P85045 (LYS_BUFGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lysozyme C EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C
Organism	Bufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
Taxonomic identifier	61428 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Bufonidae › Bufo › Bufo gargarizans

Protein attributes

Sequence length	146 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to Gram-negative bacterium Inferred from direct assay Ref.1. Source: UniProtKB defense response to Gram-positive bacterium Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	lysozyme activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	‹1 – 16	›16	Ref.1
	Chain	17 – 146	130	Lysozyme C Ref.1		PRO_0000271190
Sites
	Active site	51	1	By similarity UniProtKB P00702
	Active site	69	1	By similarity UniProtKB P00702
Amino acid modifications
	Disulfide bond	22 ↔ 144		By similarity UniProtKB P00702
	Disulfide bond	46 ↔ 132		By similarity UniProtKB P00702
	Disulfide bond	81 ↔ 97		By similarity UniProtKB P00702
	Disulfide bond	93 ↔ 111		By similarity UniProtKB P00702
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P85045 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 126AA86ED3D01EBB	FASTA	146	16,608
	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

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
ProteinModelPortal	P85045.
SMR	P85045. Positions 19-146.
ModBase	Search...
Proteomic databases
PRIDE	P85045.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG052297.
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. IPR023346. Lysozyme-like_dom. [Graphical view]
Pfam	PF00062. Lys. 1 hit. [Graphical view]
PRINTS	PR00137. LYSOZYME. PR00135. LYZLACT.
SMART	SM00263. LYZ1. 1 hit. [Graphical view]
SUPFAM	SSF53955. SSF53955. 1 hit.
PROSITE	PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS_BUFGA

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program