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P85345

- LYSC_AMYCA

UniProt

P85345 - LYSC_AMYCA

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Protein

Lysozyme C

Gene

LYZ

Organism
Amyda cartilaginea (Asiatic softshell turtle)
Status
Reviewed - Annotation score: 3 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.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

Optimum temperature is 40 degrees Celsius. Retains the bulk of its activity after incubation for 1 hour at 90 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351By similarityPROSITE-ProRule annotation
Active sitei53 – 531By similarityPROSITE-ProRule annotation

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

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Asiatic softshell turtle lysozyme C
Short name:
ASTL
Gene namesi
Name:LYZBy similarity
OrganismiAmyda cartilaginea (Asiatic softshell turtle)
Taxonomic identifieri161655 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesCryptodiraTrionychoideaTrionychidaeAmyda

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Lysozyme CPRO_0000315890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 128By similarityPROSITE-ProRule annotation
Disulfide bondi30 ↔ 116By similarityPROSITE-ProRule annotation
Disulfide bondi65 ↔ 81By similarityPROSITE-ProRule annotation
Disulfide bondi77 ↔ 95By similarityPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP85345.
SMRiP85345. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

P85345-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
KIYEQCEAAR EMKRLGLDGY DGYSLGDWVC TAKHESNFNT GATNYNRGDQ
60 70 80 90 100
STDYGIFQIN SRWWCNDGKT PNAKNACGIE CSELLKADIT AAVICAKRVV
110 120 130
RDPNGMGAWV AWTKYCKGKD VSQWIKGCKL
Length:130
Mass (Da):14,543
Last modified:January 15, 2008 - v1
Checksum:iF6760A314D34FF91
GO

Cross-referencesi

3D structure databases

ProteinModelPortali P85345.
SMRi P85345. Positions 1-130.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

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. Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Egg white.

Entry informationi

Entry nameiLYSC_AMYCA
AccessioniPrimary (citable) accession number: P85345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 23 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.Curated

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