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P32762 (ALYS_BPHB3) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Lytic amidase

EC=3.5.1.28
Alternative name(s):
N-acetylmuramoyl-L-alanine amidase
Gene names
Name:HBL
OrganismStreptococcus pneumoniae phage HB-3
Taxonomic identifier10728 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridae
Virus hostStreptococcus pneumoniae [TaxID: 1313]

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Contains 6 cell wall-binding repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   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 – 318318Lytic amidase
PRO_0000164406

Regions

Repeat175 – 19420Cell wall-binding 1
Repeat196 – 21520Cell wall-binding 2
Repeat217 – 23721Cell wall-binding 3
Repeat238 – 25720Cell wall-binding 4
Repeat258 – 27720Cell wall-binding 5
Repeat280 – 30122Cell wall-binding 6

Sequences

Sequence LengthMass (Da)Tools
P32762 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 65B30A9127E58351

FASTA31836,509
        10         20         30         40         50         60 
MDIDRNRLRT GLPQVGVQPY RQVHAHSTGN RNSTVQNEAD YHWRKDPELG FFSHVVGNFR 

        70         80         90        100        110        120 
IMQVGPVNNG SWDVGGGWNA ETYAAVELIE SHSTKEEFMA DYRLYIELLR NLADEAGLPK 

       130        140        150        160        170        180 
TLDTDDLAGI KTHEYCTNNQ PNNHSDHVDP YPYLASWGIS REQFKQDIEN GLSAATGWQK 

       190        200        210        220        230        240 
NGTGYWYVHS DGSYSKDKFE KINGTWYYFD GSGYMLSDRW KKHTDGNWYY FDQSGEMATG 

       250        260        270        280        290        300 
WKKIADKWYY FDVEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT 

       310 
LADKPEFTVE PDGLITVK 

« Hide

References

[1]"Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin."
Romero A., Lopez R., Garcia P.
J. Bacteriol. 172:5064-5070(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning and expression in Escherichia coli."
Romero A., Lopez R., Garcia P.
J. Virol. 64:137-142(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34652 Genomic DNA. Translation: AAA50574.1.
PIRS16016.

3D structure databases

ProteinModelPortalP32762.
SMRP32762. Positions 188-318.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
PROSITEPS51170. CW. 6 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALYS_BPHB3
AccessionPrimary (citable) accession number: P32762
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families