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P39848

- LYTD_BACSU

UniProt

P39848 - LYTD_BACSU

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Protein

Beta-N-acetylglucosaminidase

Gene
lytD, cwlG, BSU35780
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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. Secretedcell wall 1 Publication

GO - Cellular componenti

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

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 (1 Publication); under control of SigD (1 Publication).2 Publications

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.BSU35780.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini235 – 30672SPORAdd
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

Contains 1 SPOR domain.

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]

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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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