P48816 (LYS_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lysozyme EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase
Organism	Bombyx mori (Silk moth) [Reference proteome]
Taxonomic identifier	7091 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Amphiesmenoptera › Lepidoptera › Glossata › Neolepidoptera › Heteroneura › Ditrysia › Obtectomera › Bombycoidea › Bombyciformes › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	137 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	Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Active against E.coli and M.luteus. Ref.2
Catalytic activity	Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Developmental stage	Expressed within 6 hours after induction, reaches maximum levels after 48 hours and declines after 72 hours after induction.
Induction	By bacterial infection.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	lysozyme 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 – 18

18

Ref.2

Chain

19 – 137

119

Lysozyme

PRO_0000018505

Sites

Active site

50

1

By similarity

Active site

67

1

By similarity

Amino acid modifications

Disulfide bond

24 ↔ 137

By similarity

Disulfide bond

45 ↔ 127

By similarity

Disulfide bond

79 ↔ 93

By similarity

Disulfide bond

89 ↔ 107

By similarity

Secondary structure

1

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137

Helix Strand Turn

Details...

Helix

23 – 32

10

Helix

37 – 39

3

Helix

40 – 50

11

Turn

51 – 53

3

Beta strand

58 – 60

3

Beta strand

66 – 68

3

Turn

69 – 72

4

Turn

75 – 78

4

Beta strand

80 – 84

5

Turn

87 – 90

4

Helix

93 – 96

4

Beta strand

97 – 99

3

Helix

102 – 115

14

Helix

116 – 119

4

Helix

121 – 124

4

Beta strand

127 – 129

3

Sequences

	Sequence		Length	Mass (Da)
	P48816 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: FFE5710506C61A1D	FASTA	137	15,668
	10 20 30 40 50 60 MQKLIIFALV VLCVGSEAKT FTRCGLVHEL RKHGFEENLM RNWVCLVEHE SSRDTSKTNT 70 80 90 100 110 120 NRNGSKDYGL FQINDRYWCS KGASPGKDCN VKCSDLLTDD ITKAAKCAKK IYKRHRFDAW 130 YGWKNHCQGS LPDISSC

References

[1]	"Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori." Lee W.J., Brey P.T. Gene 161:199-203(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fat body.
[2]	"Purification and partial characterization of an induced antibacterial protein in the silkworm, Bombyx mori." Abraham E.G., Nagaraju J., Salunke D., Gupta H.M., Datta R.K. J. Invertebr. Pathol. 65:17-24(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-38, FUNCTION. Strain: NB18. Tissue: Larval hemolymph.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L37416 mRNA. Translation: AAB40947.1.

PIR

JC4233.

RefSeq

NP_001037448.1. NM_001043983.1.

UniGene

Bmo.2011.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GD6	X-ray	2.50	A	19-137	[»]
2RSC	NMR	-	A	19-137	[»]

ProteinModelPortal

P48816.

SMR

P48816. Positions 19-137.

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

BGIBMGA010439-RA; BGIBMGA010439-TA; BGIBMGA010439.

GeneID

693015.

Organism-specific databases

CTD

693015.

Phylogenomic databases

OMA

RVTNYNP.

OrthoDB

EOG4CNP7F.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P48816.

Entry information

Entry name

LYS_BOMMO

Accession

Primary (citable) accession number: P48816
Secondary accession number(s): Q9TWL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)