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Protein

Lytic amidase

Gene

HBL

Organism
Streptococcus pneumoniae phage HB-3
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Lytic amidase (EC:3.5.1.28)
Alternative name(s):
N-acetylmuramoyl-L-alanine amidase
Gene namesi
Name:HBL
OrganismiStreptococcus pneumoniae phage HB-3
Taxonomic identifieri10728 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridae
Virus hostiStreptococcus pneumoniae [TaxID: 1313]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Lytic amidasePRO_0000164406Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP32762.
SMRiP32762. Positions 188-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 19420Cell wall-binding 1Add
BLAST
Repeati196 – 21520Cell wall-binding 2Add
BLAST
Repeati217 – 23721Cell wall-binding 3Add
BLAST
Repeati238 – 25720Cell wall-binding 4Add
BLAST
Repeati258 – 27720Cell wall-binding 5Add
BLAST
Repeati280 – 30122Cell wall-binding 6Add
BLAST

Sequence similaritiesi

Contains 6 cell wall-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51170. CW. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIDRNRLRT GLPQVGVQPY RQVHAHSTGN RNSTVQNEAD YHWRKDPELG
60 70 80 90 100
FFSHVVGNFR IMQVGPVNNG SWDVGGGWNA ETYAAVELIE SHSTKEEFMA
110 120 130 140 150
DYRLYIELLR NLADEAGLPK TLDTDDLAGI KTHEYCTNNQ PNNHSDHVDP
160 170 180 190 200
YPYLASWGIS REQFKQDIEN GLSAATGWQK NGTGYWYVHS DGSYSKDKFE
210 220 230 240 250
KINGTWYYFD GSGYMLSDRW KKHTDGNWYY FDQSGEMATG WKKIADKWYY
260 270 280 290 300
FDVEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT
310
LADKPEFTVE PDGLITVK
Length:318
Mass (Da):36,509
Last modified:October 1, 1993 - v1
Checksum:i65B30A9127E58351
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34652 Genomic DNA. Translation: AAA50574.1.
PIRiS16016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34652 Genomic DNA. Translation: AAA50574.1.
PIRiS16016.

3D structure databases

ProteinModelPortaliP32762.
SMRiP32762. Positions 188-318.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR002502. Amidase_domain.
IPR018337. Cell_wall/Cho-bd_repeat.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01473. CW_binding_1. 5 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51170. CW. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiALYS_BPHB3
AccessioniPrimary (citable) accession number: P32762
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.