Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39848 (LYTD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-N-acetylglucosaminidase

EC=3.2.1.96
Alternative name(s):
Cell wall-associated polypeptide 90
Short name=CWBP90
Gene names
Name:lytD
Synonyms:cwlG
Ordered Locus Names:BSU35780
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length880 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

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 regulation

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

Subunit structure

Homodimer.

Subcellular location

Secreted. Secretedcell wall Ref.5.

Induction

In stationary phase (Ref.5); under control of SigD (Ref.2). Ref.2 Ref.5

Disruption phenotype

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. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 73 family.

Contains 1 SPOR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.4
Chain28 – 880853Beta-N-acetylglucosaminidase
PRO_0000012118

Regions

Domain235 – 30672SPOR
Repeat439 – 473351
Repeat479 – 513352
Compositional bias72 – 754Poly-Thr
Compositional bias337 – 3404Poly-Lys
Compositional bias568 – 5714Poly-Ala

Sequences

Sequence LengthMass (Da)Tools
P39848 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 2A912A478FCFC1D1

FASTA88095,554
        10         20         30         40         50         60 
MKKRLIAPML LSAASLAFFA MSGSAQAAAY TDYSLYKVEP SNTFSTESQA SQAVAKLEKD 

        70         80         90        100        110        120 
TGWDASYQAS GTTTTYQISA SGIHSESEAK AILSGLAKQT SITGTSSPVG SKQPYVTISS 

       130        140        150        160        170        180 
GAISGEKQAN TILAKLKQET GVAGAVKAYG AAQPYMNVMT SDIADETKVK ALIQSLAKQT 

       190        200        210        220        230        240 
GIKSSYQPIT HTVSVTTIQS GTIVGDSRAA QIKNAFQKES GLQASLKETV KGQAYYTFTT 

       250        260        270        280        290        300 
AAISGEANAK TLLQQLKQST GITGSYKSIN QKTTVESYNV QSAYFKGLST VKDAISQIKK 

       310        320        330        340        350        360 
NTGVSGSYQQ VGKSTSYTVN MKGITKQQLQ KIDTFFKKKK WHYTSSSVKK TTTSAAYQIT 

       370        380        390        400        410        420 
TAKILGEQQA NKAAAFFAQK KVKAAKTAAG STAENQYQLI SEETSDQAKV TKGLNILKKN 

       430        440        450        460        470        480 
QLSASAKSVK KQIADTFKIT TESLLDQTKV NQALTFFKSN HISVASQKTG QTAASSYQIT 

       490        500        510        520        530        540 
TEAIISQEEI DRVLTFFKQN HIAVTTSKTG QTAYTQYKIV TTQLSSKTAL NNGLTYLKSK 

       550        560        570        580        590        600 
SVTPSYTTKS NTLYKISVNE QFTGNDTAAA ASTKLKQLYG WTSSIVKIKN GPQIMKTNYN 

       610        620        630        640        650        660 
LSLRDMVQKQ MTVSPQTDGA AYVSLTYINT ATSTVTADVL NIRSTPEVSP TNVIGQFKKG 

       670        680        690        700        710        720 
DKVKVIGQIN GWAKINLGWR NASSDEVVQY VDPNNFSRDS KYYFQFLKLS QTAGLSVTEV 

       730        740        750        760        770        780 
NQKVLAGKGI LTGRAKAFID AANQYSINEL YLISHALLET GNGTSALANG LTYNGKTVYN 

       790        800        810        820        830        840 
MYGIGAYDSN PNYYGAKYAY EQGWFTPEAA IIGGAKFIGS SYIHNTAYNQ DTLYKMRWSA 

       850        860        870        880 
TATHQYATDI GWAYKQVNRM YSLYSLLDGY TLYFDVPEYR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02562 Genomic DNA. Translation: AAA67857.1.
D45048 Genomic DNA. Translation: BAA08089.1.
AL009126 Genomic DNA. Translation: CAB15595.1.
PIRS60137.
RefSeqNP_391459.1. NC_000964.3.

3D structure databases

ProteinModelPortalP39848.
SMRP39848. Positions 632-682, 735-861.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU35780.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Proteomic databases

PaxDbP39848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15595; CAB15595; BSU35780.
GeneID936822.
KEGGbsu:BSU35780.
PATRIC18979172. VBIBacSub10457_3748.

Organism-specific databases

GenoListBSU35780. [Micado]

Phylogenomic databases

eggNOGCOG4193.
HOGENOMHOG000009151.
KOK01227.
OMAFQFLKLS.
OrthoDBEOG6TXQWM.
ProtClustDBCLSK887978.

Enzyme and pathway databases

BioCycBSUB:BSU35780-MONOMER.

Family and domain databases

InterProIPR013338. Lysozyme_dom_subfam2.
IPR002901. Mano_Glyc_endo_b_GlcNAc.
IPR003646. SH3-like_bac-type.
IPR007730. Sporulation-related_dom.
[Graphical view]
PfamPF01832. Glucosaminidase. 1 hit.
PF08239. SH3_3. 1 hit.
PF05036. SPOR. 1 hit.
[Graphical view]
SMARTSM00047. LYZ2. 1 hit.
SM00287. SH3b. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYTD_BACSU
AccessionPrimary (citable) accession number: P39848
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList