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P81730 (ACLY_ACHLY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Achromolysin

EC=3.4.24.-
OrganismAchromobacter lyticus
Taxonomic identifier224 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

Protein attributes

Sequence length119 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has staphylolytic activity.

Cofactor

Binds 4 calcium ions per subunit Potential.

Binds 1 zinc ion per subunit Potential.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M4 family.

Ontologies

Keywords
   Cellular componentSecreted
   LigandCalcium
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›119›119Achromolysin
PRO_0000078174

Experimental info

Non-adjacent residues42 – 432
Non-adjacent residues62 – 632
Non-adjacent residues80 – 812
Non-terminal residue1191

Sequences

Sequence LengthMass (Da)Tools
P81730 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: 738F492DDB14F18D

FASTA11912,555
        10         20         30         40         50         60 
AQVGTGPGGN QKIGQYEYGS GGRPFLDVAQ SGSTYTFNTT NLTVNLNHGT SGSTAYSYTG 

        70         80         90        100        110 
PRNTINGAYS PLNDAHYFGR DYWTPSTNFN QGGQGVRQAA ADLGYSTADV IDAFRQVGV 

« Hide

References

[1]"Achromolysin, a metalloproteinase from Achromobacter lyticus."
Li S.L.
Submitted (MAR-1999) to UniProtKB
Cited for: PROTEIN SEQUENCE.
Strain: M497-1.

Cross-references

3D structure databases

ProteinModelPortalP81730.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.170.10. 1 hit.
InterProIPR013856. Peptidase_M4_domain.
[Graphical view]
PfamPF01447. Peptidase_M4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACLY_ACHLY
AccessionPrimary (citable) accession number: P81730
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries