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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. cell wall organization Source: UniProtKB-KW
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. establishment of competence for transformation Source: UniProtKB-KW
  5. peptidoglycan catabolic process Source: InterPro
  6. 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 Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Add
BLAST
Chaini38 – 251214N-acetylmuramoyl-L-alanine amidase CwlAPRO_0000006452Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14892.
SMRiP14892. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

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

« Hide

        10         20         30         40         50
MEIKQMLVPV SRYSVLCPYE MNPTEITFHN TYNDAPAINE RNNVANNSTG
60 70 80 90 100
TSFHIAVDDK EAIQLIPFNR NAWHAGDGTN GRGNRHSIGV EICYSQSGGA
110 120 130 140 150
RYRKAELNAV EVIAQLMIQF DIPISKVKTH QERNGKYCPH RMLDEGRVQW
160 170 180 190 200
FKNQCANRAS SIKNSNKTQE TGKVEIIVNK FNKVVTYEFG TALVPEMLGM
210 220 230 240 250
MDALGYESRI ISYGDKQGLV RFETAYRQGN ELDKATAWLD AKGLKYFYTK

E
Length:251
Mass (Da):28,473
Last modified:April 1, 1990 - v1
Checksum:i1F52F36B20576F0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13524 Genomic DNA. Translation: CAA31877.1.
PIRiS08306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 67 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