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P61627

- LYSC_PANPA

UniProt

P61627 - LYSC_PANPA

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Protein
Lysozyme C
Gene
LYZ, LZM
Organism
Pan paniscus (Pygmy chimpanzee) (Bonobo)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity
Active sitei71 – 711 By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC
Complete GO annotation...

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
Synonyms:LZM
OrganismiPan paniscus (Pygmy chimpanzee) (Bonobo)
Taxonomic identifieri9597 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Subcellular locationi

Secreted By similarity

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 – 1818 By similarity
Add
BLAST
Chaini19 – 148130Lysozyme C
PRO_0000018475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 146 By similarity
Disulfide bondi48 ↔ 134 By similarity
Disulfide bondi83 ↔ 99 By similarity
Disulfide bondi95 ↔ 113 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP61627.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP61627.
SMRiP61627. Positions 19-148.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.
KOiK13915.

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.

P61627-1 [UniParc]FASTAAdd to Basket

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MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA    50
KWESGYNTRA TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS 100
ALLQDNIADA VACAKRVVRD PQGIRAWVAW RNRCQNRDVR QYVQGCGV 148
Length:148
Mass (Da):16,537
Last modified:June 7, 2004 - v1
Checksum:i8ECFD276BEB2678A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76933
, U76930, U76931, U76932 Genomic DNA. Translation: AAB41214.1.
RefSeqiXP_003808770.1. XM_003808722.1.

Genome annotation databases

GeneIDi100970943.
KEGGipps:100970943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76933
, U76930 , U76931 , U76932 Genomic DNA. Translation: AAB41214.1 .
RefSeqi XP_003808770.1. XM_003808722.1.

3D structure databases

ProteinModelPortali P61627.
SMRi P61627. Positions 19-148.
ModBasei Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P61627.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100970943.
KEGGi pps:100970943.

Organism-specific databases

CTDi 4069.

Phylogenomic databases

HOVERGENi HBG052297.
KOi K13915.

Miscellaneous databases

NextBioi 15952.

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. "Episodic adaptive evolution of primate lysozymes."
    Messier W., Stewart C.B.
    Nature 385:151-154(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.

Entry informationi

Entry nameiLYSC_PANPA
AccessioniPrimary (citable) accession number: P61627
Secondary accession number(s): P00695, Q13170, Q9UCF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: October 16, 2013
This is version 54 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.

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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