Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q931U2 (PT1_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Gene names
Name:ptsI
Ordered Locus Names:SAV1084
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Domain

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147081

Sites

Active site1911Tele-phosphohistidine intermediate By similarity
Active site5041Proton donor By similarity
Metal binding4331Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site2981Substrate By similarity
Binding site3341Substrate By similarity
Binding site4331Substrate By similarity
Binding site4541Substrate; via carbonyl oxygen By similarity
Binding site4551Substrate; via amide nitrogen By similarity
Binding site4561Substrate By similarity
Binding site4571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q931U2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F2AAE2D47B7853C7

FASTA57263,206
        10         20         30         40         50         60 
MSKLIKGIAA SDGVAIAKAY LLVEPDLTFD KNEKVTDVEG EVAKFNSAIE ASKVELTKIR 

        70         80         90        100        110        120 
NNAEVQLGAD KAAIFDAHLL VLDDPELIQP IQDKIKNENA NAATALTDVT TQFVTIFESM 

       130        140        150        160        170        180 
DNEYMKERAA DIRDVSKRVL SHILGVELPN PSMIDESVVI VGNDLTPSDT AQLNKEFVQG 

       190        200        210        220        230        240 
FATNIGGRTS HSAIMSRSLE IPAIVGTKSI TQEVKQGDII IVDGLNGDVI VNPTEDELIA 

       250        260        270        280        290        300 
YQDKRECYFA DKKELQKLRD ADTVTVDGVH AELAANIGTP NDLPGVIENG AQGIGLYRTE 

       310        320        330        340        350        360 
FLYMGRDQMP TEEEQFEAYK EVLEAMDGKR VVVRTLDIGG DKELSYLNLP EEMNPFLGYR 

       370        380        390        400        410        420 
AIRLCLAQQD IFRPQLRALL RASVYGKLNI MFPMVATINE FREAKAILLE EKENLKNEGH 

       430        440        450        460        470        480 
DISDDIELGI MVEIPATAAL ADVFAKEVDF FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN 

       490        500        510        520        530        540 
PSILRLVKQV IEASHKEGKW TGMCGEMAGD ETAIPLLLGL GLDEFSMSAT SILKARRQIN 

       550        560        570 
GLSKNEMTEL ANRAVDCATQ EEVIELVNNY VK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB57246.1.
RefSeqNP_371608.1. NC_002758.2.

3D structure databases

ProteinModelPortalQ931U2.
SMRQ931U2. Positions 5-572.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ931U2.

2D gel databases

World-2DPAGE0002:Q931U2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000005580; EBSTAP00000005398; EBSTAG00000005579.
GeneID1121061.
GenomeReviewsGene locus SAV1084 in contig BA000017_GR.
KEGGsav:SAV1084.
PATRIC19562865. VBIStaAur52173_1111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1080.
GeneTreeEBGT00050000024576.
HOGENOMHBG456539.
OMAIFSAHLL.
PhylomeDBQ931U2.
ProtClustDBCLSK885128.

Enzyme and pathway databases

BioCycSAUR158878:SAV1084-MONOMER.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_STAAM
AccessionPrimary (citable) accession number: Q931U2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 64 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents