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P0AD67

- PBP2_ECO57

UniProt

P0AD67 - PBP2_ECO57

Protein

Penicillin-binding protein 2

Gene

mrdA

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. Its synthesize cross-linked peptidoglycan from the lipid intermediates By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei330 – 3301Acyl-ester intermediateBy similarity

    GO - Molecular functioni

    1. catalytic activity Source: UniProtKB-KW
    2. penicillin binding Source: InterPro

    GO - Biological processi

    1. peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
    2. regulation of cell shape Source: UniProtKB-KW
    3. response to antibiotic Source: UniProtKB-KW

    Keywords - Biological processi

    Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-668-MONOMER.
    ECOO157:MRDA-MONOMER.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Penicillin-binding protein 2
    Short name:
    PBP-2
    Gene namesi
    Name:mrdA
    Synonyms:pbpA
    Ordered Locus Names:Z0781, ECs0673
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Penicillin-binding protein 2PRO_0000195445Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi155864.Z0781.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AD67.
    SMRiP0AD67. Positions 56-614.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei22 – 4221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    Has a penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).By similarity

    Sequence similaritiesi

    Belongs to the transpeptidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0768.
    HOGENOMiHOG000266120.
    KOiK05515.
    OMAiNDGQVKT.
    OrthoDBiEOG6N0HHV.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR005311. PBP_dimer.
    IPR001460. PCN-bd_Tpept.
    IPR017790. Penicillin-binding_protein_2.
    [Graphical view]
    PfamiPF03717. PBP_dimer. 1 hit.
    PF00905. Transpeptidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56519. SSF56519. 1 hit.
    SSF56601. SSF56601. 1 hit.
    TIGRFAMsiTIGR03423. pbp2_mrdA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AD67-1 [UniParc]FASTAAdd to Basket

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    MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY    50
    QTRSNENRIK LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ 100
    TLDALRSVVD LTDDDIAAFR KERARSHRFT SIPVKTNLTE VQVARFAVNQ 150
    YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS KINDKDVERL NNDGKLANYA 200
    ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK EVPPQAGHDI 250
    YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG 300
    ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT 350
    TLFDPGWWQL PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG 400
    IDRLSEWMGK FGYGHYTGID LAEERSGNMP TREWKQKRFK KPWYQGDTIP 450
    VGIGQGYWTA TPIQMSKALM ILINDGIVKV PHLLMSTAED GKQVPWVQPH 500
    EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK IAAKSGTAQV 550
    FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV 600
    GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH 633
    Length:633
    Mass (Da):70,857
    Last modified:August 1, 1988 - v1
    Checksum:iFE2305C002743AF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG54969.1.
    BA000007 Genomic DNA. Translation: BAB34096.1.
    PIRiA90713.
    E85563.
    RefSeqiNP_286361.1. NC_002655.2.
    NP_308700.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG54969; AAG54969; Z0781.
    BAB34096; BAB34096; BAB34096.
    GeneIDi917034.
    957678.
    KEGGiece:Z0781.
    ecs:ECs0673.
    PATRICi18350336. VBIEscCol44059_0687.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG54969.1 .
    BA000007 Genomic DNA. Translation: BAB34096.1 .
    PIRi A90713.
    E85563.
    RefSeqi NP_286361.1. NC_002655.2.
    NP_308700.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0AD67.
    SMRi P0AD67. Positions 56-614.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z0781.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG54969 ; AAG54969 ; Z0781 .
    BAB34096 ; BAB34096 ; BAB34096 .
    GeneIDi 917034.
    957678.
    KEGGi ece:Z0781.
    ecs:ECs0673.
    PATRICi 18350336. VBIEscCol44059_0687.

    Phylogenomic databases

    eggNOGi COG0768.
    HOGENOMi HOG000266120.
    KOi K05515.
    OMAi NDGQVKT.
    OrthoDBi EOG6N0HHV.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci ECOL386585:GJFA-668-MONOMER.
    ECOO157:MRDA-MONOMER.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR012338. Beta-lactam/transpept-like.
    IPR005311. PBP_dimer.
    IPR001460. PCN-bd_Tpept.
    IPR017790. Penicillin-binding_protein_2.
    [Graphical view ]
    Pfami PF03717. PBP_dimer. 1 hit.
    PF00905. Transpeptidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56519. SSF56519. 1 hit.
    SSF56601. SSF56601. 1 hit.
    TIGRFAMsi TIGR03423. pbp2_mrdA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiPBP2_ECO57
    AccessioniPrimary (citable) accession number: P0AD67
    Secondary accession number(s): P08150
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 66 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

    Complete proteome, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3