi53 – 6715Combined sources
Helixi73 – 10331Combined sources
Turni104 – 1063Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 1143Combined sources
Helixi119 – 13012Combined sources
Helixi132 – 1343Combined sources
Turni146 – 1494Combined sources
Beta strandi155 – 1639Combined sources
Beta strandi166 – 1738Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi195 – 1984Combined sources
Helixi199 – 21113Combined sources
Turni212 – 2143Combined sources
Beta strandi218 – 22912Combined sources
Turni235 – 2384Combined sources
Beta strandi241 – 2433Combined sources
Turni253 – 2553Combined sources
Beta strandi260 – 2645Combined sources
Helixi270 – 27910Combined sources
Beta strandi284 – 2907Combined sources
Helixi297 – 3026Combined sources
Helixi309 – 3113Combined sources
Helixi322 – 3254Combined sources
Helixi332 – 3387Combined sources
Beta strandi341 – 3455Combined sources
Helixi351 – 36212Combined sources
Beta strandi366 – 37510Combined sources
Helixi381 – 39111Combined sources
Beta strandi395 – 4006Combined sources
Turni407 – 4159Combined sources
Helixi416 – 4205Combined sources
Beta strandi424 – 4274Combined sources
Beta strandi437 – 4459Combined sources
Beta strandi448 – 45811Combined sources
Helixi464 – 4663Combined sources
Beta strandi468 – 4758Combined sources
Helixi478 – 49215Combined sources
Beta strandi504 – 5063Combined sources
Helixi510 – 52617Combined sources
Beta strandi533 – 5386Combined sources
Helixi543 – 55412Combined sources
Beta strandi559 – 5657Combined sources
Turni574 – 5763Combined sources
Beta strandi580 – 5856Combined sources
Beta strandi587 – 5915Combined sources
Beta strandi595 – 5984Combined sources
Helixi600 – 6023Combined sources
Beta strandi605 – 6106Combined sources
Helixi615 – 6195Combined sources
Beta strandi620 – 6278Combined sources
Helixi631 – 64515Combined sources
Beta strandi649 – 6535Combined sources
Helixi673 – 68412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XDOX-ray3.00A/B2-688[»]
1XDPX-ray2.50A/B2-688[»]
ProteinModelPortaliP0A7B1.
SMRiP0A7B1. Positions 2-688.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7B1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini430 – 46435PLD phosphodiesteraseUniRule annotationAdd
BLAST

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.
OrthoDBiEOG65TRRG.
PhylomeDBiP0A7B1.

Family and domain databases

Gene3Di3.30.1840.10. 1 hit.
HAMAPiMF_00347. Polyphosphate_kinase.
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 AAA83900.1 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1XDOX-ray3.00A/B2-688[»]
1XDPX-ray2.50A/B2-688[»]
ProteinModelPortaliP0A7B1.
SMRiP0A7B1. Positions 2-688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261066. 17 interactions.
DIPiDIP-36218N.
IntActiP0A7B1. 29 interactions.
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.
OrthoDBiEOG65TRRG.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The polyphosphate kinase gene of Escherichia coli. Isolation and sequence of the ppk gene and membrane location of the protein."
    Akiyama M., Crooke E., Kornberg A.
    J. Biol. Chem. 267:22556-22561(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12."
    Smith J.M., Daum H.A. III
    J. Biol. Chem. 262:10565-10569(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
    Strain: K12.
  6. "An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon."
    Akiyama M., Crooke E., Kornberg A.
    J. Biol. Chem. 268:633-639(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 679-688.
    Strain: K12.
  7. "Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli."
    Kumble K.D., Ahn K., Kornberg A.
    Proc. Natl. Acad. Sci. U.S.A. 93:14391-14395(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 434-437, FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, MUTAGENESIS OF HISTIDINE RESIDUES.

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: January 20, 2016
This is version 101 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.