Reviewed, UniProtKB/Swiss-Prot P00720 (LYS_BPT4)

Names and origin

Protein names

Recommended name:
    Lysozyme
    EC=3.2.1.17
Alternative name(s):
    Lysis protein
    Muramidase
    Endolysin

Gene names

Name:

E

Organism

Enterobacteria phage T4 (Bacteriophage T4)

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › T4-like viruses

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 24 family.

Ontologies

Keywords
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall 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 peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	lysozyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 164

164

Lysozyme

PRO_0000218107

Sites

Active site

11

1

Proton donor

Active site

20

1

Nucleophile

Experimental info

Sequence conflict

12

1

G → R Ref.3 Ref.4

Sequence conflict

137

1

R → I Ref.3 Ref.4

Secondary structure

1

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164

Helix Strand Turn

Details...

Helix

3 – 11

9

Beta strand

14 – 19

6

Beta strand

25 – 28

4

Helix

39 – 50

12

Helix

60 – 80

21

Helix

84 – 90

7

Helix

93 – 106

14

Helix

108 – 112

5

Helix

115 – 122

8

Helix

126 – 133

8

Helix

137 – 141

5

Helix

143 – 155

13

Beta strand

156 – 158

3

Turn

159 – 163

5

Sequences

	Sequence		Length	Mass (Da)
	P00720-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 6042E2F77B6308A0	FASTA	164	18,635
	10 20 30 40 50 60 MNIFEMLRID EGLRLKIYKD TEGYYTIGIG HLLTKSPSLN AAKSELDKAI GRNCNGVITK 70 80 90 100 110 120 DEAEKLFNQD VDAAVRGILR NAKLKPVYDS LDAVRRCALI NMVFQMGETG VAGFTNSLRM 130 140 150 160 LQQKRWDEAA VNLAKSRWYN QTPNRAKRVI TTFRTGTWDA YKNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The amino acid sequence of T4 phage lysozyme. IV. Dilute acid hydrolysis and the order of tryptic peptides." Inouye M., Imada M., Tsugita A. J. Biol. Chem. 245:3479-3484(1970) [PubMed: 5470817] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Nucleotide sequence of the lysozyme gene of bacteriophage T4. Analysis of mutations involving repeated sequences." Owen J.E., Schultz D.W., Taylor A., Smith G.R. J. Mol. Biol. 165:229-248(1983) [PubMed: 6302287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of bacteriophage T4." Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K. Nucleic Acids Res. 14:8637-8654(1986) [PubMed: 3024113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Bacteriophage T4 genome." Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W. Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed: 12626685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The three dimensional structure of the lysozyme from bacteriophage T4." Matthews B.W., Remington S.J. Proc. Natl. Acad. Sci. U.S.A. 71:4178-4182(1974) [PubMed: 4530293] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]	"Structure of bacteriophage T4 lysozyme refined at 1.7-A resolution." Weaver L.H., Matthews B.W. J. Mol. Biol. 193:189-200(1987) [PubMed: 3586019] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[7]	"Atomic coordinates for T4 phage lysozyme." Remington S.J., ten Eyck L.F., Matthews B.W. Biochem. Biophys. Res. Commun. 75:265-270(1977) [PubMed: 322662] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[8]	"Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3." Matsumura M., Becktel W.J., Matthews B.W. Nature 334:406-410(1988) [PubMed: 3405287] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT ILE-3.
[9]	"A mutant T4 lysozyme displays five different crystal conformations." Faber H.R., Matthews B.W. Nature 348:263-266(1990) [PubMed: 2234094] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
[10]	"A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene." Eriksson A.E., Baase W.A., Wozniak J.A., Matthews B.W. Nature 355:371-373(1992) [PubMed: 1731252] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT.
[11]	"Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme." McIntosh L.P., Wand A.J., Lowry D.F., Redfield A.G., Dahlquist F.W. Biochemistry 29:6341-6362(1990) [PubMed: 2207079] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04567 Genomic DNA. Translation: CAA28212.1.
AF158101 Genomic DNA. Translation: AAD42568.1.

PIR

LZBPT4. A92896.

RefSeq

NP_049736.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
102L	X-ray	1.74	A	1-164	[»]
103L	X-ray	1.90	A	1-164	[»]
104L	X-ray	2.80	A/B	1-164	[»]
107L	X-ray	1.80	A	1-164	[»]
108L	X-ray	1.80	A	1-164	[»]
109L	X-ray	1.85	A	1-164	[»]
110L	X-ray	1.70	A	1-164	[»]
111L	X-ray	1.80	A	1-164	[»]
112L	X-ray	1.80	A	1-164	[»]
113L	X-ray	1.80	A	1-164	[»]
114L	X-ray	1.80	A	1-164	[»]
115L	X-ray	1.80	A	1-164	[»]
118L	X-ray	1.80	A	1-164	[»]
119L	X-ray	1.65	A	1-164	[»]
120L	X-ray	1.80	A	1-164	[»]
122L	X-ray	1.80	A	1-164	[»]
123L	X-ray	1.80	A	1-164	[»]
125L	X-ray	1.85	A	1-164	[»]
126L	X-ray	1.80	A	1-164	[»]
127L	X-ray	1.85	A	1-164	[»]
128L	X-ray	1.70	A	1-164	[»]
129L	X-ray	1.70	A	1-164	[»]
130L	X-ray	1.70	A	1-164	[»]
131L	X-ray	1.70	A	1-164	[»]
137L	X-ray	1.85	A/B	1-164	[»]
138L	X-ray	1.70	A	1-164	[»]
139L	X-ray	1.70	A	1-164	[»]
140L	X-ray	2.10	A	1-164	[»]
141L	X-ray	2.00	A	1-164	[»]
142L	X-ray	2.00	A	1-164	[»]
143L	X-ray	2.00	A	1-164	[»]
144L	X-ray	2.10	A	1-164	[»]
145L	X-ray	2.00	A	1-164	[»]
146L	X-ray	1.85	A	1-164	[»]
147L	X-ray	2.00	A	1-164	[»]
148L	X-ray	1.90	E	1-164	[»]
149L	X-ray	2.60	A	1-164	[»]
150L	X-ray	2.20	A/B/C/D	1-164	[»]
151L	X-ray	2.20	A	1-164	[»]
152L	X-ray	2.00	A	1-163	[»]
155L	X-ray	1.85	A	1-164	[»]
156L	X-ray	1.80	A	1-164	[»]
157L	X-ray	1.85	A	1-164	[»]
158L	X-ray	1.80	A	1-164	[»]
159L	X-ray	1.80	A	1-164	[»]
160L	X-ray	1.80	A	1-164	[»]
161L	X-ray	1.70	A	1-164	[»]
162L	X-ray	1.80	A	1-164	[»]
163L	X-ray	1.80	A	1-164	[»]
164L	X-ray	1.80	A	1-164	[»]
165L	X-ray	1.75	A	1-164	[»]
166L	X-ray	1.75	A	1-164	[»]
167L	X-ray	2.20	A/B	1-163	[»]
168L	X-ray	2.90	A/B/C/D/E	1-164	[»]
169L	X-ray	3.00	A/B/C/D/E	1-164	[»]
170L	X-ray	2.60	A	1-164	[»]
171L	X-ray	2.50	A	1-164	[»]
172L	X-ray	1.90	A	1-164	[»]
173L	X-ray	1.70	A	1-164	[»]
174L	X-ray	2.30	A/B	1-164	[»]
175L	X-ray	2.10	A/B	1-164	[»]
176L	X-ray	2.20	A/B	1-164	[»]
177L	X-ray	2.20	A	1-164	[»]
178L	X-ray	2.70	A	1-164	[»]
179L	X-ray	2.70	A	1-164	[»]
180L	X-ray	1.75	A/B	1-164	[»]
181L	X-ray	1.80	A	1-164	[»]
182L	X-ray	1.80	A	1-164	[»]
183L	X-ray	1.80	A	1-164	[»]
184L	X-ray	1.80	A	1-164	[»]
185L	X-ray	1.80	A	1-164	[»]
186L	X-ray	1.80	A	1-164	[»]
187L	X-ray	1.80	A	1-164	[»]
188L	X-ray	1.80	A	1-164	[»]
189L	X-ray	2.50	A	1-164	[»]
190L	X-ray	2.00	A	1-164	[»]
191L	X-ray	1.95	A	1-164	[»]
192L	X-ray	1.90	A	1-164	[»]
195L	X-ray	1.90	A	1-164	[»]
196L	X-ray	2.30	A	1-164	[»]
197L	X-ray	2.10	A	1-164	[»]
198L	X-ray	2.00	A	1-164	[»]
199L	X-ray	1.85	A	1-164	[»]
1B6I	X-ray	1.90	A	1-164	[»]
1C60	X-ray	2.00	A	1-164	[»]
1C61	X-ray	2.00	A	1-164	[»]
1C62	X-ray	2.30	A	1-164	[»]
1C63	X-ray	2.00	A	1-164	[»]
1C64	X-ray	2.00	A	1-164	[»]
1C65	X-ray	2.00	A	1-164	[»]
1C66	X-ray	2.10	A	1-164	[»]
1C67	X-ray	2.20	A	1-164	[»]
1C68	X-ray	2.50	A	1-164	[»]
1C69	X-ray	1.80	A	1-164	[»]
1C6A	X-ray	2.10	A	1-164	[»]
1C6B	X-ray	2.20	A	1-164	[»]
1C6C	X-ray	2.00	A	1-164	[»]
1C6D	X-ray	2.00	A	1-164	[»]
1C6E	X-ray	1.90	A	1-164	[»]
1C6F	X-ray	2.00	A	1-164	[»]
1C6G	X-ray	1.90	A	1-164	[»]
1C6H	X-ray	1.90	A	1-164	[»]
1C6I	X-ray	1.90	A	1-164	[»]
1C6J	X-ray	1.90	A	1-164	[»]
1C6K	X-ray	1.90	A	1-164	[»]
1C6L	X-ray	1.90	A	1-164	[»]
1C6M	X-ray	2.10	A	1-164	[»]
1C6N	X-ray	2.20	A	1-164	[»]
1C6P	X-ray	1.90	A	1-164	[»]
1C6Q	X-ray	1.90	A	1-164	[»]
1C6T	X-ray	2.00	A	1-164	[»]
1CTW	X-ray	2.10	A	1-164	[»]
1CU0	X-ray	2.20	A	1-164	[»]
1CU2	X-ray	1.85	A	1-164	[»]
1CU3	X-ray	2.12	A	1-164	[»]
1CU5	X-ray	2.05	A	1-164	[»]
1CU6	X-ray	2.10	A	1-164	[»]
1CUP	X-ray	1.89	A	1-164	[»]
1CUQ	X-ray	2.05	A	1-164	[»]
1CV0	X-ray	2.12	A	1-164	[»]
1CV1	X-ray	2.10	A	1-164	[»]
1CV3	X-ray	1.80	A	1-164	[»]
1CV4	X-ray	1.90	A	1-164	[»]
1CV5	X-ray	1.87	A	1-164	[»]
1CV6	X-ray	1.90	A	1-164	[»]
1CVK	X-ray	1.80	A	1-164	[»]
1CX6	X-ray	2.01	A	1-164	[»]
1CX7	X-ray	1.94	A	1-164	[