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P00801 (PRLB_LYSEN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-lytic metalloendopeptidase

EC=3.4.24.32
Alternative name(s):
Beta-lytic protease
OrganismLysobacter enzymogenes
Taxonomic identifier69 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO3H).

Cofactor

Binds 1 zinc ion per subunit.

Sequence similarities

Belongs to the peptidase M23A family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Beta-lytic metalloendopeptidase
PRO_0000165903

Sites

Metal binding1201Zinc Potential
Metal binding1221Zinc Potential

Amino acid modifications

Disulfide bond65 ↔ 111 Ref.1
Disulfide bond155 ↔ 168 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00801 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9EFCD3DD45FD2870

FASTA17819,100
        10         20         30         40         50         60 
SPNGLLQFPF PRGASWHVGG AHTNTGSGNY PMSSLDMSRG GGSNQNGNWV SASAAGGSFK 

        70         80         90        100        110        120 
RHSSCFAEIV HTGGWSTTYY HLMNIQYNTG ANVSMNTAIA NAPNTQAQAL CNGGQSTGPH 

       130        140        150        160        170 
QHWSLKQNGS FYHLNGTYLS GYRITATGSS YDTNCSRFYL TKNGQNYCYG YYVNPGPN 

« Hide

References

[1]Damaglou A.P., Allen L.C., Whitaker D.R.
Submitted (MAR-1974) to the PIR data bank
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.

Cross-references

Sequence databases

PIRLYYXB4. A00994.

3D structure databases

ProteinModelPortalP00801.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011055. Dup_hybrid_motif.
IPR000841. Pept_M23A_Blytic.
IPR016047. Peptidase_M23.
[Graphical view]
PfamPF01551. Peptidase_M23. 1 hit.
[Graphical view]
PRINTSPR00933. BLYTICPTASE.
SUPFAMSSF51261. Dup_hybrid_motif. 1 hit.
ProtoNetSearch...

Entry information

Entry namePRLB_LYSEN
AccessionPrimary (citable) accession number: P00801
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families