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Reviewed, UniProtKB/Swiss-Prot Q7A7T0 (LYTM_STAAN)

Last modified January 19, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycyl-glycine endopeptidase lytM
    EC=3.4.24.75
Alternative name(s):
    Autolysin lytM
Gene names
Name: lytM
Ordered Locus Names: SA0265
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan By similarity.

Catalytic activity

Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the peptidase M23B family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Virulence
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 316291Glycyl-glycine endopeptidase lytM
PRO_0000026822

Sites

Metal binding1171Zinc By similarity
Metal binding2101Zinc By similarity
Metal binding2141Zinc By similarity
Metal binding2931Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7A7T0-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B2914E862691DC0C

FASTA31634,302
        10         20         30         40         50         60 
MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTLMST QSQDVSYGTY YTIDSNGDYH 

        70         80         90        100        110        120 
HTPDGNWNQA MFDNKEYSYT FVDAQGHTHY FYNCYPKNAN ANGSGQTYVN PATAGDNNDY 

       130        140        150        160        170        180 
TASQSQQHIN QYGYQSNVGP DASYYSHSNN NQAYNSHDGN GKVNYPNGTS NQNGGSASKA 

       190        200        210        220        230        240 
TASGHAKDAS WLTSRKQLQP YGQYHGGGAH YGVDYAMPEN SPVYSLTDGT VVQAGWSNYG 

       250        260        270        280        290        300 
GGNQVTIKEA NSNNYQWYMH NNRLTVSAGD KVKAGDQIAY SGSTGNSTAP HVHFQRMSGG 

       310 
IGNQYAVDPT SYLQSR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB41489.1.
PIRF89791.
RefSeqNP_373511.1.

3D structure databases

SMRQ7A7T0. Positions 45-314, 185-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7A7T0.

Genome annotation databases

GeneID1123044.
GenomeReviewsGene locus SA0265 in contig BA000018_GR.
KEGGsau:SA0265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3942.
HOGENOMHBG693570.
OMAAYNSHNG.

Enzyme and pathway databases

BioCycSAUR158879:SA0265-MONOMER.

Family and domain databases

InterProIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
IPR002886. Peptidase_M23B.
[Graphical view]
PANTHERPTHR21666:SF7. Peptidase_M23B. 1 hit.
PfamPF01551. Peptidase_M23. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYTM_STAAN
AccessionPrimary (citable) accession number: Q7A7T0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: July 5, 2004
Last modified: January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents