Skip Header

Contribute Send feedback
Read comments (?) or add your own

P39046 (MUR2_ENTHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Muramidase-2
EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramoylhydrolase
Lysozyme
Peptidoglycan hydrolase
Pg-hydrolase 2
Gene names
Ordered Locus Names:EHR_05900
OrganismEnterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258) [Complete proteome] [HAMAP]
Taxonomic identifier768486 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Enterococcus ›

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4

Catalytic activity

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.

Subcellular location

Secreted.

Domain

LysM repeats are thought to be involved in peptidoglycan binding.

Sequence similarities

Belongs to the glycosyl hydrolase 73 family.

Contains 6 LysM repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4949 Ref.1
Chain50 – 666617Muramidase-2
PRO_0000012120

Regions

Repeat257 – 29943LysM 1
Repeat338 – 38043LysM 2
Repeat414 – 45643LysM 3
Repeat489 – 53143LysM 4
Repeat565 – 60743LysM 5
Repeat623 – 66543LysM 6

Sequences

Sequence LengthMass (Da)Tools
P39046 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: FF0A7FAFCD810BA3

FASTA66670,670
        10         20         30         40         50         60 
MENIARKERR RLNETKRFRK VKRSAALVGT AMVGCSVAAP LIQPVQVDAD QTPTQFGARI 

        70         80         90        100        110        120 
NTAAFIAEIA TYAQPIAQAN DLYASVMIAQ AVVESGWGSS ALSQAPYYNL FGIKGSYQGQ 

       130        140        150        160        170        180 
TVYMDTLEYL NNKWVSKKEP FRQYPSFAES FNDNAYVLRN TSFGNGYYYA GTWKSNTKSY 

       190        200        210        220        230        240 
TDATACLTGR YATDPGYAGK LNNIITTYGL TKYDTPASGN AGGGVTIGNG GNTGNTSNSG 

       250        260        270        280        290        300 
STSGNSGGSA TTTGTTYTVK SGDSVWGISH SFGITMAQLI EWNNIKNNFI YPGQKLTIKG 

       310        320        330        340        350        360 
GQSAGSSTTN TGNNASSGNT SGNTNTSGST GQATGAKYTV KSGDSVWKIA NDHGISMNQL 

       370        380        390        400        410        420 
IEWNNIKNNF VYPGQQLVVS KGSSSASGST SNTSTGNTSS NTANTGSTTS GSTYTVKAGE 

       430        440        450        460        470        480 
SVWSVSNKFG ISMNQLIQWN NIKNNFIYPG QKLIVKGGSS SSNASTSTAN NKNTASSNTS 

       490        500        510        520        530        540 
STATGQATYT VKAGESVWGV ANKNGISMNQ LIEWNNIKNN FIYPGQKLIV KGGSSKASAT 

       550        560        570        580        590        600 
ATIKPTASTP ASTTPTASST GDTKYTVKAG ESVWGVANKH HITMDQLIEW NNIKNNFIYP 

       610        620        630        640        650        660 
GQEVIVKKGT AQSTPAKSDE KTYTVKAGES VWGVADSHGI TMNQLIEWNN IKNNFIYPGQ 


QLIVKK

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae."
Chu C.-P., Kariyama R., Daneo-Moore L., Shockman G.D.
J. Bacteriol. 174:1619-1625(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-73.
Strain: ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258.
[2]"Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790, a model organism for the study of ion transport, bioenergetics, and copper homeostasis."
Gaechter T., Wunderlin C., Schmidheini T., Solioz M.
J. Bacteriol. 194:5126-5127(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258.
[3]"The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin."
Dolinger D.L., Daneo-Moore L., Shockman G.D.
J. Bacteriol. 171:4355-4361(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258.
[4]"Thermosensitive cell growth mutants of Enterococcus hirae that elongate at non-permissive temperature are stimulated to divide by parental autolytic enzymes."
Del Mar Lleo M., Canepari P., Satta G.
J. Gen. Microbiol. 139:3099-3117(1993)
Cited for: FUNCTION.
Strain: ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M77639 Genomic DNA. Translation: AAA24776.1.
CP003504 Genomic DNA. Translation: AFM70129.1.
PIRA42296.
RefSeqYP_006487020.1. NC_018081.1.

3D structure databases

ProteinModelPortalP39046.
ModBaseSearch...

Protein family/group databases

CAZyCBM50. Carbohydrate-Binding Module Family 50.
GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13177133.
KEGGehr:EHR_05900.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR013338. Lysozyme_dom_subfam2.
IPR002901. Mano_Glyc_endo_b_GlcNAc.
IPR018392. Peptidoglycan-bd_lysin.
IPR002482. Peptidoglycan-bd_Lysin_subgr.
[Graphical view]
PfamPF01832. Glucosaminidase. 1 hit.
PF01476. LysM. 6 hits.
[Graphical view]
SMARTSM00257. LysM. 6 hits.
SM00047. LYZ2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMUR2_ENTHA
AccessionPrimary (citable) accession number: P39046
Secondary accession number(s): I6TA70
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents