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Q3AFC6 (HPPA_CARHZ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
K(+)-stimulated pyrophosphate-energized sodium pump

EC=3.6.1.1
Alternative name(s):
Membrane-bound sodium-translocating pyrophosphatase
Pyrophosphate-energized inorganic pyrophosphatase
Short name=Na(+)-PPase
Gene names
Name:hppA
Ordered Locus Names:CHY_0286
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na+ movement across the membrane By similarity. HAMAP-Rule MF_01129

Catalytic activity

Diphosphate + H2O = 2 phosphate. Ref.2

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01129

Enzyme regulation

Requires K+ for maximal activity. Ref.2

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01129

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01129.

Sequence similarities

Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-stimulated subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 686686K(+)-stimulated pyrophosphate-energized sodium pump HAMAP-Rule MF_01129
PRO_0000401066

Regions

Transmembrane6 – 2621Helical; Potential
Transmembrane58 – 7821Helical; Potential
Transmembrane89 – 10921Helical; Potential
Transmembrane139 – 15921Helical; Potential
Transmembrane165 – 18521Helical; Potential
Transmembrane231 – 25121Helical; Potential
Transmembrane264 – 28421Helical; Potential
Transmembrane294 – 31421Helical; Potential
Transmembrane327 – 34721Helical; Potential
Transmembrane386 – 40621Helical; Potential
Transmembrane408 – 42821Helical; Potential
Transmembrane459 – 47921Helical; Potential
Transmembrane509 – 52921Helical; Potential
Transmembrane577 – 59721Helical; Potential
Transmembrane599 – 61921Helical; Potential
Transmembrane666 – 68621Helical; Potential

Sites

Metal binding1911Magnesium 1 By similarity
Metal binding1951Magnesium 1 By similarity
Metal binding2181Magnesium 2 By similarity
Metal binding2211Magnesium 2 By similarity
Metal binding4301Magnesium 2 By similarity
Metal binding6261Calcium or magnesium By similarity
Metal binding6521Calcium or magnesium By similarity
Metal binding6561Calcium or magnesium By similarity
Binding site1881Substrate By similarity
Binding site6591Substrate By similarity
Site1801Important for ion transport By similarity
Site2251Important for ion transport By similarity
Site2321Important for ion transport By similarity
Site4601Important for potassium dependence
Site6601Important for ion transport By similarity
Site6711Important for ion transport By similarity

Experimental info

Mutagenesis4601A → K: Confers K(+) independence to both pyrophosphate hydrolysis and pyrophosphate-energized H(+) translocation. Ref.2
Mutagenesis4631A → T: Does not affect the K(+) dependence of H(+)-PPase. Decreased affinity for K(+). Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3AFC6 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 39AAC4A0A6ECBD70

FASTA68671,063
        10         20         30         40         50         60 
MENGMTLAYY GLGAGILAIL FALYLFSSVL KEDMGNEKMR EISQAIFEGA MAYLNRQYKT 

        70         80         90        100        110        120 
LIPFALVVFV LLVVGFGYKE GDFGYGLKVG VSFLVGAIAS ALAGYAGMTS TTKANARTTQ 

       130        140        150        160        170        180 
AARKSLNAAL NVAFRAGGVM GMSVAGLGLL GVSALYIIFK DVHVIDSFAF GASAIAFFAR 

       190        200        210        220        230        240 
VGGGIYTKAA DVGADLVGKV EAGIPEDDPR NPAVIADNVG DNVGDTAGMG ADLFESYGAT 

       250        260        270        280        290        300 
TMAAMLLGLT FAKNHGFSEV LGATFPLLLG AAGIVAAIIS TFFVRTSEDG NPQMALNIGL 

       310        320        330        340        350        360 
WSTNFITAIF TYIIAQYVFG SEWAPKIFIA VVSGLVVNVA IGSLTEYYTS NLKPPAQKIA 

       370        380        390        400        410        420 
EASTTGPATN IISGIAVGMR STYLPIIVIV AAIMVGYWAA GFYGIALAAM GMLATAAMVV 

       430        440        450        460        470        480 
AVDSFGPVAD NAGGIAEMAE LGPEIRNKTD KLDAVGNTTA AVAKGFAIGS AALTALALFS 

       490        500        510        520        530        540 
AYTDLAKTNP NLQKYLVNGK FDLNITDPWV LVGLFLGGTV AFLVAALTME SVGKAAFDMI 

       550        560        570        580        590        600 
EEVRRQFREI PGLMEGKARP DYARCVSIST AAAIRQMIAP GLLAVGAPLA IGFILGFKAL 

       610        620        630        640        650        660 
TGYLAGVTAT GVLLAIYMAN AGGAWDNAKK YIEAGNLGGK GSDTHKAAVV GDTVGDPFKD 

       670        680 
TSGPAMNPLM KVAGTFALII VPLLLF 

« Hide

References

« Hide 'large scale' references
[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z-2901 / DSM 6008.
[2]"A lysine substitute for K+. A460K mutation eliminates K+ dependence in H+-pyrophosphatase of Carboxydothermus hydrogenoformans."
Belogurov G.A., Lahti R.
J. Biol. Chem. 277:49651-49654(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF ALA-460 AND ALA-463, IDENTIFICATION OF SITE IMPORTANT FOR POTASSIUM DEPENDENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000141 Genomic DNA. Translation: ABB14908.1.
RefSeqYP_359158.1. NC_007503.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246194.CHY_0286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB14908; ABB14908; CHY_0286.
GeneID3726517.
KEGGchy:CHY_0286.
PATRIC21273745. VBICarHyd26463_0272.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3808.
HOGENOMHOG000007098.
KOK15987.
OMAHIAQAST.
OrthoDBEOG6TXQSF.
ProtClustDBPRK00733.

Enzyme and pathway databases

BioCycCHYD246194:GJCN-287-MONOMER.

Family and domain databases

HAMAPMF_01129. PPase_energized_pump.
InterProIPR004131. PPase-energised_H-pump.
[Graphical view]
PfamPF03030. H_PPase. 1 hit.
[Graphical view]
PIRSFPIRSF001265. H+-PPase. 1 hit.
TIGRFAMsTIGR01104. V_PPase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHPPA_CARHZ
AccessionPrimary (citable) accession number: Q3AFC6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families