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Protein

Muramidase-2

Gene

EHR_05900

Organism
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May work in concert with and potentiate the processive hydrolytic action of muramidase-1, which requires binding of the enzyme to non-reducing ends of glycan chains. Hydrolysis in the midst of glycan chains would increase the number of binding sites for muramidase-1. May function in facilitating septum formation and cell separation. Active on M.luteus cell walls and on E.hirae cell wall fractions, but not active on E.hirae intact cell walls. Can covalently bind penicillin.2 Publications

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Cell wall biogenesis/degradation, Septation

Protein family/group databases

CAZyiCBM50. Carbohydrate-Binding Module Family 50.
GH73. Glycoside Hydrolase Family 73.

Names & Taxonomyi

Protein namesi
Recommended name:
Muramidase-2 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramoylhydrolase
Lysozyme
Peptidoglycan hydrolase
Pg-hydrolase 2
Gene namesi
Ordered Locus Names:EHR_05900
OrganismiEnterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Taxonomic identifieri768486 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000002895 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 491 PublicationAdd BLAST49
ChainiPRO_000001212050 – 666Muramidase-2Add BLAST617

Structurei

3D structure databases

ProteinModelPortaliP39046.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini255 – 298LysM 1PROSITE-ProRule annotationAdd BLAST44
Domaini336 – 379LysM 2PROSITE-ProRule annotationAdd BLAST44
Domaini412 – 455LysM 3PROSITE-ProRule annotationAdd BLAST44
Domaini487 – 530LysM 4PROSITE-ProRule annotationAdd BLAST44
Domaini563 – 606LysM 5PROSITE-ProRule annotationAdd BLAST44
Domaini621 – 664LysM 6PROSITE-ProRule annotationAdd BLAST44

Domaini

LysM domains are thought to be involved in peptidoglycan binding.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 73 family.Curated
Contains 6 LysM domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

OrthoDBiPOG091H05V1.

Family and domain databases

CDDicd00118. LysM. 6 hits.
Gene3Di3.10.350.10. 6 hits.
InterProiIPR018392. LysM_dom.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 6 hits.
[Graphical view]
SMARTiSM00257. LysM. 6 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 6 hits.
PROSITEiPS51782. LYSM. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39046-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENIARKERR RLNETKRFRK VKRSAALVGT AMVGCSVAAP LIQPVQVDAD
60 70 80 90 100
QTPTQFGARI NTAAFIAEIA TYAQPIAQAN DLYASVMIAQ AVVESGWGSS
110 120 130 140 150
ALSQAPYYNL FGIKGSYQGQ TVYMDTLEYL NNKWVSKKEP FRQYPSFAES
160 170 180 190 200
FNDNAYVLRN TSFGNGYYYA GTWKSNTKSY TDATACLTGR YATDPGYAGK
210 220 230 240 250
LNNIITTYGL TKYDTPASGN AGGGVTIGNG GNTGNTSNSG STSGNSGGSA
260 270 280 290 300
TTTGTTYTVK SGDSVWGISH SFGITMAQLI EWNNIKNNFI YPGQKLTIKG
310 320 330 340 350
GQSAGSSTTN TGNNASSGNT SGNTNTSGST GQATGAKYTV KSGDSVWKIA
360 370 380 390 400
NDHGISMNQL IEWNNIKNNF VYPGQQLVVS KGSSSASGST SNTSTGNTSS
410 420 430 440 450
NTANTGSTTS GSTYTVKAGE SVWSVSNKFG ISMNQLIQWN NIKNNFIYPG
460 470 480 490 500
QKLIVKGGSS SSNASTSTAN NKNTASSNTS STATGQATYT VKAGESVWGV
510 520 530 540 550
ANKNGISMNQ LIEWNNIKNN FIYPGQKLIV KGGSSKASAT ATIKPTASTP
560 570 580 590 600
ASTTPTASST GDTKYTVKAG ESVWGVANKH HITMDQLIEW NNIKNNFIYP
610 620 630 640 650
GQEVIVKKGT AQSTPAKSDE KTYTVKAGES VWGVADSHGI TMNQLIEWNN
660
IKNNFIYPGQ QLIVKK
Length:666
Mass (Da):70,670
Last modified:February 1, 1995 - v1
Checksum:iFF0A7FAFCD810BA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77639 Genomic DNA. Translation: AAA24776.1.
CP003504 Genomic DNA. Translation: AFM70129.1.
PIRiA42296.
RefSeqiWP_010736969.1. NZ_KB946228.1.

Genome annotation databases

EnsemblBacteriaiAFM70129; AFM70129; EHR_05900.
GeneIDi13177133.
KEGGiehr:EHR_05900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77639 Genomic DNA. Translation: AAA24776.1.
CP003504 Genomic DNA. Translation: AFM70129.1.
PIRiA42296.
RefSeqiWP_010736969.1. NZ_KB946228.1.

3D structure databases

ProteinModelPortaliP39046.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM50. Carbohydrate-Binding Module Family 50.
GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFM70129; AFM70129; EHR_05900.
GeneIDi13177133.
KEGGiehr:EHR_05900.

Phylogenomic databases

OrthoDBiPOG091H05V1.

Family and domain databases

CDDicd00118. LysM. 6 hits.
Gene3Di3.10.350.10. 6 hits.
InterProiIPR018392. LysM_dom.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 6 hits.
[Graphical view]
SMARTiSM00257. LysM. 6 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 6 hits.
PROSITEiPS51782. LYSM. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMUR2_ENTHA
AccessioniPrimary (citable) accession number: P39046
Secondary accession number(s): I6TA70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.