Reviewed, UniProtKB/Swiss-Prot P39848 (LYTD_BACSU)

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › cell 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Repeat Signal
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amidase activity Inferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27
	Chain	28 – 880	853	Beta-N-acetylglucosaminidase		PRO_0000012118
Regions
	Repeat	439 – 473	35	1
	Repeat	479 – 513	35	2
	Compositional bias	72 – 75	4	Poly-Thr
	Compositional bias	337 – 340	4	Poly-Lys
	Compositional bias	568 – 571	4	Poly-Ala

Sequences

	Sequence		Length	Mass (Da)
	P39848-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 2A912A478FCFC1D1	FASTA	880	95,554
	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

References

	« Hide 'large scale' referencesShow '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: 7934877] [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: 7581999] [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: 9384377] [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: 8405954] [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: 11987133] [Abstract] Cited for: MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION. 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.
PIR	S60137.
RefSeq	NP_391459.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Genome annotation databases
GeneID	936822.
GenomeReviews	Gene locus BSU35780 in contig AL009126_GR.
KEGG	bsu:BSU35780.
NMPDR	fig|224308.1.peg.3585.
Organism-specific databases
SubtiList	BG10455. lytD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	HBG338369.
OMA	GAYDSNP.
Enzyme and pathway databases
BRENDA	3.2.1.96. 150.
Family and domain databases
InterPro	IPR013338. Lysozyme_dom_subfam2. IPR002901. Mano_Glyc_endo_b_GlcNAc. IPR003646. SH3-like_bac. IPR013247. SH3_3. IPR007730. Sporulation_related_dom. [Graphical view]
Pfam	PF01832. Glucosaminidase. 1 hit. PF08239. SH3_3. 1 hit. PF05036. SPOR. 1 hit. [Graphical view]
SMART	SM00047. LYZ2. 1 hit. SM00287. SH3b. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYTD_BACSU

Accession

Primary (citable) accession number: P39848

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 19, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)