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Protein

Lysozyme RrrD

Gene

rrrD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Exhibits lytic activity against E.coli and S.typhi cell wall substrate.1 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)DescriptionActionsGraphical viewLength
Active sitei35Proton donorBy similarity1
Active sitei44NucleophileBy similarity1

GO - Molecular functioni

  • lysozyme activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:G6310-MONOMER.
ECOL316407:JW0544-MONOMER.
MetaCyc:G6310-MONOMER.

Protein family/group databases

CAZyiGH24. Glycoside Hydrolase Family 24.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme RrrD (EC:3.2.1.17)
Alternative name(s):
Endolysin
Lysis protein
Muramidase
Gene namesi
Name:rrrD
Synonyms:arrD, ybcS
Ordered Locus Names:b0555, JW0544
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13635. rrrD.

Pathology & Biotechi

Disruption phenotypei

Mutants are unable to form wild-type biofilms, which could be due to altered peptidoglycan metabolism.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002181091 – 165Lysozyme RrrDAdd BLAST165

Proteomic databases

PaxDbiP78285.
PRIDEiP78285.

Interactioni

Protein-protein interaction databases

BioGridi4259885. 4 interactors.
IntActiP78285. 3 interactors.
STRINGi511145.b0555.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi13 – 15Combined sources3
Helixi16 – 26Combined sources11
Beta strandi30 – 35Combined sources6
Beta strandi38 – 43Combined sources6
Beta strandi49 – 52Combined sources4
Helixi68 – 86Combined sources19
Helixi87 – 89Combined sources3
Helixi96 – 109Combined sources14
Helixi111 – 115Combined sources5
Helixi118 – 124Combined sources7
Helixi128 – 134Combined sources7
Helixi135 – 137Combined sources3
Helixi147 – 160Combined sources14
Turni161 – 164Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZPUX-ray2.40A/B/C/D1-165[»]
ProteinModelPortaliP78285.
SMRiP78285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.Curated

Phylogenomic databases

eggNOGiENOG4105KUS. Bacteria.
COG3772. LUCA.
HOGENOMiHOG000277068.
InParanoidiP78285.
KOiK01185.
OMAiGACRAIN.
PhylomeDBiP78285.

Family and domain databases

CDDicd00737. endolysin_autolysin. 1 hit.
Gene3Di1.10.530.40. 1 hit.
InterProiIPR033907. Endolysin_autolysin.
IPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
[Graphical view]
PfamiPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

P78285-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPSLRKAVA AAIGGGAIAI ASVLITGPSG NDGLEGVSYI PYKDIVGVWT
60 70 80 90 100
VCHGHTGKDI MLGKTYTKAE CKALLNKDLA TVARQINPYI KVDIPETTRG
110 120 130 140 150
ALYSFVYNVG AGNFRTSTLL RKINQGDIKG ACDQLRRWTY AGGKQWKGLM
160
TRREIEREVC LWGQQ
Length:165
Mass (Da):17,972
Last modified:February 1, 1997 - v1
Checksum:i370CECD5B419329B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40751.1.
U00096 Genomic DNA. Translation: AAC73656.1.
AP009048 Genomic DNA. Translation: BAE76330.1.
PIRiA64788.
RefSeqiNP_415087.1. NC_000913.3.
WP_001135281.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC73656; AAC73656; b0555.
BAE76330; BAE76330; BAE76330.
GeneIDi947539.
KEGGiecj:JW0544.
eco:b0555.
PATRICi32116276. VBIEscCol129921_0578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40751.1.
U00096 Genomic DNA. Translation: AAC73656.1.
AP009048 Genomic DNA. Translation: BAE76330.1.
PIRiA64788.
RefSeqiNP_415087.1. NC_000913.3.
WP_001135281.1. NZ_CP014272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZPUX-ray2.40A/B/C/D1-165[»]
ProteinModelPortaliP78285.
SMRiP78285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259885. 4 interactors.
IntActiP78285. 3 interactors.
STRINGi511145.b0555.

Protein family/group databases

CAZyiGH24. Glycoside Hydrolase Family 24.

Proteomic databases

PaxDbiP78285.
PRIDEiP78285.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73656; AAC73656; b0555.
BAE76330; BAE76330; BAE76330.
GeneIDi947539.
KEGGiecj:JW0544.
eco:b0555.
PATRICi32116276. VBIEscCol129921_0578.

Organism-specific databases

EchoBASEiEB3399.
EcoGeneiEG13635. rrrD.

Phylogenomic databases

eggNOGiENOG4105KUS. Bacteria.
COG3772. LUCA.
HOGENOMiHOG000277068.
InParanoidiP78285.
KOiK01185.
OMAiGACRAIN.
PhylomeDBiP78285.

Enzyme and pathway databases

BioCyciEcoCyc:G6310-MONOMER.
ECOL316407:JW0544-MONOMER.
MetaCyc:G6310-MONOMER.

Miscellaneous databases

PROiP78285.

Family and domain databases

CDDicd00737. endolysin_autolysin. 1 hit.
Gene3Di1.10.530.40. 1 hit.
InterProiIPR033907. Endolysin_autolysin.
IPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
[Graphical view]
PfamiPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLYSD_ECOLI
AccessioniPrimary (citable) accession number: P78285
Secondary accession number(s): Q2MBM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Encoded by the cryptic lambdoid prophage DLP12.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.