Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Exopolyphosphatase

Gene

ppx

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

Functioni

Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues.3 Publications

Catalytic activityi

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.3 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activity is redox-regulated. Highly sensitive to inactivation by oxidation (PubMed:24560923). Strongly stimulated by potassium salts (PubMed:8380170).2 Publications

pH dependencei

Optimum pH is 8.1 Publication

GO - Molecular functioni

  • exopolyphosphatase activity Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • polyphosphate catabolic process Source: EcoCyc

Keywordsi

Molecular functionHydrolase
LigandMagnesium

Enzyme and pathway databases

BioCyciEcoCyc:PPX-MONOMER
MetaCyc:PPX-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Exopolyphosphatase1 Publication (EC:3.6.1.111 Publication)
Short name:
ExopolyPaseCurated
Alternative name(s):
Metaphosphatase
Gene namesi
Name:ppx1 Publication
Ordered Locus Names:b2502, JW2487
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11403 ppx

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Deletion mutant accumulates polyP.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121E → A: Almost loss of activity. 1 Publication1
Mutagenesisi143D → A: Almost loss of activity. 1 Publication1
Mutagenesisi150E → A: Almost loss of activity. 1 Publication1
Mutagenesisi371E → A: Decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001942992 – 513ExopolyphosphataseAdd BLAST512

Proteomic databases

PaxDbiP0AFL6
PRIDEiP0AFL6

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-551996,EBI-551996

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260594, 11 interactors
DIPiDIP-29140N
IntActiP0AFL6, 9 interactors
STRINGi316385.ECDH10B_2668

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 18Combined sources6
Beta strandi23 – 31Combined sources9
Beta strandi34 – 43Combined sources10
Helixi48 – 50Combined sources3
Helixi59 – 75Combined sources17
Turni76 – 78Combined sources3
Helixi81 – 83Combined sources3
Beta strandi84 – 88Combined sources5
Helixi90 – 94Combined sources5
Helixi98 – 105Combined sources8
Turni106 – 108Combined sources3
Beta strandi113 – 115Combined sources3
Helixi118 – 132Combined sources15
Beta strandi139 – 144Combined sources6
Beta strandi149 – 155Combined sources7
Beta strandi158 – 166Combined sources9
Helixi169 – 176Combined sources8
Helixi178 – 180Combined sources3
Helixi184 – 198Combined sources15
Turni199 – 201Combined sources3
Helixi202 – 208Combined sources7
Beta strandi211 – 217Combined sources7
Helixi218 – 229Combined sources12
Beta strandi233 – 235Combined sources3
Helixi239 – 249Combined sources11
Helixi255 – 257Combined sources3
Helixi267 – 269Combined sources3
Helixi271 – 285Combined sources15
Beta strandi290 – 292Combined sources3
Helixi297 – 309Combined sources13
Helixi314 – 325Combined sources12
Helixi330 – 350Combined sources21
Helixi352 – 354Combined sources3
Helixi357 – 369Combined sources13
Turni370 – 376Combined sources7
Helixi381 – 391Combined sources11
Helixi399 – 410Combined sources12
Beta strandi412 – 414Combined sources3
Helixi429 – 444Combined sources16
Turni445 – 448Combined sources4
Helixi449 – 451Combined sources3
Beta strandi459 – 463Combined sources5
Beta strandi466 – 471Combined sources6
Helixi475 – 478Combined sources4
Helixi480 – 493Combined sources14
Beta strandi500 – 505Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U6ZX-ray1.90A/B1-513[»]
ProteinModelPortaliP0AFL6
SMRiP0AFL6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFL6

Family & Domainsi

Sequence similaritiesi

Belongs to the GppA/Ppx family.Curated

Phylogenomic databases

eggNOGiENOG4105C9X Bacteria
COG0248 LUCA
HOGENOMiHOG000258672
InParanoidiP0AFL6
KOiK01524
OMAiRISEGCY
PhylomeDBiP0AFL6

Family and domain databases

InterProiView protein in InterPro
IPR022371 Exopolyphosphatase
IPR003695 Ppx_GppA
IPR030673 PyroPPase_GppA_Ppx
PfamiView protein in Pfam
PF02541 Ppx-GppA, 1 hit
PIRSFiPIRSF001267 Pyrophosphatase_GppA_Ppx, 1 hit
TIGRFAMsiTIGR03706 exo_poly_only, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0AFL6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIHDKSPRP QEFAAVDLGS NSFHMVIARV VDGAMQIIGR LKQRVHLADG
60 70 80 90 100
LGPDNMLSEE AMTRGLNCLS LFAERLQGFS PASVCIVGTH TLRQALNATD
110 120 130 140 150
FLKRAEKVIP YPIEIISGNE EARLIFMGVE HTQPEKGRKL VIDIGGGSTE
160 170 180 190 200
LVIGENFEPI LVESRRMGCV SFAQLYFPGG VINKENFQRA RMAAAQKLET
210 220 230 240 250
LTWQFRIQGW NVAMGASGTI KAAHEVLMEM GEKDGIITPE RLEKLVKEVL
260 270 280 290 300
RHRNFASLSL PGLSEERKTV FVPGLAILCG VFDALAIREL RLSDGALREG
310 320 330 340 350
VLYEMEGRFR HQDVRSRTAS SLANQYHIDS EQARRVLDTT MQMYEQWREQ
360 370 380 390 400
QPKLAHPQLE ALLRWAAMLH EVGLNINHSG LHRHSAYILQ NSDLPGFNQE
410 420 430 440 450
QQLMMATLVR YHRKAIKLDD LPRFTLFKKK QFLPLIQLLR LGVLLNNQRQ
460 470 480 490 500
ATTTPPTLTL ITDDSHWTLR FPHDWFSQNA LVLLDLEKEQ EYWEGVAGWR
510
LKIEEESTPE IAA
Length:513
Mass (Da):58,136
Last modified:January 23, 2007 - v2
Checksum:i58E58E0F5D9FB9C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06129 Genomic DNA Translation: AAA24415.1
U00096 Genomic DNA Translation: AAC75555.1
AP009048 Genomic DNA Translation: BAA16390.1
PIRiA45333
RefSeqiNP_416997.1, NC_000913.3
WP_001121363.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75555; AAC75555; b2502
BAA16390; BAA16390; BAA16390
GeneIDi946970
KEGGiecj:JW2487
eco:b2502
PATRICifig|1411691.4.peg.4236

Similar proteinsi

Entry informationi

Entry nameiPPX_ECOLI
AccessioniPrimary (citable) accession number: P0AFL6
Secondary accession number(s): P29014, P76981
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 92 of the entry and version 2 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health