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P14892 (CWLA_BACSP) 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:
N-acetylmuramoyl-L-alanine amidase CwlA

EC=3.5.1.28
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene names
Name:cwlA
OrganismBacillus sp.
Taxonomic identifier1409 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Catalytic activity

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

Subcellular location

Secreted Potential.

Miscellaneous

Retention of enzymatic activity was limited to the N-terminal fragment (AA 1-196).

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737
Chain38 – 251214N-acetylmuramoyl-L-alanine amidase CwlA
PRO_0000006452

Sequences

Sequence LengthMass (Da)Tools
P14892 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1F52F36B20576F0D

FASTA25128,473
        10         20         30         40         50         60 
MEIKQMLVPV SRYSVLCPYE MNPTEITFHN TYNDAPAINE RNNVANNSTG TSFHIAVDDK 

        70         80         90        100        110        120 
EAIQLIPFNR NAWHAGDGTN GRGNRHSIGV EICYSQSGGA RYRKAELNAV EVIAQLMIQF 

       130        140        150        160        170        180 
DIPISKVKTH QERNGKYCPH RMLDEGRVQW FKNQCANRAS SIKNSNKTQE TGKVEIIVNK 

       190        200        210        220        230        240 
FNKVVTYEFG TALVPEMLGM MDALGYESRI ISYGDKQGLV RFETAYRQGN ELDKATAWLD 

       250 
AKGLKYFYTK E 

« Hide

References

[1]"Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli."
Potvin C., Leclerc D., Tremblay G., Asselin A., Bellemare G.
Mol. Gen. Genet. 214:241-248(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13524 Genomic DNA. Translation: CAA31877.1.
PIRS08306.

3D structure databases

ProteinModelPortalP14892.
SMRP14892. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR021976. Amidase02_C.
IPR002502. Amidase_domain.
[Graphical view]
PfamPF12123. Amidase02_C. 1 hit.
PF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCWLA_BACSP
AccessionPrimary (citable) accession number: P14892
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
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 programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families