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P37712

- LYSC_CAMDR

UniProt

P37712 - LYSC_CAMDR

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Protein
Lysozyme C
Gene
LYZ
Organism
Camelus dromedarius (Dromedary) (Arabian camel)
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.

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 By similarity
Active sitei53 – 531 By 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. digestion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Biological processi

Digestion

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
Gene namesi
Name:LYZ
OrganismiCamelus dromedarius (Dromedary) (Arabian camel)
Taxonomic identifieri9838 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaTylopodaCamelidaeCamelus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Lysozyme C
PRO_0000208844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 128 By similarity
Disulfide bondi30 ↔ 116 By similarity
Disulfide bondi65 ↔ 81 By similarity
Disulfide bondi77 ↔ 95 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP37712.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP37712.

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.

P37712-1 [UniParc]FASTAAdd to Basket

« Hide

KVWERCALAR KLKELGMDGY RGVSLANWMC LTKWESDYNT DATNYNPSSE    50
STDYGIFQIN SRYWCNNGKT PHAVNGCGIN CNVLLEDDIT KAVQCAKRVV 100
RDPQGVRAWV AWKNHCEGHD VEQYVEGCDL 130
Length:130
Mass (Da):14,795
Last modified:October 1, 1994 - v1
Checksum:i6CFFCB41B02FD287
GO

Cross-referencesi

3D structure databases

ProteinModelPortali P37712.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P37712.

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. "Amino acid sequences of stomach and nonstomach lysozymes of ruminants."
    Jolles J., Prager E.M., Alnemri E.S., Jolles P., Ibrahimi I.M., Wilson A.C.
    J. Mol. Evol. 30:370-382(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Stomach.
  2. Erratum
    Jolles J., Prager E.M., Alnemri E.S., Jolles P., Ibrahimi I.M., Wilson A.C.
    J. Mol. Evol. 30:563-563(1990)

Entry informationi

Entry nameiLYSC_CAMDR
AccessioniPrimary (citable) accession number: P37712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 61 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

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

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