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P37156

- LYSC1_TACAC

UniProt

P37156 - LYSC1_TACAC

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Protein

Lysozyme C I

Gene
N/A
Organism
Tachyglossus aculeatus aculeatus (Australian echidna)
Status
Reviewed - 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.

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 sitei35 – 351
Active sitei52 – 521

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
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C I (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismiTachyglossus aculeatus aculeatus (Australian echidna)
Taxonomic identifieri49271 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMonotremataTachyglossidaeTachyglossus

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
Chaini1 – 125125Lysozyme C IPRO_0000208857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi9 ↔ 125
Disulfide bondi30 ↔ 115
Disulfide bondi64 ↔ 80
Disulfide bondi76 ↔ 94

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410
Helixi25 – 3612
Beta strandi43 – 453
Beta strandi51 – 533
Turni54 – 574
Turni60 – 634
Helixi80 – 834
Beta strandi84 – 863
Helixi89 – 10214
Helixi109 – 1146
Turni115 – 1173
Helixi121 – 1233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JUGX-ray1.90A1-125[»]
ProteinModelPortaliP37156.
SMRiP37156. Positions 1-125.

Miscellaneous databases

EvolutionaryTraceiP37156.

Family & Domainsi

Sequence similaritiesi

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.
[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.

P37156-1 [UniParc]FASTAAdd to Basket

« Hide

KILKKQELCK NLVAQGMNGY QHITLPNWVC TAFHESSYNT RATNHNTDGS    50
TDYGILQINS RYWCHDGKTP GSKNACNISC SKLLDDDITD DLKCAKKIAG 100
EAKGLTPWVA WKSKCRGHDL SKFKC 125
Length:125
Mass (Da):13,994
Last modified:October 1, 1994 - v1
Checksum:i18D8A1DBA3724073
GO

Sequence databases

PIRiA45660.

Cross-referencesi

Sequence databases

PIRi A45660.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JUG X-ray 1.90 A 1-125 [» ]
ProteinModelPortali P37156.
SMRi P37156. Positions 1-125.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

Miscellaneous databases

EvolutionaryTracei P37156.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The isolation and amino acid sequences of echidna (Tachyglossus aculeatus) milk lysozyme I and II."
    Teahan C.G., McKenzie H.A., Shaw D.C., Griffiths M.
    Biochem. Int. 24:85-95(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Milk.
  2. "Structure of the calcium-binding Echidna milk lysozyme at 1.9-A resolution."
    Guss J.M., Messer M., Costello M., Hardy K., Kumar V.
    Acta Crystallogr. D 53:355-363(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiLYSC1_TACAC
AccessioniPrimary (citable) accession number: P37156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 70 of the entry and version 1 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, 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

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