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P85143 (NAAA_LYSSP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-acetylmuramoyl-L-alanine amidase L2

EC=3.5.1.28
OrganismLysobacter sp.
Taxonomic identifier72226 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

Protein attributes

Sequence length13 AA.
Sequence statusFragment.
Protein existenceEvidence 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 componentSecreted
   Molecular functionAntibiotic
Antimicrobial
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›13›13N-acetylmuramoyl-L-alanine amidase L2
PRO_0000287396

Experimental info

Non-terminal residue131

Sequences

Sequence LengthMass (Da)Tools
P85143 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 49FA0BA84E42E447

FASTA131,547
        10 
XNVVFLNXPX PQW 

« Hide

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

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameNAAA_LYSSP
AccessionPrimary (citable) accession number: P85143
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program