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Protein

Lysozyme

Gene
N/A
Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: 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. Active against E.coli and M.luteus.PROSITE-ProRule annotation1 Publication

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 sitei50 – 501PROSITE-ProRule annotation
Active sitei67 – 671PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
Proteomesi
  • UP000005204 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 137119LysozymePRO_0000018505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 137PROSITE-ProRule annotation
Disulfide bondi45 ↔ 127PROSITE-ProRule annotation
Disulfide bondi79 ↔ 93PROSITE-ProRule annotation
Disulfide bondi89 ↔ 107PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Developmental stagei

Expressed within 6 hours after induction, reaches maximum levels after 48 hours and declines after 72 hours after induction.

Inductioni

By bacterial infection.

Interactioni

Protein-protein interaction databases

STRINGi7091.BGIBMGA010439-TA.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210Combined sources
Helixi37 – 393Combined sources
Helixi40 – 5011Combined sources
Turni51 – 533Combined sources
Beta strandi58 – 603Combined sources
Beta strandi66 – 683Combined sources
Turni69 – 724Combined sources
Turni75 – 784Combined sources
Beta strandi80 – 845Combined sources
Turni87 – 904Combined sources
Helixi93 – 964Combined sources
Beta strandi97 – 993Combined sources
Helixi102 – 11514Combined sources
Helixi116 – 1194Combined sources
Helixi121 – 1244Combined sources
Beta strandi127 – 1293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GD6X-ray2.50A19-137[»]
2RSCNMR-A19-137[»]
ProteinModelPortaliP48816.
SMRiP48816. Positions 19-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48816.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
InParanoidiP48816.
KOiK13915.
OMAiHGYRAWY.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
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.

P48816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKLIIFALV VLCVGSEAKT FTRCGLVHEL RKHGFEENLM RNWVCLVEHE
60 70 80 90 100
SSRDTSKTNT NRNGSKDYGL FQINDRYWCS KGASPGKDCN VKCSDLLTDD
110 120 130
ITKAAKCAKK IYKRHRFDAW YGWKNHCQGS LPDISSC
Length:137
Mass (Da):15,668
Last modified:February 1, 1996 - v1
Checksum:iFFE5710506C61A1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37416 mRNA. Translation: AAB40947.1.
PIRiJC4233.
RefSeqiNP_001037448.1. NM_001043983.1.
UniGeneiBmo.2011.
Bmo.2379.

Genome annotation databases

EnsemblMetazoaiBGIBMGA010439-RA; BGIBMGA010439-TA; BGIBMGA010439.
GeneIDi693015.
KEGGibmor:693015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37416 mRNA. Translation: AAB40947.1.
PIRiJC4233.
RefSeqiNP_001037448.1. NM_001043983.1.
UniGeneiBmo.2011.
Bmo.2379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GD6X-ray2.50A19-137[»]
2RSCNMR-A19-137[»]
ProteinModelPortaliP48816.
SMRiP48816. Positions 19-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7091.BGIBMGA010439-TA.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiBGIBMGA010439-RA; BGIBMGA010439-TA; BGIBMGA010439.
GeneIDi693015.
KEGGibmor:693015.

Organism-specific databases

CTDi693015.

Phylogenomic databases

eggNOGiENOG410IXGD. Eukaryota.
ENOG4111QHM. LUCA.
InParanoidiP48816.
KOiK13915.
OMAiHGYRAWY.

Miscellaneous databases

EvolutionaryTraceiP48816.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiLYS_BOMMO
AccessioniPrimary (citable) accession number: P48816
Secondary accession number(s): Q9TWL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 7, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.