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P06653 (ALYS_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 117. 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:
Autolysin

EC=3.5.1.28
Alternative name(s):
Cell wall hydrolase
Mucopeptide aminohydrolase
Murein hydrolase
N-acetylmuramoyl-L-alanine amidase
Gene names
Name:lytA
Ordered Locus Names:SP_1937
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

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

General annotation (Comments)

Function

Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity.

Catalytic activity

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

Subcellular location

Secreted Potential.

Domain

The C-terminal domain could be responsible for the substrate recognition.

Sequence similarities

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

Contains 6 cell wall-binding repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Autolysin
PRO_0000164408

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

Experimental info

Sequence conflict3041K → R Ref.1
Sequence conflict3041K → R Ref.2

Secondary structure

......................................................... 318
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06653 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 3CA7F3CD132FB502

FASTA31836,544
        10         20         30         40         50         60 
MEINVSKLRT DLPQVGVQPY RQVHAHSTGN PHSTVQNEAD YHWRKDPELG FFSHIVGNGC 

        70         80         90        100        110        120 
IMQVGPVDNG AWDVGGGWNA ETYAAVELIE SHSTKEEFMT DYRLYIELLR NLADEAGLPK 

       130        140        150        160        170        180 
TLDTGSLAGI KTHEYCTNNQ PNNHSDHVDP YPYLAKWGIS REQFKHDIEN GLTIETGWQK 

       190        200        210        220        230        240 
NDTGYWYVHS DGSYPKDKFE KINGTWYYFD SSGYMLADRW RKHTDGNWYW FDNSGEMATG 

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

       310 
LADKPEFTVE PDGLITVK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coli."
Garcia P., Garcia J.L., Garcia E., Lopez R.
Gene 43:265-272(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Martin B.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: R800.
[3]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13812 Genomic DNA. Translation: AAA26917.1.
Z34303 Genomic DNA. Translation: CAA84074.1.
AE005672 Genomic DNA. Translation: AAK76005.1.
PIRA25634.
D95226.
H98090.
RefSeqNP_346365.1. NC_003028.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVMX-ray2.80A/B/C/D/E/F188-318[»]
1H8GX-ray2.40A/B224-318[»]
1HCXX-ray2.60A/B192-318[»]
2BMLX-ray2.60A/B193-318[»]
4IVVX-ray1.05A1-180[»]
ProteinModelPortalP06653.
SMRP06653. Positions 188-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING170187.SP_1937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK76005; AAK76005; SP_1937.
GeneID931994.
KEGGspn:SP_1937.
PATRIC19708391. VBIStrPne105772_2017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5263.
HOGENOMHOG000284833.
KOK01447.
OrthoDBEOG6FBWV3.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-1967-MONOMER.

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...

Other

EvolutionaryTraceP06653.

Entry information

Entry nameALYS_STRPN
AccessionPrimary (citable) accession number: P06653
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: September 26, 2001
Last modified: May 14, 2014
This is version 117 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references