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Reviewed, UniProtKB/Swiss-Prot P00801 (PRLB_LYSEN)

Last modified March 3, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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: InterPro

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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
P00801-1 [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

ModBaseSearch...

Protein family/group databases

MEROPSM23.001.

Enzyme and pathway databases

BRENDA3.4.24.32. 19052.

Family and domain databases

InterProIPR000841. Pept_M23A_Blytic.
[Graphical view]
PRINTSPR00933. BLYTICPTASE.
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: March 3, 2009
This is version 47 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)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents