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P39848

- LYTD_BACSU

UniProt

P39848 - LYTD_BACSU

Protein

Beta-N-acetylglucosaminidase

Gene

lytD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Cell wall hydrolase not involved in cell autolysis, competence, sporulation or germination. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain.2 Publications

    Catalytic activityi

    Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

    Enzyme regulationi

    Inhibited by diethyl pyrocarbonate, slightly by EDTA. Not inhibited by PMSF, diisopropyl fluorophosphate, 2-mercaptoethanol or N-ethylmaleimide.1 Publication

    GO - Molecular functioni

    1. amidase activity Source: InterPro
    2. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell wall macromolecule metabolic process Source: InterPro
    2. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU35780-MONOMER.

    Protein family/group databases

    CAZyiGH73. Glycoside Hydrolase Family 73.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-N-acetylglucosaminidase (EC:3.2.1.96)
    Alternative name(s):
    Cell wall-associated polypeptide 90
    Short name:
    CWBP90
    Gene namesi
    Name:lytD
    Synonyms:cwlG
    Ordered Locus Names:BSU35780
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU35780. [Micado]

    Subcellular locationi

    Secreted 1 Publication. Secretedcell wall 1 Publication

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show no motility changes on swarm plates; however in combination with an amidase deletion (lytC, AC Q02114) greatly reduced motility is seen.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 880853Beta-N-acetylglucosaminidasePRO_0000012118Add
    BLAST

    Proteomic databases

    PaxDbiP39848.

    Expressioni

    Inductioni

    In stationary phase (PubMed:11987133); under control of SigD (PubMed:7581999).2 Publications

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi224308.BSU35780.

    Structurei

    3D structure databases

    ProteinModelPortaliP39848.
    SMRiP39848. Positions 632-682, 735-861.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini70 – 14980SPOR 1Add
    BLAST
    Domaini150 – 22980SPOR 2Add
    BLAST
    Domaini230 – 31182SPOR 3Add
    BLAST
    Repeati439 – 473351Add
    BLAST
    Repeati479 – 513352Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi72 – 754Poly-Thr
    Compositional biasi337 – 3404Poly-Lys
    Compositional biasi568 – 5714Poly-Ala

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 73 family.Curated
    Contains 3 SPOR domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4193.
    HOGENOMiHOG000009151.
    KOiK01227.
    OMAiFQFLKLS.
    OrthoDBiEOG6TXQWM.

    Family and domain databases

    InterProiIPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    IPR003646. SH3-like_bac-type.
    IPR007730. Sporulation-related_dom.
    [Graphical view]
    PfamiPF01832. Glucosaminidase. 1 hit.
    PF08239. SH3_3. 1 hit.
    PF05036. SPOR. 1 hit.
    [Graphical view]
    SMARTiSM00047. LYZ2. 1 hit.
    SM00287. SH3b. 1 hit.
    [Graphical view]
    PROSITEiPS51724. SPOR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P39848-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRLIAPML LSAASLAFFA MSGSAQAAAY TDYSLYKVEP SNTFSTESQA    50
    SQAVAKLEKD TGWDASYQAS GTTTTYQISA SGIHSESEAK AILSGLAKQT 100
    SITGTSSPVG SKQPYVTISS GAISGEKQAN TILAKLKQET GVAGAVKAYG 150
    AAQPYMNVMT SDIADETKVK ALIQSLAKQT GIKSSYQPIT HTVSVTTIQS 200
    GTIVGDSRAA QIKNAFQKES GLQASLKETV KGQAYYTFTT AAISGEANAK 250
    TLLQQLKQST GITGSYKSIN QKTTVESYNV QSAYFKGLST VKDAISQIKK 300
    NTGVSGSYQQ VGKSTSYTVN MKGITKQQLQ KIDTFFKKKK WHYTSSSVKK 350
    TTTSAAYQIT TAKILGEQQA NKAAAFFAQK KVKAAKTAAG STAENQYQLI 400
    SEETSDQAKV TKGLNILKKN QLSASAKSVK KQIADTFKIT TESLLDQTKV 450
    NQALTFFKSN HISVASQKTG QTAASSYQIT TEAIISQEEI DRVLTFFKQN 500
    HIAVTTSKTG QTAYTQYKIV TTQLSSKTAL NNGLTYLKSK SVTPSYTTKS 550
    NTLYKISVNE QFTGNDTAAA ASTKLKQLYG WTSSIVKIKN GPQIMKTNYN 600
    LSLRDMVQKQ MTVSPQTDGA AYVSLTYINT ATSTVTADVL NIRSTPEVSP 650
    TNVIGQFKKG DKVKVIGQIN GWAKINLGWR NASSDEVVQY VDPNNFSRDS 700
    KYYFQFLKLS QTAGLSVTEV NQKVLAGKGI LTGRAKAFID AANQYSINEL 750
    YLISHALLET GNGTSALANG LTYNGKTVYN MYGIGAYDSN PNYYGAKYAY 800
    EQGWFTPEAA IIGGAKFIGS SYIHNTAYNQ DTLYKMRWSA TATHQYATDI 850
    GWAYKQVNRM YSLYSLLDGY TLYFDVPEYR 880
    Length:880
    Mass (Da):95,554
    Last modified:February 1, 1995 - v1
    Checksum:i2A912A478FCFC1D1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02562 Genomic DNA. Translation: AAA67857.1.
    D45048 Genomic DNA. Translation: BAA08089.1.
    AL009126 Genomic DNA. Translation: CAB15595.1.
    PIRiS60137.
    RefSeqiNP_391459.1. NC_000964.3.
    WP_003243594.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15595; CAB15595; BSU35780.
    GeneIDi936822.
    KEGGibsu:BSU35780.
    PATRICi18979172. VBIBacSub10457_3748.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02562 Genomic DNA. Translation: AAA67857.1 .
    D45048 Genomic DNA. Translation: BAA08089.1 .
    AL009126 Genomic DNA. Translation: CAB15595.1 .
    PIRi S60137.
    RefSeqi NP_391459.1. NC_000964.3.
    WP_003243594.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P39848.
    SMRi P39848. Positions 632-682, 735-861.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU35780.

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Proteomic databases

    PaxDbi P39848.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15595 ; CAB15595 ; BSU35780 .
    GeneIDi 936822.
    KEGGi bsu:BSU35780.
    PATRICi 18979172. VBIBacSub10457_3748.

    Organism-specific databases

    GenoListi BSU35780. [Micado ]

    Phylogenomic databases

    eggNOGi COG4193.
    HOGENOMi HOG000009151.
    KOi K01227.
    OMAi FQFLKLS.
    OrthoDBi EOG6TXQWM.

    Enzyme and pathway databases

    BioCyci BSUB:BSU35780-MONOMER.

    Family and domain databases

    InterProi IPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    IPR003646. SH3-like_bac-type.
    IPR007730. Sporulation-related_dom.
    [Graphical view ]
    Pfami PF01832. Glucosaminidase. 1 hit.
    PF08239. SH3_3. 1 hit.
    PF05036. SPOR. 1 hit.
    [Graphical view ]
    SMARTi SM00047. LYZ2. 1 hit.
    SM00287. SH3b. 1 hit.
    [Graphical view ]
    PROSITEi PS51724. SPOR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis."
      Margot P., Maueel C., Karamata D.
      Mol. Microbiol. 12:535-545(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: 168.
    2. "Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization."
      Rashid M.H., Mori M., Sekiguchi J.
      Microbiology 141:2391-2404(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, REGULATION BY SIGD.
      Strain: 168 / AC327.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility."
      Rashid M.H., Kuroda A., Sekiguchi J.
      FEMS Microbiol. Lett. 112:135-140(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, DISRUPTION PHENOTYPE.
      Strain: 168 / AC327.
    5. "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic approach."
      Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.
      Proteomics 2:591-602(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiLYTD_BACSU
    AccessioniPrimary (citable) accession number: P39848
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 107 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, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3