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Q9X913 (HPPA_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
K(+)-insensitive pyrophosphate-energized proton pump
EC=3.6.1.1
Alternative name(s):
Membrane-bound proton-translocating pyrophosphatase
Pyrophosphate-energized inorganic pyrophosphatase
Short name=H(+)-PPase
Gene names
Name:hppA
Ordered Locus Names:SCO3547
ORF Names:SCH5.10c
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. Ref.2

Catalytic activity

Diphosphate + H2O = 2 phosphate. Ref.2

Cofactor

Magnesium By similarity. HAMAP MF_01129

Subunit structure

Homodimer By similarity. HAMAP MF_01129

Subcellular location

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

Sequence similarities

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

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandMagnesium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproton transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrogen-translocating pyrophosphatase activity

Inferred from electronic annotation. Source: InterPro

inorganic diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 794794K(+)-insensitive pyrophosphate-energized proton pump HAMAP MF_01129
PRO_0000217032

Regions

Transmembrane20 – 4021Helical; Potential
Transmembrane74 – 9421Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane163 – 18321Helical; Potential
Transmembrane194 – 21421Helical; Potential
Transmembrane264 – 28421Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane321 – 34121Helical; Potential
Transmembrane365 – 38521Helical; Potential
Transmembrane422 – 44221Helical; Potential
Transmembrane446 – 46621Helical; Potential
Transmembrane508 – 52821Helical; Potential
Transmembrane564 – 58421Helical; Potential
Transmembrane641 – 66121Helical; Potential
Transmembrane717 – 73721Helical; Potential
Transmembrane747 – 76721Helical; Potential

Sites

Site5071Determinant of potassium independence By similarity

Experimental info

Mutagenesis3881F → Y: Increased PPase activity and H(+) pump activity. The coupling ratio is approximately two-fold that of the wild-type. Ref.2
Mutagenesis5141A → S: Increased PPase activity and H(+) pump activity. The coupling ratio is approximately two-fold that of the wild-type. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9X913 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 1525557A88198CA8

FASTA79480,650
        10         20         30         40         50         60 
MAELPTSHLA AAVLTDGNRA LVAVIAVVAL AALVLAGVLV RQVLAAGEGT DSMKKIAAAV 

        70         80         90        100        110        120 
QEGANAYLAR QLRTLGVFAV VVFFLLMLLP ADDWNQRAGR SIFFLIGAAF SAATGYIGMW 

       130        140        150        160        170        180 
LAVRSNVRVA AAAREATPAP GEPEKDLALV SHKATKIAFR TGGVVGMFTV GLGLLGACCV 

       190        200        210        220        230        240 
VLVYAADAPK VLEGFGLGAA LIAMFMRVGG GIFTKAADVG ADLVGKVEQG IPEDDPRNAA 

       250        260        270        280        290        300 
TIADNVGDNV GDCAGMAADL FESYAVTLVA ALILGKVAFG DFGLAFPLLV PAIGVLTAMI 

       310        320        330        340        350        360 
GIFAVAPRRS DRSGMSAINR GFFISAVISL VLVAVAVFVY LPGKYADLDG VTDAAIAGKS 

       370        380        390        400        410        420 
GDPRILALVA VAIGIVLAAL IQQLTGYFTE TTRRPVKDIG KSSLTGPATV VLAGISLGLE 

       430        440        450        460        470        480 
SAVYTALLIG LGVYGAFLLG GTSIMLALFA VALAGTGLLT TVGVIVAMDT FGPVSDNAQG 

       490        500        510        520        530        540 
IAEMSGDVEG AGAQVLTDLD AVGNTTKAIT KGIAIATAVL AAAALFGSYR DAITTGAADV 

       550        560        570        580        590        600 
GEKLSGEGAP MTLMMDISQP NNLVGLIAGA AVVFLFSGLA INAVSRSAGA VVYEVRRQFR 

       610        620        630        640        650        660 
ERPGIMDYSE KPEYGKVVDI CTRDALRELA TPGLLAVMAP IFIGFTLGVG ALGAFLAGAI 

       670        680        690        700        710        720 
GAGTLMAVFL ANSGGSWDNA KKLVEDGHHG GKGSEAHAAT VIGDTVGDPF KDTAGPAINP 

       730        740        750        760        770        780 
LLKVMNLVAL LIAPAVIKFS YGADKSVVVR VLIAVVAFAV IAAAVYVSKR RGIAMGDEDD 

       790 
ADPEPKSADP AVVS

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed: 12000953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Functional enhancement by single-residue substitution of Streptomyces coelicolor A3(2) H+-translocating pyrophosphatase."
Hirono M., Maeshima M.
J. Biochem. 146:617-621(2009) [PubMed: 19628678] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-388 AND ALA-514.
Strain: A3(2) / NRRL B-16638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL939117 Genomic DNA. Translation: CAB38484.1.
PIRT36668.
RefSeqNP_627745.1. NC_003888.3.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1098983.
GenomeReviewsGene locus SCO3547 in contig AL645882_GR.
KEGGsco:SCO3547.
NMPDRfig|100226.1.peg.3504.
PATRIC23736838. VBIStrCoe124346_3603.

Phylogenomic databases

HOGENOMHBG593668.
OMAAINRGFF.
PhylomeDBQ9X913.
ProtClustDBPRK00733.

Enzyme and pathway databases

BRENDA3.6.1.1. 5998.

Family and domain databases

HAMAPMF_01129. PPase-energized_pump.
[Tree]
InterProIPR004131. PPase-energised_H-pump.
[Graphical view]
KOK01507.
PfamPF03030. H_PPase. 1 hit.
[Graphical view]
PIRSFPIRSF001265. H+-PPase. 1 hit.
TIGRFAMsTIGR01104. V_PPase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHPPA_STRCO
AccessionPrimary (citable) accession number: Q9X913
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 61 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

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