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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Streptococcus equinus (Streptococcus bovis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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).

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911Tele-phosphohistidine intermediateBy similarity
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei334 – 3341SubstrateBy similarity
Metal bindingi435 – 4351MagnesiumBy similarity
Binding sitei435 – 4351SubstrateBy similarity
Binding sitei456 – 4561Substrate; via carbonyl oxygenBy similarity
Binding sitei457 – 4571Substrate; via amide nitrogenBy similarity
Binding sitei458 – 4581SubstrateBy similarity
Metal bindingi459 – 4591MagnesiumBy similarity
Binding sitei459 – 4591Substrate; via amide nitrogenBy similarity
Active sitei506 – 5061Proton donorBy similarity

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 phosphotransferase (EC:2.7.3.9)
Alternative name(s):
Phosphotransferase system, enzyme I
Gene namesi
Name:ptsI
OrganismiStreptococcus equinus (Streptococcus bovis)
Taxonomic identifieri1335 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Phosphoenolpyruvate-protein phosphotransferasePRO_0000147090Add
BLAST

Expressioni

Inductioni

Transcription of ptsI appears to be regulated in response to sugars supplied, i.e. is four-fold lower when cells were grown on lactose than when grown on glucose.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi525379.HMPREF0819_0152.

Structurei

3D structure databases

ProteinModelPortaliQ9WXK9.
SMRiQ9WXK9. Positions 5-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.

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.

Q9WXK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALKA
60 70 80 90 100
SQDELSIIRE KAVETLGEEA AAVFDAHLMV LADPEMISQI KETIRAKQTN
110 120 130 140 150
AEAGLKEVTD MFITIFEGME DNPYMQERAA DIRDVAKRVL AHLLGAKLPN
160 170 180 190 200
PATIDEESIV IAHDLTPSDT AQLNKQFVKA FVTNIGGRTS HSAIMARTLE
210 220 230 240 250
IAAVLGTNDI TSRVKDGDIV AVNGITGEVI INPTDEQVAE FKAAGEAYAK
260 270 280 290 300
QKAEWALLKD AKTVTADGKH FELAANIGTP KDVEGVNANG AEAVGLYRTE
310 320 330 340 350
FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYLDLP
360 370 380 390 400
KEMNPFLGFR ALRISISETG NAMFRTQIRA LLRASVHGQL RIMFPMVALL
410 420 430 440 450
KEFRAAKAIF DEEKANLKAE GVAVSDDIQV GIMIEIPAAA MLADQFAKEV
460 470 480 490 500
DFFSIGTNDL IQYTMAADRM NEQVSYLYQP YNPSILRLIN NVIKAAHAEG
510 520 530 540 550
KWVGMCGEMA GDQKAVPLLV EMGLDEFSMS ATSILRTRSL MKKLDTAKMQ
560 570
EYANRALTEC STMEEVLELS KEYVNVD
Length:577
Mass (Da):63,219
Last modified:November 1, 1999 - v1
Checksum:i989FF58D1B6DDD12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027569 Genomic DNA. Translation: BAA78049.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027569 Genomic DNA. Translation: BAA78049.1.

3D structure databases

ProteinModelPortaliQ9WXK9.
SMRiQ9WXK9. Positions 5-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi525379.HMPREF0819_0152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.

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...

Publicationsi

  1. "Molecular characterization of HPr and related enzymes, and regulation of HPr phosphorylation in the ruminal bacterium Streptococcus bovis."
    Asanuma N., Hino T.
    Arch. Microbiol. 179:205-213(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 700410 / JB1.

Entry informationi

Entry nameiPT1_STREI
AccessioniPrimary (citable) accession number: Q9WXK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1999
Last modified: January 20, 2016
This is version 82 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).By similarity

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.