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P00702

- LYSC_PHACO

UniProt

P00702 - LYSC_PHACO

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Protein

Lysozyme C

Gene
LYZ
Organism
Phasianus colchicus colchicus (Ring-necked pheasant)
Status
Reviewed - Annotation score: 5 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 sitei53 – 531
Active sitei70 – 701

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

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
Gene namesi
Name:LYZ
OrganismiPhasianus colchicus colchicus (Ring-necked pheasant)
Taxonomic identifieri9057 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaePhasianus

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
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 147130Lysozyme CPRO_0000018499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 145
Disulfide bondi48 ↔ 133
Disulfide bondi82 ↔ 98
Disulfide bondi94 ↔ 112

Post-translational modificationi

By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds.

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00702.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210
Helixi43 – 5412
Beta strandi55 – 573
Beta strandi61 – 633
Beta strandi69 – 713
Turni72 – 754
Turni78 – 803
Beta strandi85 – 873
Helixi98 – 1025
Beta strandi103 – 1053
Helixi107 – 11711
Turni118 – 1214
Helixi122 – 1254
Helixi127 – 1326
Turni133 – 1353
Helixi138 – 1425

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHLX-ray2.10A/B18-147[»]
1JHLX-ray2.40A19-147[»]
ProteinModelPortaliP00702.
SMRiP00702. Positions 18-147.

Miscellaneous databases

EvolutionaryTraceiP00702.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00702-1 [UniParc]FASTAAdd to Basket

« Hide

MRSLLILVLC FLPLAAPGKV YGRCELAAAM KRMGLDNYRG YSLGNWVCAA    50
KFESNFNTGA TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCHIPCSA 100
LLSSDITASV NCAKKIVSDG NGMNAWVAWR KHCKGTDVNV WIRGCRL 147
Length:147
Mass (Da):16,166
Last modified:June 1, 1994 - v2
Checksum:i7A0EF8CCFD6B8249
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GHL X-ray 2.10 A/B 18-147 [» ]
1JHL X-ray 2.40 A 19-147 [» ]
ProteinModelPortali P00702.
SMRi P00702. Positions 18-147.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P00702.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

Miscellaneous databases

EvolutionaryTracei P00702.

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. "Evolutionary shift in the site of cleavage of prelysozyme."
    Weisman L.S., Krummel B.M., Wilson A.C.
    J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18.
  2. "Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozyme."
    Jolles J., Ibrahimi I.M., Prager E.M., Schoentgen F., Jolles P., Wilson A.C.
    Biochemistry 18:2744-2752(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-147.
  3. "Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex."
    Chitarra V., Alzari P.M., Bentley G.A., Bhat T.N., Eisele J.L., Houdusse A., Lescar J., Souchon H., Poljak R.J.
    Proc. Natl. Acad. Sci. U.S.A. 90:7711-7715(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  4. "Crystal structures of pheasant and guinea fowl egg-white lysozymes."
    Lescar J., Souchon H., Alzari P.M.
    Protein Sci. 3:788-798(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 121.

Entry informationi

Entry nameiLYSC_PHACO
AccessioniPrimary (citable) accession number: P00702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 83 of the entry and version 2 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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