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Protein

Lysozyme C

Gene
N/A
Organism
Bufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 PublicationPROSITE-ProRule annotation

Catalytic activityi

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.1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511By similarityPROSITE-ProRule annotation
Active sitei69 – 691By similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to Gram-negative bacterium Source: UniProtKB
  3. defense response to Gram-positive bacterium Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiBufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
Taxonomic identifieri61428 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeBufo

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 16›161 PublicationAdd
BLAST
Chaini17 – 146130Lysozyme C1 PublicationPRO_0000271190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 144By similarityPROSITE-ProRule annotation
Disulfide bondi46 ↔ 132By similarityPROSITE-ProRule annotation
Disulfide bondi81 ↔ 97By similarityPROSITE-ProRule annotation
Disulfide bondi93 ↔ 111By similarityPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP85045.

Expressioni

Tissue specificityi

Expressed by the skin glands.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP85045.
SMRiP85045. Positions 19-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P85045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SGKYISWEDS CSYLQLQKYE RCELAKALKK GGLADFKGYS LENWICTAFH
60 70 80 90 100
ESGYNTASTN YNPPDKSTDY GIFQINSRWW CNDYKTPRSK NTCNIDCKVL
110 120 130 140
LGDDISPAIK CAKRVVSDPN GMGAWVAWKK YCKGKNLSQW TQGCKL
Length:146
Mass (Da):16,608
Last modified:January 9, 2007 - v1
Checksum:i126AA86ED3D01EBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 111 Publication

Cross-referencesi

3D structure databases

ProteinModelPortaliP85045.
SMRiP85045. Positions 19-146.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP85045.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 secretion1 Publication.

Entry informationi

Entry nameiLYS_BUFGA
AccessioniPrimary (citable) accession number: P85045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: March 4, 2015
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.