ID   LYTM_STAAS              Reviewed;         316 AA.
AC   Q6GCJ6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Glycyl-glycine endopeptidase lytM;
DE            EC=3.4.24.75;
DE   AltName: Full=Autolysin lytM;
DE   Flags: Precursor;
GN   Name=lytM; OrderedLocusNames=SAS0252;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting
CC       on polyglycine interpeptide bridges of the cell wall peptidoglycan
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of the -Gly-|-Gly- bond in the
CC       pentaglycine inter-peptide link joining staphylococcal cell wall
CC       peptidoglycans.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M23B family.
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DR   EMBL; BX571857; CAG42023.1; -; Genomic_DNA.
DR   RefSeq; YP_042377.1; -.
DR   SMR; Q6GCJ6; 45-314.
DR   GeneID; 2863939; -.
DR   GenomeReviews; BX571857_GR; SAS0252.
DR   KEGG; sas:SAS0252; -.
DR   HOGENOM; Q6GCJ6; -.
DR   OMA; Q6GCJ6; AYNSHNG.
DR   BioCyc; SAUR282459:SAS0252-MON; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR002886; Peptidase_M23B.
DR   PANTHER; PTHR21666:SF7; Peptidase_M23B; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Virulence;
KW   Zinc; Zymogen.
FT   SIGNAL        1     25       By similarity.
FT   CHAIN        26    316       Glycyl-glycine endopeptidase lytM.
FT                                /FTId=PRO_0000026824.
FT   METAL       117    117       Zinc (By similarity).
FT   METAL       210    210       Zinc (By similarity).
FT   METAL       214    214       Zinc (By similarity).
FT   METAL       293    293       Zinc (By similarity).
SQ   SEQUENCE   316 AA;  34355 MW;  3A53C4331E8B024F CRC64;
     MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTQMST QSQDVSYGTY YTIDSNGDYH
     HTPDGNWNQA MFDNKEYSYT FVDAQGHTHY FYNCYPKNAN ANGSGQTYVN PAIAGDNNDY
     TASQSQQHIN QYGYQSNVGP DASYYSHSNN NQAYNSHDGN GKVNYPNGTS NQNGGLASKA
     TASGHAKDAS WLTSRKQLQP YGQYHGGGAH YGVDYAMPEN SPVYSLTDGT VVQAGWSNYG
     GGNQVTIKEA NSNNYQWYMH NNRLTVSAGD KVKAGDQIAY SGSTGNSTAP HVHFQRMSGG
     IGNQYAVDPT SYLQSR
//