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Protein

Ascorbate-specific PTS system EIIC component

Gene

ulaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.1 Publication1 Publication

Kineticsi

  1. KM=18 µM for L-ascorbate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei314Ascorbate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    • L-ascorbic acid transport Source: EcoCyc
    • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
    Complete GO annotation...

    Keywords - Biological processi

    Phosphotransferase system, Sugar transport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:SGAT-MONOMER.
    ECOL316407:JW5744-MONOMER.
    MetaCyc:SGAT-MONOMER.

    Protein family/group databases

    TCDBi4.A.7.1.1. the pts l-ascorbate (l-asc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ascorbate-specific PTS system EIIC component1 Publication
    Alternative name(s):
    Ascorbate-specific permease IIC component UlaA1 Publication
    Gene namesi
    Name:ulaA1 Publication
    Synonyms:sgaT, yjfS
    Ordered Locus Names:b4193, JW5744
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12493. ulaA.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transmembranei14 – 34Helical1 PublicationAdd BLAST21
    Transmembranei38 – 58Helical1 PublicationAdd BLAST21
    Transmembranei101 – 121Helical1 PublicationAdd BLAST21
    Transmembranei141 – 161Helical1 PublicationAdd BLAST21
    Transmembranei233 – 253Helical1 PublicationAdd BLAST21
    Transmembranei263 – 283Helical1 PublicationAdd BLAST21
    Transmembranei316 – 336Helical1 PublicationAdd BLAST21
    Transmembranei338 – 358Helical1 PublicationAdd BLAST21
    Transmembranei379 – 399Helical1 PublicationAdd BLAST21
    Transmembranei427 – 447Helical1 PublicationAdd BLAST21

    GO - Cellular componenti

    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: EcoCyc
    • plasma membrane Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to use L-ascorbate.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000977141 – 465Ascorbate-specific PTS system EIIC componentAdd BLAST465

    Proteomic databases

    PaxDbiP39301.
    PRIDEiP39301.

    Expressioni

    Inductioni

    Induced by L-ascorbate. Repressed by UlaR.3 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4262713. 6 interactors.
    DIPiDIP-10870N.
    IntActiP39301. 1 interactor.
    MINTiMINT-1255643.
    STRINGi511145.b4193.

    Structurei

    Secondary structure

    1465
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni8 – 10Combined sources3
    Helixi11 – 14Combined sources4
    Turni15 – 17Combined sources3
    Helixi19 – 33Combined sources15
    Helixi38 – 76Combined sources39
    Beta strandi81 – 84Combined sources4
    Helixi86 – 97Combined sources12
    Helixi98 – 101Combined sources4
    Helixi102 – 120Combined sources19
    Helixi122 – 125Combined sources4
    Beta strandi129 – 131Combined sources3
    Helixi134 – 150Combined sources17
    Helixi155 – 185Combined sources31
    Helixi197 – 206Combined sources10
    Helixi207 – 209Combined sources3
    Helixi213 – 215Combined sources3
    Turni217 – 219Combined sources3
    Helixi224 – 230Combined sources7
    Helixi232 – 249Combined sources18
    Helixi253 – 260Combined sources8
    Helixi265 – 304Combined sources40
    Beta strandi310 – 313Combined sources4
    Helixi315 – 321Combined sources7
    Helixi323 – 346Combined sources24
    Beta strandi353 – 355Combined sources3
    Helixi357 – 402Combined sources46
    Beta strandi405 – 407Combined sources3
    Helixi412 – 415Combined sources4
    Helixi417 – 427Combined sources11
    Helixi428 – 430Combined sources3
    Helixi431 – 455Combined sources25

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4RP8X-ray2.36A/C1-465[»]
    4RP9X-ray1.65A1-465[»]
    ProteinModelPortaliP39301.
    SMRiP39301.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni86 – 87Ascorbate binding1 Publication2
    Regioni135 – 139Ascorbate binding1 Publication5
    Regioni194 – 195Ascorbate binding1 Publication2

    Domaini

    In classical PTS systems, the PTS EIIC type-2 domain forms the translocation channel and contains the specific substrate-binding site. UlaA does not exhibit the topological features of any recognized enzyme IIC.Curated

    Sequence similaritiesi

    Belongs to the UlaA family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG4105CZC. Bacteria.
    COG3037. LUCA.
    HOGENOMiHOG000218566.
    InParanoidiP39301.
    KOiK03475.
    OMAiPNSFGDE.
    PhylomeDBiP39301.

    Family and domain databases

    InterProiIPR004703. PTS_sugar-sp_permease.
    [Graphical view]
    PfamiPF03611. EIIC-GAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39301-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEILYNIFTV FFNQVMTNAP LLLGIVTCLG YILLRKSVSV IIKGTIKTII
    60 70 80 90 100
    GFMLLQAGSG ILTSTFKPVV AKMSEVYGIN GAISDTYASM MATIDRMGDA
    110 120 130 140 150
    YSWVGYAVLL ALALNICYVL LRRITGIRTI MLTGHIMFQQ AGLIAVTLFI
    160 170 180 190 200
    FGYSMWTTII CTAILVSLYW GITSNMMYKP TQEVTDGCGF SIGHQQQFAS
    210 220 230 240 250
    WIAYKVAPFL GKKEESVEDL KLPGWLNIFH DNIVSTAIVM TIFFGAILLS
    260 270 280 290 300
    FGIDTVQAMA GKVHWTVYIL QTGFSFAVAI FIITQGVRMF VAELSEAFNG
    310 320 330 340 350
    ISQRLIPGAV LAIDCAAIYS FAPNAVVWGF MWGTIGQLIA VGILVACGSS
    360 370 380 390 400
    ILIIPGFIPM FFSNATIGVF ANHFGGWRAA LKICLVMGMI EIFGCVWAVK
    410 420 430 440 450
    LTGMSAWMGM ADWSILAPPM MQGFFSIGIA FMAVIIVIAL AYMFFAGRAL
    460
    RAEEDAEKQL AEQSA
    Length:465
    Mass (Da):50,737
    Last modified:April 4, 2006 - v3
    Checksum:iCCFF1C776FEA4716
    GO

    Sequence cautioni

    The sequence AAA97089 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti451 – 465RAEED…AEQSA → AQKKMQKNNWQNSLLNKEF in AAA97089 (PubMed:7610040).CuratedAdd BLAST15

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U14003 Genomic DNA. Translation: AAA97089.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77150.2.
    AP009048 Genomic DNA. Translation: BAE78194.1.
    PIRiD65230.
    RefSeqiNP_418614.4. NC_000913.3.
    WP_001350568.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77150; AAC77150; b4193.
    BAE78194; BAE78194; BAE78194.
    GeneIDi948717.
    KEGGiecj:JW5744.
    eco:b4193.
    PATRICi32123961. VBIEscCol129921_4325.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U14003 Genomic DNA. Translation: AAA97089.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77150.2.
    AP009048 Genomic DNA. Translation: BAE78194.1.
    PIRiD65230.
    RefSeqiNP_418614.4. NC_000913.3.
    WP_001350568.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4RP8X-ray2.36A/C1-465[»]
    4RP9X-ray1.65A1-465[»]
    ProteinModelPortaliP39301.
    SMRiP39301.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262713. 6 interactors.
    DIPiDIP-10870N.
    IntActiP39301. 1 interactor.
    MINTiMINT-1255643.
    STRINGi511145.b4193.

    Protein family/group databases

    TCDBi4.A.7.1.1. the pts l-ascorbate (l-asc) family.

    Proteomic databases

    PaxDbiP39301.
    PRIDEiP39301.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77150; AAC77150; b4193.
    BAE78194; BAE78194; BAE78194.
    GeneIDi948717.
    KEGGiecj:JW5744.
    eco:b4193.
    PATRICi32123961. VBIEscCol129921_4325.

    Organism-specific databases

    EchoBASEiEB2386.
    EcoGeneiEG12493. ulaA.

    Phylogenomic databases

    eggNOGiENOG4105CZC. Bacteria.
    COG3037. LUCA.
    HOGENOMiHOG000218566.
    InParanoidiP39301.
    KOiK03475.
    OMAiPNSFGDE.
    PhylomeDBiP39301.

    Enzyme and pathway databases

    BioCyciEcoCyc:SGAT-MONOMER.
    ECOL316407:JW5744-MONOMER.
    MetaCyc:SGAT-MONOMER.

    Miscellaneous databases

    PROiP39301.

    Family and domain databases

    InterProiIPR004703. PTS_sugar-sp_permease.
    [Graphical view]
    PfamiPF03611. EIIC-GAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiULAA_ECOLI
    AccessioniPrimary (citable) accession number: P39301
    Secondary accession number(s): Q2M6B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: April 4, 2006
    Last modified: November 2, 2016
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.