ID   LYTM_STAAR              Reviewed;         316 AA.
AC   Q6GK35;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SAR0273;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   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 on
CC       polyglycine interpeptide bridges of the cell wall peptidoglycan.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-
CC         peptide link joining staphylococcal cell wall peptidoglycans.;
CC         EC=3.4.24.75;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG39300.1; -; Genomic_DNA.
DR   RefSeq; WP_000736790.1; NC_002952.2.
DR   AlphaFoldDB; Q6GK35; -.
DR   SMR; Q6GK35; -.
DR   MEROPS; M23.013; -.
DR   KEGG; sar:SAR0273; -.
DR   HOGENOM; CLU_073067_0_0_9; -.
DR   OMA; ANGHMHY; -.
DR   OrthoDB; 1891666at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..316
FT                   /note="Glycyl-glycine endopeptidase LytM"
FT                   /id="PRO_0000026823"
FT   REGION          133..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  34374 MW;  060C5A8907A69FC3 CRC64;
     MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTQMST QSQDVSYGTY YTIDSNGDYH
     HTPDGNWNQA MFDNKEYSYT FVDAQGHKHY FYNCYPKNAN ANGSGQTYVN QATAGDNNDY
     TASQSQQHIN QYGYQSNVGP DASYYSHSNN NQAYNSHNGN GKVNYPNGTS NQNGGSASKA
     TASGHAKDAS WLTSRKQLQP YGQYHGGGAH YGVDYAMPEN SPVYSLTDGT VVQAGWSNYG
     GGNQVTIKEA NSNNYQWYMH NNRLTVSAGD KVKAGDQIAY SGSTGNSTAP HVHFQRMSGG
     IGNQYAVDPT SYLQSR