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	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