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Q5HJ99 (LYTM_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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

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:SACOL0263
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [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.

Sequence caution

The sequence AAW38817.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

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_0000026820

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q5HJ99 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 9974F78A19522C09

FASTA31634,317
        10         20         30         40         50         60 
MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTQMST 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

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW38817.1. Different initiation.
RefSeqYP_185158.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HJ99.
SMRQ5HJ99. Positions 45-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HJ99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000008349; EBSTAP00000008084; EBSTAG00000008348.
GeneID3236682.
GenomeReviewsGene locus SACOL0263 in contig CP000046_GR.
KEGGsac:SACOL0263.
PATRIC19526780. VBIStaAur112458_0256.
TIGRSACOL0263.

Phylogenomic databases

eggNOGCOG3942.
GeneTreeEBGT00050000023683.
HOGENOMHBG693570.
OMAIQEANSN.
ProtClustDBCLSK884525.

Enzyme and pathway databases

BioCycSAUR93062:SACOL0263-MONOMER.

Family and domain databases

InterProIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
[Graphical view]
KOK08259.
PfamPF01551. Peptidase_M23. 1 hit.
[Graphical view]
SUPFAMSSF51261. Dup_hybrid_motif. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLYTM_STAAC
AccessionPrimary (citable) accession number: Q5HJ99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families