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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei191Tele-phosphohistidine intermediateBy similarity1
Binding sitei298PEPBy similarity1
Binding sitei334PEPBy similarity1
Metal bindingi433MagnesiumBy similarity1
Metal bindingi457MagnesiumBy similarity1
Binding sitei467PEPBy similarity1
Active sitei504Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-protein phosphotransferaseBy similarity (EC:2.7.3.9By similarity)
Alternative name(s):
Phosphotransferase system, enzyme IBy similarity
Gene namesi
Name:ptsI
Ordered Locus Names:SA0935
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001470821 – 572Phosphoenolpyruvate-protein phosphotransferaseAdd BLAST572

Proteomic databases

PRIDEiQ99V14.

2D gel databases

SWISS-2DPAGEQ99V14.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ99V14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni456 – 457PEP bindingBy similarity2

Domaini

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

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

HOGENOMiHOG000278513.
KOiK08483.
OMAiDYVLGFA.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99V14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLIKGIAA SDGVAIAKAY LLVEPDLTFD KNEKVTDVEG EVAKFNSAIE
60 70 80 90 100
ASKVELTKIR NNAEVQLGAD KAAIFDAHLL VLDDPELIQP IQDKIKNENA
110 120 130 140 150
NAATALTDVT TQFVTIFESM DNEYMKERAA DIRDVSKRVL SHILGVELPN
160 170 180 190 200
PSMIDESVVI VGNDLTPSDT AQLNKEFVQG FATNIGGRTS HSAIMSRSLE
210 220 230 240 250
IPAIVGTKSI TQEVKQGDMI IVDGLNGDVI VNPTEDELIA YQDKRECYFA
260 270 280 290 300
DKKELQKLRD ADTVTVDGVH AELAANIGTP NDLPGVIENG AQGIGLYRTE
310 320 330 340 350
FLYMGRDQMP TEEEQFEAYK EVLEAMDGKR VVVRTLDIGG DKELSYLNLP
360 370 380 390 400
EEMNPFLGYR AIRLCLAQQD IFRPQLRALL RASVYGKLNI MFPMVATINE
410 420 430 440 450
FREAKAILLE EKENLKNEGH DISDDIELGI MVEIPATAAL ADVFAKEVDF
460 470 480 490 500
FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN PSILRLVKQV IEASHKEGKW
510 520 530 540 550
TGMCGEMAGD ETAIPLLLGL GLDEFSMSAT SILKARRQIN GLSKNEMTEL
560 570
ANRAVDCATQ EEVIELVNNY VK
Length:572
Mass (Da):63,224
Last modified:June 1, 2001 - v1
Checksum:i88D6B3F829BCC926
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42181.1.
PIRiB89878.
RefSeqiWP_000040051.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42181; BAB42181; BAB42181.
KEGGisau:SA0935.
PATRICi19574058. VBIStaAur116463_0999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42181.1.
PIRiB89878.
RefSeqiWP_000040051.1. NC_002745.2.

3D structure databases

ProteinModelPortaliQ99V14.
ModBaseiSearch...
MobiDBiSearch...

2D gel databases

SWISS-2DPAGEQ99V14.

Proteomic databases

PRIDEiQ99V14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42181; BAB42181; BAB42181.
KEGGisau:SA0935.
PATRICi19574058. VBIStaAur116463_0999.

Phylogenomic databases

HOGENOMiHOG000278513.
KOiK08483.
OMAiDYVLGFA.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPT1_STAAN
AccessioniPrimary (citable) accession number: Q99V14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome

Documents

  1. 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.