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P14892

- CWLA_BACSP

UniProt

P14892 - CWLA_BACSP

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Protein
N-acetylmuramoyl-L-alanine amidase CwlA
Gene
cwlA
Organism
Bacillus sp.
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. establishment of competence for transformation Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
  5. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Competence, Sporulation

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase CwlA (EC:3.5.1.28)
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene namesi
Name:cwlA
OrganismiBacillus sp.
Taxonomic identifieri1409 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

Secreted Reviewed prediction

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737
Add
BLAST
Chaini38 – 251214N-acetylmuramoyl-L-alanine amidase CwlA
PRO_0000006452Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14892.
SMRiP14892. Positions 1-147.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR021976. Amidase02_C.
IPR002502. Amidase_domain.
[Graphical view]
PfamiPF12123. Amidase02_C. 1 hit.
PF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14892-1 [UniParc]FASTAAdd to Basket

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MEIKQMLVPV SRYSVLCPYE MNPTEITFHN TYNDAPAINE RNNVANNSTG    50
TSFHIAVDDK EAIQLIPFNR NAWHAGDGTN GRGNRHSIGV EICYSQSGGA 100
RYRKAELNAV EVIAQLMIQF DIPISKVKTH QERNGKYCPH RMLDEGRVQW 150
FKNQCANRAS SIKNSNKTQE TGKVEIIVNK FNKVVTYEFG TALVPEMLGM 200
MDALGYESRI ISYGDKQGLV RFETAYRQGN ELDKATAWLD AKGLKYFYTK 250
E 251
Length:251
Mass (Da):28,473
Last modified:April 1, 1990 - v1
Checksum:i1F52F36B20576F0D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13524 Genomic DNA. Translation: CAA31877.1.
PIRiS08306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13524 Genomic DNA. Translation: CAA31877.1 .
PIRi S08306.

3D structure databases

ProteinModelPortali P14892.
SMRi P14892. Positions 1-147.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR021976. Amidase02_C.
IPR002502. Amidase_domain.
[Graphical view ]
Pfami PF12123. Amidase02_C. 1 hit.
PF01510. Amidase_2. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiCWLA_BACSP
AccessioniPrimary (citable) accession number: P14892
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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