Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P85045 (LYS_BUFGA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 6, 2013. Version 24. 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:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismBufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
Taxonomic identifier61428 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeBufo

Protein attributes

Sequence length146 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram-positive bacterium S.aureus and against the Gram-negative bacterium E.coli with a MIC of 1 µM and 8 µM respectively. No antifungal activity against C.albicans. Ref.1

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. Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the skin glands. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.1

Temperature dependence:

Stable from 20 degrees Celsius to 70 degrees Celsius. Activity decreases sharply above 70 degrees Celsius. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 16›16 Ref.1
Chain17 – 146130Lysozyme C Ref.1
PRO_0000271190

Sites

Active site511 By similarity UniProtKB P00702
Active site691 By similarity UniProtKB P00702

Amino acid modifications

Disulfide bond22 ↔ 144 By similarity UniProtKB P00702
Disulfide bond46 ↔ 132 By similarity UniProtKB P00702
Disulfide bond81 ↔ 97 By similarity UniProtKB P00702
Disulfide bond93 ↔ 111 By similarity UniProtKB P00702

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P85045 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 126AA86ED3D01EBB

FASTA14616,608
        10         20         30         40         50         60 
SGKYISWEDS CSYLQLQKYE RCELAKALKK GGLADFKGYS LENWICTAFH ESGYNTASTN 

        70         80         90        100        110        120 
YNPPDKSTDY GIFQINSRWW CNDYKTPRSK NTCNIDCKVL LGDDISPAIK CAKRVVSDPN 

       130        140 
GMGAWVAWKK YCKGKNLSQW TQGCKL 

« Hide

References

[1]"Purification of a lysozyme from skin secretions of Bufo andrewsi."
Zhao Y., Jin Y., Lee W.-H., Zhang Y.
Comp. Biochem. Physiol. 142C:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Skin secretion.

Cross-references

3D structure databases

ProteinModelPortalP85045.
SMRP85045. Positions 19-146.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP85045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS_BUFGA
AccessionPrimary (citable) accession number: P85045
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: February 6, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries