LYTM_STAAW
ID LYTM_STAAW Reviewed; 316 AA.
AC Q8NYG1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=MW0252;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94117.1; -; Genomic_DNA.
DR RefSeq; WP_000736792.1; NC_003923.1.
DR AlphaFoldDB; Q8NYG1; -.
DR SMR; Q8NYG1; -.
DR MEROPS; M23.013; -.
DR EnsemblBacteria; BAB94117; BAB94117; BAB94117.
DR KEGG; sam:MW0252; -.
DR HOGENOM; CLU_073067_0_0_9; -.
DR OMA; ANGHMHY; -.
DR Proteomes; UP000000418; 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_0000026825"
FT REGION 133..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..179
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; 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