P25310 (LYSM1_STRGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysozyme M1
EC=3.2.1.17

Alternative name(s):
1,4-beta-N-acetylmuramidase M1

Gene names

Name:

acm

Organism

Streptomyces globisporus

Taxonomic identifier

1908 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	294 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	This enzyme has both lysozyme (acetylmuramidase) and diacetylmuramidase activities.
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.
Subcellular location	Secreted › extracellular space.
Sequence similarities	Belongs to the glycosyl hydrolase 25 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – ?

Potential

Propeptide

? – 77

PRO_0000018517

Chain

78 – 294

217

Lysozyme M1

PRO_0000018518

Sites

Active site

86

1

By similarity

Active site

177

1

By similarity

Amino acid modifications

Disulfide bond

185 ↔ 224

Ref.1

Secondary structure

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294

Helix Strand Turn

Details...

Beta strand

81 – 87

7

Helix

89 – 91

3

Helix

96 – 101

6

Beta strand

106 – 113

8

Turn

114 – 116

3

Helix

122 – 131

10

Beta strand

135 – 141

7

Turn

144 – 146

3

Helix

149 – 158

10

Beta strand

166 – 169

4

Beta strand

173 – 175

3

Beta strand

180 – 182

3

Turn

184 – 187

4

Helix

190 – 208

19

Beta strand

213 – 216

4

Helix

218 – 225

8

Turn

230 – 234

5

Beta strand

237 – 240

4

Beta strand

253 – 255

3

Beta strand

257 – 267

11

Beta strand

270 – 281

12

Helix

283 – 291

9

Sequences

	Sequence		Length	Mass (Da)
	P25310 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: D96EFE914FA04997	FASTA	294	31,169
	10 20 30 40 50 60 MPAYSSLARR GRRPAVVLLG GLVSASLALT LAPTAAAAPL APPPGKDVGP GEAYMGVGTR 70 80 90 100 110 120 IEQGLGAGPD ERTIGPADTS GVQGIDVSHW QGSINWSSVK SAGMSFAYIK ATEGTNYKDD 130 140 150 160 170 180 RFSANYTNAY NAGIIRGAYH FARPNASSGT AQADYFASNG GGWSRDNRTL PGVLDIEHNP 190 200 210 220 230 240 SGAMCYGLST TQMRTWINDF HARYKARTTR DVVIYTTASW WNTCTGSWNG MAAKSPFWVA 250 260 270 280 290 HWGVSAPTVP SGFPTWTFWQ YSATGRVGGV SGDVDRNKFN GSAARLLALA NNTA

References

[1]	"Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene from Streptomyces globisporus." Lichenstein H.S., Hastings A.E., Langley K.E., Mendiaz E.A., Rohde M.F., Elmore R., Zukowski M.M. Gene 88:81-86(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 78-117, DISULFIDE BOND. Strain: ATCC 21553 / DSM 40991 / FERM P-596.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M30645 Genomic DNA. Translation: AAA26687.1.

PIR

MUSMM1. JQ0529.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JFX	X-ray	1.65	A	78-294	[»]

ProteinModelPortal

P25310.

SMR

P25310. Positions 78-294.

ModBase

Search...

Protein family/group databases

CAZy

GH25. Glycoside Hydrolase Family 25.

Proteomic databases

PRIDE

P25310.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF01183. Glyco_hydro_25. 1 hit.
[Graphical view]

SMART

SM00641. Glyco_25. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25310.

Entry information

Entry name

LYSM1_STRGL

Accession

Primary (citable) accession number: P25310

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program