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P25310 (LYSM1_STRGL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 81. 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:
Lysozyme M1

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase M1
Gene names
Name:acm
OrganismStreptomyces globisporus
Taxonomic identifier1908 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 25 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate 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_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Propeptide? – 77PRO_0000018517
Chain78 – 294217Lysozyme M1
PRO_0000018518

Sites

Active site861 By similarity
Active site1771 By similarity

Amino acid modifications

Disulfide bond185 ↔ 224 Ref.1

Secondary structure

............................................ 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25310 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: D96EFE914FA04997

FASTA29431,169
        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 

« Hide

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.
PIRMUSMM1. JQ0529.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFXX-ray1.65A78-294[»]
ProteinModelPortalP25310.
SMRP25310. Positions 78-294.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH25. Glycoside Hydrolase Family 25.

Proteomic databases

PRIDEP25310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01183. Glyco_hydro_25. 1 hit.
[Graphical view]
SMARTSM00641. Glyco_25. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25310.

Entry information

Entry nameLYSM1_STRGL
AccessionPrimary (citable) accession number: P25310
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 81 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries