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P75168

- PT1_MYCPN

UniProt

P75168 - PT1_MYCPN

Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei190 – 1901Tele-phosphohistidine intermediateBy similarity
    Binding sitei297 – 2971SubstrateBy similarity
    Binding sitei333 – 3331SubstrateBy similarity
    Metal bindingi427 – 4271MagnesiumBy similarity
    Binding sitei427 – 4271SubstrateBy similarity
    Binding sitei448 – 4481Substrate; via carbonyl oxygenBy similarity
    Binding sitei449 – 4491Substrate; via amide nitrogenBy similarity
    Binding sitei450 – 4501SubstrateBy similarity
    Metal bindingi451 – 4511MagnesiumBy similarity
    Binding sitei451 – 4511Substrate; via amide nitrogenBy similarity
    Active sitei498 – 4981Proton donorBy similarity

    GO - Molecular functioni

    1. kinase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. phosphoenolpyruvate-protein phosphotransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Phosphotransferase system, Sugar transport, Transport

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMPNE272634:GJ6Z-673-MONOMER.

    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
    Ordered Locus Names:MPN_627
    ORF Names:MP215
    OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
    Taxonomic identifieri272634 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    ProteomesiUP000000808: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 572572Phosphoenolpyruvate-protein phosphotransferasePRO_0000147077Add
    BLAST

    Proteomic databases

    PaxDbiP75168.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP75168. 1 interaction.
    STRINGi272634.MPN627.

    Structurei

    3D structure databases

    ProteinModelPortaliP75168.
    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

    eggNOGiCOG1080.
    KOiK08483.
    OMAiWQISSIV.
    OrthoDBiEOG657JBQ.

    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.
    IPR006318. PEP_util_enz.
    IPR024692. PTS_EI.
    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.
    PRINTSiPR01736. PHPHTRNFRASE.
    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.

    P75168-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLSGIGVS DGMALAKAFL VKTPEFAVNK YLKHQLTKAQ AKRLLDSAFK    50
    KAVKDLEEIK EITVNNINTE AGMIFDAHIQ MLNDPTITEQ LEQQLAQNVH 100
    PVIAVDTVFS QTATMFSQMQ DKYFQERAAD ILDLRQRLLA YLTGQKPHDL 150
    VKIKSDVIIV AHDLTPSQTA TLNKKYVKGF LTEIGGRTSH AAIMARSLEI 200
    PAVVGIKGIT TKVKDGQIVG VDGRKGIAGL DLNSKDTTEW KKQKALEEKY 250
    QQELKQYTNK ETVTLDGHAV VVAANIGNVK DMELACQYNT NGVGLFRTEF 300
    LYMNSQEWPD EETQYQAYKA VLEQAHGDLV IIRTLDIGGD KKLNYYEFPH 350
    EDNPFLGYRA LRLTLDKQDI FKTQLRALLR AADHGQLGIM FPMVATLDEL 400
    LQAKQLLNQV HQELGGNKQF KLGIMIEIPA AVLAANTLSH HVDFFSIGTN 450
    DLIQYSFAAD RMNKNVSYLY QPLNPALLKL IYLTIEGGKV NDIWTGMCGE 500
    MAGEPLAIPL LLGLGLKEFS MSASSMFKAR MIIAKLNYTE CQTLAQKALT 550
    LANAKEVEKL VEKFFKKKDI FI 572
    Length:572
    Mass (Da):63,950
    Last modified:February 1, 1997 - v1
    Checksum:i5B12EF54B0CB80CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB95863.1.
    PIRiS73541.
    RefSeqiNP_110316.1. NC_000912.1.

    Genome annotation databases

    EnsemblBacteriaiAAB95863; AAB95863; MPN_627.
    GeneIDi876731.
    KEGGimpn:MPN627.
    PATRICi20022737. VBIMycPne110_0691.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB95863.1 .
    PIRi S73541.
    RefSeqi NP_110316.1. NC_000912.1.

    3D structure databases

    ProteinModelPortali P75168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P75168. 1 interaction.
    STRINGi 272634.MPN627.

    Proteomic databases

    PaxDbi P75168.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB95863 ; AAB95863 ; MPN_627 .
    GeneIDi 876731.
    KEGGi mpn:MPN627.
    PATRICi 20022737. VBIMycPne110_0691.

    Phylogenomic databases

    eggNOGi COG1080.
    KOi K08483.
    OMAi WQISSIV.
    OrthoDBi EOG657JBQ.

    Enzyme and pathway databases

    BioCyci MPNE272634:GJ6Z-673-MONOMER.

    Family and domain databases

    Gene3Di 1.10.274.10. 1 hit.
    3.20.20.60. 1 hit.
    3.50.30.10. 1 hit.
    InterProi IPR008279. PEP-util_enz_mobile_dom.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR006318. PEP_util_enz.
    IPR024692. PTS_EI.
    IPR008731. PTS_EIN.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    Pfami PF05524. PEP-utilisers_N. 1 hit.
    PF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000732. PTS_enzyme_I. 1 hit.
    PRINTSi PR01736. PHPHTRNFRASE.
    SUPFAMi SSF47831. SSF47831. 1 hit.
    SSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsi TIGR01417. PTS_I_fam. 1 hit.
    PROSITEi PS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
      Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
      Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29342 / M129.

    Entry informationi

    Entry nameiPT1_MYCPN
    AccessioniPrimary (citable) accession number: P75168
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 95 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Mycoplasma pneumoniae
      Mycoplasma pneumoniae (strain M129): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3