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Protein

Lysozyme g

Gene
N/A
Organism
Struthio camelus (Ostrich)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has bacteriolytic activity against M.luteus.1 Publication

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921By similarity
Active sitei105 – 1051By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme g (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
Goose-type lysozyme
OrganismiStruthio camelus (Ostrich)
Taxonomic identifieri8801 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeStruthioniformesStruthionidaeStruthio

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 204185Lysozyme gPRO_0000193516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 79By similarity
Disulfide bondi37 ↔ 48By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Helixi27 – 293Combined sources
Helixi37 – 404Combined sources
Helixi41 – 433Combined sources
Helixi50 – 6516Combined sources
Helixi68 – 7811Combined sources
Helixi82 – 9312Combined sources
Turni94 – 985Combined sources
Turni105 – 1084Combined sources
Turni111 – 1144Combined sources
Turni117 – 1193Combined sources
Helixi129 – 14921Combined sources
Helixi155 – 16814Combined sources
Helixi170 – 1723Combined sources
Turni177 – 1826Combined sources
Helixi184 – 1863Combined sources
Helixi188 – 19912Combined sources
Turni200 – 2034Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WYHX-ray1.77A/B20-204[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 23 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P00719-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHLMLVLLGL AALLGTSQSR TGCYGDVNRV DTTGASCKSA KPEKLNYCGV
60 70 80 90 100
AASRKIAERD LQSMDRYKAL IKKVGQKLCV DPAVIAGIIS RESHAGKALR
110 120 130 140 150
NGWGDNGNGF GLMQVDRRSH KPVGEWNGER HLMQGTEILI SMIKAIQKKF
160 170 180 190 200
PRWTKEQQLK GGISAYNAGP GNVRSYERMD IGTTHDDYAN DVVARAQYYK

QHGY
Length:204
Mass (Da):22,514
Last modified:September 5, 2012 - v2
Checksum:iDD9F02D65DA21A65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB469329 Genomic DNA. Translation: BAL03620.1.
PIRiA00874. LZOSG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB469329 Genomic DNA. Translation: BAL03620.1.
PIRiA00874. LZOSG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WYHX-ray1.77A/B20-204[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white."
    Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.
    Gene 492:244-249(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Tissue: Muscle.
  2. "Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme."
    Schoentgen F., Jolles J., Jolles P.
    Eur. J. Biochem. 123:489-497(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-204.
    Tissue: Egg white.
  3. "The ostrich (Struthio camelus) egg-white lysozyme."
    Jolles J., Perin J.-P., Jolles P.
    Mol. Cell. Biochem. 17:39-44(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-53.
    Tissue: Egg white.

Entry informationi

Entry nameiLYG_STRCA
AccessioniPrimary (citable) accession number: P00719
Secondary accession number(s): G3XDE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 5, 2012
Last modified: February 4, 2015
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.