P85152 (LYS1_LYSSX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lysozyme EC=3.2.1.17 Alternative name(s): Endolysin Lysis protein Muramidase L3
Organism	Lysobacter sp. (strain XL1)
Taxonomic identifier	186334 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter

Protein attributes

Sequence length	20 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has bacteriolytic activity. Ref.1
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. Ref.1
Subunit structure	Monomer. Ref.1
Subcellular location	Secreted Ref.1.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. Ref.1 Temperature dependence: Optimum temperature is 60 degrees Celsius. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region 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
	Chain	1 – ›20	›20	Lysozyme		PRO_0000291306
Experimental info
	Non-terminal residue	20	1

Sequences

	Sequence		Length	Mass (Da)
	P85152 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 8F48EE97DE5EC7AB	FASTA	20	2,094
	10 20 IAIQGGXGYL XQPGDGYKYA

References

[1]	"Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1." Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S. Submitted (MAY-2007) to UniProtKB Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

LYS1_LYSSX

Accession

Primary (citable) accession number: P85152

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	October 5, 2010
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program