ID   LYTM_STAAE              Reviewed;         316 AA.
AC   A0A0H3K6J4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 2.
DT   03-AUG-2022, entry version 24.
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=NWMN_0210;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Newman;
RX   PubMed=24434550; DOI=10.1073/pnas.1317181111;
RA   Becker S., Frankel M.B., Schneewind O., Missiakas D.;
RT   "Release of protein A from the cell wall of Staphylococcus aureus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:1574-1579(2014).
CC   -!- FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on
CC       polyglycine interpeptide bridges of the cell wall peptidoglycan (By
CC       similarity). Releases SpA, an immunologically active peptide, from the
CC       cell wall (PubMed:24434550). {ECO:0000250|UniProtKB:O33599,
CC       ECO:0000269|PubMed:24434550}.
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; Evidence={ECO:0000305|PubMed:24434550};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O33599};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O33599}.
CC   -!- DISRUPTION PHENOTYPE: Much less SpA is released from the cell wall.
CC       {ECO:0000269|PubMed:24434550}.
CC   -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF66482.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009351; BAF66482.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000736798.1; NZ_CP023390.1.
DR   AlphaFoldDB; A0A0H3K6J4; -.
DR   SMR; A0A0H3K6J4; -.
DR   EnsemblBacteria; BAF66482; BAF66482; NWMN_0210.
DR   KEGG; sae:NWMN_0210; -.
DR   HOGENOM; CLU_073067_0_0_9; -.
DR   Proteomes; UP000006386; 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:0000255"
FT   CHAIN           26..316
FT                   /note="Glycyl-glycine endopeptidase LytM"
FT                   /id="PRO_0000445585"
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|UniProtKB:O33599"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O33599"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O33599"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O33599"
SQ   SEQUENCE   316 AA;  34317 MW;  9974F78A19522C09 CRC64;
     MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTQMST QSQDVSYGTY YTIDSNGDYH
     HTPDGNWNQA MFDNKEYSYT FVDAQGHTHY FYNCYPKNAN ANGSGQTYVN PATAGDNNDY
     TASQSQQHIN QYGYQSNVGP DASYYSHSNN NQAYNSHDGN GKVNYPNGTS NQNGGSASKA
     TASGHAKDAS WLTSRKQLQP YGQYHGGGAH YGVDYAMPEN SPVYSLTDGT VVQAGWSNYG
     GGNQVTIKEA NSNNYQWYMH NNRLTVSAGD KVKAGDQIAY SGSTGNSTAP HVHFQRMSGG
     IGNQYAVDPT SYLQSR