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Reviewed, UniProtKB/Swiss-Prot P85143 (NAAA_LYSSP)

Last modified June 16, 2009. Version 7. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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.
Sequence processingThe displayed sequence is not processed.
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: 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
P85143-1 [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...

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: June 16, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information