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Reviewed, UniProtKB/Swiss-Prot P84492 (LYSC_CHEMY)

Last modified June 16, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
Gene names
Name: LYZ
OrganismChelonia mydas (Green sea-turtle) (Chelonia agassizi)
Taxonomic identifier8469 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudinesCryptodiraChelonioideaCheloniidaeChelonia

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

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.

Subunit structure

Monomer By similarity.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Lysozyme C
PRO_0000247815

Sites

Active site351 By similarity
Active site531 By similarity

Amino acid modifications

Disulfide bond6 ↔ 128 By similarity
Disulfide bond30 ↔ 116 By similarity
Disulfide bond65 ↔ 81 By similarity
Disulfide bond77 ↔ 95 By similarity

Sequences

Sequence LengthMass (Da)Tools
P84492-1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 4CBB271A77565168

FASTA13014,704
        10         20         30         40         50         60 
KTYERCELAR AMKRLGLDGY WGYSLGHWVC AAKYESNFNT GATNYNPGDQ STDYGILQIN 

        70         80         90        100        110        120 
SRWWCNDGKT PRTKNACKIQ CRELLTADIT ASVNCAKRVV RDPNGMGAWV AWTKNCKGRD 

       130 
VSPWIRDCGL 

« Hide

References

[1]Araki T., Chijiiwa Y., Okabayashi K., Kawase M., Kamesaki M., Torikata T.
Submitted (MAR-2003) to the PIR data bank
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRJC7918.

3D structure databases

SMRP84492. Positions 1-130.
ModBaseSearch...

Phylogenomic databases

HOVERGENP84492.

Enzyme and pathway databases

BRENDA3.2.1.17. 293409.

Family and domain databases

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

Entry information

Entry nameLYSC_CHEMY
AccessionPrimary (citable) accession number: P84492
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 29, 2005
Last modified: June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents