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Protein

Lysozyme C

Gene

LYZ

Organism
Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
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 strong bacteriolytic activity against M.luteus and V.cholerae, weak bacteriolytic activity against P.aeruginosa and no activity against A.hydrophila.PROSITE-ProRule annotation1 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.1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Activity rapidly decreases within 30 minutes of incubation at 90 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei36PROSITE-ProRule annotation1
Active sitei54PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.17. 6494.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Softshell turtle lysozyme C
Short name:
SSTL
Gene namesi
Name:LYZ
OrganismiPelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
Taxonomic identifieri13735 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaTestudinesCryptodiraTrionychiaTrionychidaePelodiscus
Proteomesi
  • UP000007267 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002088761 – 131Lysozyme CAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi7 ↔ 129
Disulfide bondi31 ↔ 117
Disulfide bondi66 ↔ 82
Disulfide bondi78 ↔ 96

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi13735.ENSPSIP00000018209.

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Helixi21 – 23Combined sources3
Helixi26 – 37Combined sources12
Beta strandi44 – 47Combined sources4
Turni48 – 51Combined sources4
Beta strandi52 – 55Combined sources4
Turni56 – 59Combined sources4
Turni62 – 65Combined sources4
Helixi82 – 86Combined sources5
Helixi91 – 102Combined sources12
Helixi106 – 109Combined sources4
Helixi111 – 116Combined sources6
Turni117 – 119Combined sources3
Helixi123 – 125Combined sources3
Turni126 – 128Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GV0X-ray1.90A1-131[»]
ProteinModelPortaliQ7LZQ1.
SMRiQ7LZQ1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7LZQ1.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
HOVERGENiHBG052297.
OrthoDBiEOG091G0R9V.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
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: Complete.

Q7LZQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GKIYEQCELA REFKRHGMDG YHGYSLGDWV CTAKHESNFN TAATNYNRGD
60 70 80 90 100
QSTDYGILQI NSRWWCNDGK TPKAKNACGI ECSELLKADI TAAVNCAKRI
110 120 130
VRDPNGMGAW VAWTKYCKGK DVSQWIKGCK L
Length:131
Mass (Da):14,732
Last modified:September 22, 2009 - v3
Checksum:iD59A7791775E6AA1
GO

Sequence databases

PIRiJC5493.

Cross-referencesi

Sequence databases

PIRiJC5493.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GV0X-ray1.90A1-131[»]
ProteinModelPortaliQ7LZQ1.
SMRiQ7LZQ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi13735.ENSPSIP00000018209.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
HOVERGENiHBG052297.
OrthoDBiEOG091G0R9V.

Enzyme and pathway databases

BRENDAi3.2.1.17. 6494.

Miscellaneous databases

EvolutionaryTraceiQ7LZQ1.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
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...

Entry informationi

Entry nameiLYSC_PELSI
AccessioniPrimary (citable) accession number: Q7LZQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: September 22, 2009
Last modified: November 2, 2016
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

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 one 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.