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Q8ZQ06

- NAGZ_SALTY

UniProt

Q8ZQ06 - NAGZ_SALTY

Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.2 PublicationsUniRule annotation

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.2 PublicationsUniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621Substrate
    Binding sitei70 – 701SubstrateUniRule annotation
    Binding sitei133 – 1331Substrate
    Sitei174 – 1741Important for catalytic activityUniRule annotation
    Active sitei176 – 1761Proton donor/acceptor1 Publication
    Active sitei248 – 2481Nucleophile1 PublicationUniRule annotation

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. peptidoglycan biosynthetic process Source: UniProtKB-KW
    5. peptidoglycan turnover Source: UniProtKB-HAMAP
    6. regulation of cell shape Source: UniProtKB-KW
    7. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-1218-MONOMER.
    UniPathwayiUPA00544.

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidaseUniRule annotation (EC:3.2.1.52UniRule annotation)
    Alternative name(s):
    Beta-N-acetylhexosaminidaseUniRule annotation
    N-acetyl-beta-glucosaminidaseUniRule annotation
    Gene namesi
    Name:nagZUniRule annotation
    Ordered Locus Names:STM1209
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761H → G: Reduced enzyme activity.
    Mutagenesisi248 – 2481D → N: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341Beta-hexosaminidasePRO_0000210797Add
    BLAST

    Proteomic databases

    PaxDbiQ8ZQ06.
    PRIDEiQ8ZQ06.

    Interactioni

    Protein-protein interaction databases

    STRINGi99287.STM1209.

    Structurei

    Secondary structure

    1
    341
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi9 – 124
    Helixi15 – 217
    Beta strandi26 – 316
    Helixi33 – 353
    Helixi39 – 5214
    Beta strandi58 – 614
    Beta strandi63 – 653
    Beta strandi68 – 703
    Helixi83 – 10927
    Turni110 – 1123
    Turni128 – 1303
    Helixi131 – 1333
    Helixi139 – 15618
    Beta strandi161 – 1655
    Beta strandi175 – 1784
    Helixi186 – 1916
    Helixi193 – 20210
    Beta strandi207 – 2115
    Turni217 – 2193
    Helixi224 – 2263
    Helixi228 – 2314
    Helixi232 – 2387
    Beta strandi243 – 2497
    Helixi250 – 2523
    Helixi256 – 2583
    Helixi261 – 27111
    Beta strandi274 – 2785
    Helixi282 – 29110
    Helixi298 – 3036
    Helixi311 – 3166
    Helixi318 – 33922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GVFX-ray1.35A/B1-341[»]
    4GVGX-ray1.70A/B1-341[»]
    4GVHX-ray1.45A/B1-341[»]
    4GVIX-ray1.55A/B1-341[»]
    4HZMX-ray1.45A/B1-341[»]
    ProteinModelPortaliQ8ZQ06.
    SMRiQ8ZQ06. Positions 1-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni163 – 1642Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000248526.
    KOiK01207.
    OMAiYTEADPR.
    OrthoDBiEOG6BCT06.
    PhylomeDBiQ8ZQ06.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    HAMAPiMF_00364. NagZ.
    InterProiIPR022956. Beta_hexosaminidase_bac.
    IPR019800. Glyco_hydro_3_AS.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00933. Glyco_hydro_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8ZQ06-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPVMLNVEG CELDAEEREI LAHPLVGGLI LFTRNYHDPE QLRELVRQIR    50
    AASRNHLVVA VDQEGGRVQR FREGFTRLPA AQSFFALHGL EEGGRLAQEA 100
    GWLMASEMIA MDIDISFAPV LDVGHISAAI GERSYHADPA KALAMATRFI 150
    DGMHDAGMKT TGKHFPGHGA VTADSHKETP CDPRPETDIR GKDMSVFRTL 200
    ISENKLDAIM PAHVIYRAID PRPASGSPYW LKTVLRQELG FDGVIFSDDL 250
    SMEGAAIMGS YAERAQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV 300
    TRLYHKGSFS RRELMDSARW KTASAQLNQL HERWQEEKAG H 341
    Length:341
    Mass (Da):37,698
    Last modified:March 1, 2002 - v1
    Checksum:iE07E83487336A300
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL20138.1.
    RefSeqiNP_460179.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20138; AAL20138; STM1209.
    GeneIDi1252727.
    KEGGistm:STM1209.
    PATRICi32380867. VBISalEnt20916_1278.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL20138.1 .
    RefSeqi NP_460179.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GVF X-ray 1.35 A/B 1-341 [» ]
    4GVG X-ray 1.70 A/B 1-341 [» ]
    4GVH X-ray 1.45 A/B 1-341 [» ]
    4GVI X-ray 1.55 A/B 1-341 [» ]
    4HZM X-ray 1.45 A/B 1-341 [» ]
    ProteinModelPortali Q8ZQ06.
    SMRi Q8ZQ06. Positions 1-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM1209.

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Proteomic databases

    PaxDbi Q8ZQ06.
    PRIDEi Q8ZQ06.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20138 ; AAL20138 ; STM1209 .
    GeneIDi 1252727.
    KEGGi stm:STM1209.
    PATRICi 32380867. VBISalEnt20916_1278.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000248526.
    KOi K01207.
    OMAi YTEADPR.
    OrthoDBi EOG6BCT06.
    PhylomeDBi Q8ZQ06.

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    BioCyci SENT99287:GCTI-1218-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    HAMAPi MF_00364. NagZ.
    InterProi IPR022956. Beta_hexosaminidase_bac.
    IPR019800. Glyco_hydro_3_AS.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00933. Glyco_hydro_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion."
      Bacik J.P., Whitworth G.E., Stubbs K.A., Vocadlo D.J., Mark B.L.
      Chem. Biol. 19:1471-1482(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH DISACCHARIDE SUBSTRATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF ASP-248.
    3. "The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams."
      Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E., Gloster T.M., Vocadlo D.J., Mark B.L.
      ChemBioChem 14:1973-1981(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiNAGZ_SALTY
    AccessioniPrimary (citable) accession number: Q8ZQ06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 81 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3