P85143 (NAAA_LYSSP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: N-acetylmuramoyl-L-alanine amidase L2 EC=3.5.1.28
Organism	Lysobacter sp.
Taxonomic identifier	72226 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter

Protein attributes

Sequence length	13 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has bacteriolytic activity. Ref.1
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Ref.1
Enzyme regulation	Inhibited by phenylmethanesulfonyl fluoride (PMSF) and EDTA. 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 65 degrees Celsius. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase 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 – ›13	›13	N-acetylmuramoyl-L-alanine amidase L2		PRO_0000287396
Experimental info
	Non-terminal residue	13	1

Sequences

	Sequence		Length	Mass (Da)
	P85143 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 49FA0BA84E42E447	FASTA	13	1,547
	10 XNVVFLNXPX PQW

References

[1]

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

Cross-references

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

Entry information

Entry name

NAAA_LYSSP

Accession

Primary (citable) accession number: P85143

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 15, 2007
Last modified:	June 16, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program