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Protein

Lysozyme B

Gene

LysB

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food.

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 sitei68 – 681PROSITE-ProRule annotation

GO - Molecular functioni

  • lysozyme activity Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_359416. Lactose synthesis.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme B (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase B
Gene namesi
Name:LysB
ORF Names:CG1179
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004425. LysB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 140122Lysozyme BPRO_0000018510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 139PROSITE-ProRule annotation
Disulfide bondi45 ↔ 129PROSITE-ProRule annotation
Disulfide bondi80 ↔ 96PROSITE-ProRule annotation
Disulfide bondi92 ↔ 110PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ08694.

Expressioni

Tissue specificityi

Found in the midgut.

Developmental stagei

Maximal expression is found during the third larval instar, it drops to become undetectable in the late pupal stage. The expression in adults is similar to that of first and second larval instars.

Gene expression databases

BgeeiQ08694.

Interactioni

Protein-protein interaction databases

BioGridi63671. 2 interactions.
DIPiDIP-20169N.
MINTiMINT-822799.
STRINGi7227.FBpp0072524.

Structurei

3D structure databases

ProteinModelPortaliQ08694.
SMRiQ08694. Positions 19-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255922.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000263866.
InParanoidiQ08694.
KOiK01185.
OMAiTYERCEF.
OrthoDBiEOG7BW0M5.
PhylomeDBiQ08694.

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.

Q08694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAFIVLVAL ALAAPALGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE
60 70 80 90 100
SSYRTGVVGP ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL
110 120 130 140
TDDITHSVRC AQKVLSQQGW SAWSTWHYCS GWLPSIDDCF
Length:140
Mass (Da):15,612
Last modified:February 21, 2001 - v2
Checksum:i70AFA5321857F093
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 132LA → SG in CAA80227 (PubMed:8159165).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22225 Genomic DNA. Translation: CAA80227.1.
AE014296 Genomic DNA. Translation: AAF47448.1.
PIRiS41574.
RefSeqiNP_001261245.1. NM_001274316.1.
NP_523882.1. NM_079158.3.
UniGeneiDm.23958.

Genome annotation databases

EnsemblMetazoaiFBtr0072628; FBpp0072524; FBgn0004425.
FBtr0336738; FBpp0307718; FBgn0004425.
GeneIDi38125.
KEGGidme:Dmel_CG1179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22225 Genomic DNA. Translation: CAA80227.1.
AE014296 Genomic DNA. Translation: AAF47448.1.
PIRiS41574.
RefSeqiNP_001261245.1. NM_001274316.1.
NP_523882.1. NM_079158.3.
UniGeneiDm.23958.

3D structure databases

ProteinModelPortaliQ08694.
SMRiQ08694. Positions 19-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63671. 2 interactions.
DIPiDIP-20169N.
MINTiMINT-822799.
STRINGi7227.FBpp0072524.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PaxDbiQ08694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072628; FBpp0072524; FBgn0004425.
FBtr0336738; FBpp0307718; FBgn0004425.
GeneIDi38125.
KEGGidme:Dmel_CG1179.

Organism-specific databases

CTDi38125.
FlyBaseiFBgn0004425. LysB.

Phylogenomic databases

eggNOGiNOG255922.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000263866.
InParanoidiQ08694.
KOiK01185.
OMAiTYERCEF.
OrthoDBiEOG7BW0M5.
PhylomeDBiQ08694.

Enzyme and pathway databases

ReactomeiREACT_359416. Lactose synthesis.

Miscellaneous databases

GenomeRNAii38125.
NextBioi807090.
PROiQ08694.

Gene expression databases

BgeeiQ08694.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract."
    Daffre S., Kylsten P., Samakovlis C., Hultmark D.
    Mol. Gen. Genet. 242:152-162(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiLYSB_DROME
AccessioniPrimary (citable) accession number: Q08694
Secondary accession number(s): P37158, Q9W0J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 21, 2001
Last modified: July 22, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.