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P0C2T5 (ACMA_LACLC) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable N-acetylmuramidase
EC=3.2.1.17
Alternative name(s):
Autolysin
Lysozyme
Peptidoglycan hydrolase
Gene names
Name:acmA
OrganismLactococcus lactis subsp. cremoris (Streptococcus cremoris)
Taxonomic identifier1359 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes the cell wall of L.lactis and M.lysodeikticus. Required for cell separation during growth.

Catalytic activity

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Subcellular location

Secreted By similarity.

Domain

The LysM repeats are thought to be involved in peptidoglycan binding.

Sequence similarities

Belongs to the glycosyl hydrolase 73 family.

Contains 3 LysM repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757 Potential
Chain58 – 437380Probable N-acetylmuramidase
PRO_0000012113

Regions

Repeat245 – 28743LysM 1
Repeat321 – 36343LysM 2
Repeat395 – 43743LysM 3

Sequences

Sequence LengthMass (Da)Tools
P0C2T5 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 169778AF09E13963

FASTA43746,597
        10         20         30         40         50         60 
MPVSRVKVKN RHLKKKTKKP LAFYKPTTKF VGAVLIAGTL TTTHELLLQQ TSPMVQAATN 

        70         80         90        100        110        120 
SSEAFIESIA ASAKPVADAN GLYPSVMIAQ AILESNWGSS QLSRAPYYNL FGIQGTYQGK 

       130        140        150        160        170        180 
SVVFKTQEYL NGKWVTKDMP FRVYPSFNQS FQDNTYVLKT TNFGNGPYYA KAWRANAATY 

       190        200        210        220        230        240 
QDATAALTGK YATDPSYGAS LNRIISQYNL TRFDGASSAG NTNSGGSTTT NTNNNSGTNS 

       250        260        270        280        290        300 
SSTTYTVKSG DTLWGISQRY GISVAQIQSA NNLKSTIIYI GQKLLLTGSA SSTNSGGSNN 

       310        320        330        340        350        360 
SASTTPTTSV TPAKPASQTS VKVKSGDTLW ALSVKYKTSI AQLKSWNHLS SDTIYIGQNL 

       370        380        390        400        410        420 
IVSQSAATSN PSTGSGSTAT NNSNSTSSNS NASIHKVVKG DTLWGLSQKS GSPIASIKAW 

       430 
NHLSSDTILI GQYLRIK

« Hide

References

[1]"Varying influence of the autolysin, N-acetyl muramidase, and the cell envelope proteinase on the rate of autolysis of six commercial Lactococcus lactis cheese starter bacteria grown in milk."
Govindasamy-Lucey S., Gopal P.K., Sullivan P.A., Pillidge C.J.
J. Dairy Res. 67:585-596(2000) [PubMed: 11131071] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 2250.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF036720 Genomic DNA. Translation: AAB93629.1.

3D structure databases

ProteinModelPortalP0C2T5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013338. Lysozyme_dom_subfam2.
IPR002901. Mano_Glyc_endo_b_GlcNAc.
IPR018392. Peptidoglycan-bd_lysin.
IPR002482. Peptidoglycan-bd_Lysin_subgr.
[Graphical view]
PfamPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 3 hits.
[Graphical view]
SMARTSM00257. LysM. 3 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACMA_LACLC
AccessionPrimary (citable) accession number: P0C2T5
Secondary accession number(s): O52362, Q48603
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: September 21, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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