Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00514

- GSPG_PSEAE

UniProt

Q00514 - GSPG_PSEAE

Protein

Type II secretion system protein G

Gene

xcpT

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of a variety of enzymes across the outer membrane.

    GO - Molecular functioni

    1. protein transporter activity Source: InterPro

    GO - Biological processi

    1. protein secretion by the type II secretion system Source: PseudoCAP

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type II secretion system protein G
    Short name:
    T2SS protein G
    Alternative name(s):
    General secretion pathway protein G
    PilD-dependent protein PddA
    Gene namesi
    Name:xcpT
    Synonyms:pddA
    Ordered Locus Names:PA3101
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA3101.

    Subcellular locationi

    GO - Cellular componenti

    1. type II protein secretion system complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 88By similarityPRO_0000024208
    Chaini9 – 142134Type II secretion system protein GPRO_0000024209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N-methylphenylalanineBy similarity

    Keywords - PTMi

    Methylation

    Interactioni

    Protein-protein interaction databases

    IntActiQ00514. 1 interaction.
    STRINGi208964.PA3101.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 6124
    Helixi70 – 767
    Turni91 – 933
    Beta strandi107 – 1093
    Beta strandi113 – 1164
    Beta strandi118 – 1214
    Beta strandi130 – 1356
    Beta strandi137 – 1393

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KEPNMR-A33-142[»]
    ProteinModelPortaliQ00514.
    SMRiQ00514. Positions 33-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00514.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GSP G family.Curated

    Phylogenomic databases

    eggNOGiCOG2165.
    HOGENOMiHOG000008196.
    KOiK02456.
    OMAiSADINSW.
    OrthoDBiEOG657JHX.

    Family and domain databases

    InterProiIPR000983. Bac_GSPG_pilin.
    IPR012902. N_methyl_site.
    IPR013545. T2SS_protein-G.
    IPR010054. Type2_sec_GspG.
    [Graphical view]
    PfamiPF13544. N_methyl_2. 1 hit.
    PF08334. T2SG. 1 hit.
    [Graphical view]
    PRINTSiPR00813. BCTERIALGSPG.
    TIGRFAMsiTIGR02532. IV_pilin_GFxxxE. 1 hit.
    TIGR01710. typeII_sec_gspG. 1 hit.
    PROSITEiPS00409. PROKAR_NTER_METHYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q00514-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRRQQSGFT LIEIMVVVVI LGILAALVVP QVMSRPDQAK VTVAKGDIKA    50
    IAAALDMYKL DNFAYPSTQQ GLEALVKKPT GNPQPKNWNK DGYLKKLPVD 100
    PWGNPYQYLA PGTKGPFDLY SLGADGKEGG SDNDADIGNW DN 142
    Length:142
    Mass (Da):15,449
    Last modified:December 1, 1992 - v1
    Checksum:iB498621CFC45B9B7
    GO

    Sequence cautioni

    The sequence AAG06489.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311S → T in AAA25946. (PubMed:1309616)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62666 Genomic DNA. Translation: CAA44535.1.
    M80792 Genomic DNA. Translation: AAA25946.1.
    AE004091 Genomic DNA. Translation: AAG06489.1. Different initiation.
    PIRiE83258.
    S25386. SKPSXT.
    RefSeqiNP_251791.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG06489; AAG06489; PA3101.
    GeneIDi878731.
    KEGGipae:PA3101.
    PATRICi19840775. VBIPseAer58763_3253.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62666 Genomic DNA. Translation: CAA44535.1 .
    M80792 Genomic DNA. Translation: AAA25946.1 .
    AE004091 Genomic DNA. Translation: AAG06489.1 . Different initiation.
    PIRi E83258.
    S25386. SKPSXT.
    RefSeqi NP_251791.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KEP NMR - A 33-142 [» ]
    ProteinModelPortali Q00514.
    SMRi Q00514. Positions 33-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q00514. 1 interaction.
    STRINGi 208964.PA3101.

    Protocols and materials databases

    DNASUi 878731.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG06489 ; AAG06489 ; PA3101 .
    GeneIDi 878731.
    KEGGi pae:PA3101.
    PATRICi 19840775. VBIPseAer58763_3253.

    Organism-specific databases

    PseudoCAPi PA3101.

    Phylogenomic databases

    eggNOGi COG2165.
    HOGENOMi HOG000008196.
    KOi K02456.
    OMAi SADINSW.
    OrthoDBi EOG657JHX.

    Miscellaneous databases

    EvolutionaryTracei Q00514.

    Family and domain databases

    InterProi IPR000983. Bac_GSPG_pilin.
    IPR012902. N_methyl_site.
    IPR013545. T2SS_protein-G.
    IPR010054. Type2_sec_GspG.
    [Graphical view ]
    Pfami PF13544. N_methyl_2. 1 hit.
    PF08334. T2SG. 1 hit.
    [Graphical view ]
    PRINTSi PR00813. BCTERIALGSPG.
    TIGRFAMsi TIGR02532. IV_pilin_GFxxxE. 1 hit.
    TIGR01710. typeII_sec_gspG. 1 hit.
    PROSITEi PS00409. PROKAR_NTER_METHYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase."
      Bally M., Filloux A., Akrim M., Ball G., Lazdunski A., Tommassen J.
      Mol. Microbiol. 6:1121-1131(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    2. "Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase."
      Nunn D.N., Lory S.
      Proc. Natl. Acad. Sci. U.S.A. 89:47-51(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiGSPG_PSEAE
    AccessioniPrimary (citable) accession number: Q00514
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3