ID   LDP_STAA8               Reviewed;         279 AA.
AC   Q2G278;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Probable autolysin LDP {ECO:0000305};
DE            EC=3.5.1.28 {ECO:0000269|PubMed:25690309};
DE   Flags: Precursor;
GN   OrderedLocusNames=SAOUHSC_00773 {ECO:0000312|EMBL:ABD29903.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 35556 / SA113;
RX   PubMed=25690309; DOI=10.1007/s00253-015-6443-2;
RA   Osipovitch D.C., Therrien S., Griswold K.E.;
RT   "Discovery of novel S. aureus autolysins and molecular engineering to
RT   enhance bacteriolytic activity.";
RL   Appl. Microbiol. Biotechnol. 99:6315-6326(2015).
CC   -!- FUNCTION: Has weak lytic activity toward S.aureus cells.
CC       {ECO:0000269|PubMed:25690309}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000269|PubMed:25690309};
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DR   EMBL; CP000253; ABD29903.1; -; Genomic_DNA.
DR   RefSeq; WP_000749380.1; NZ_LS483365.1.
DR   RefSeq; YP_499330.1; NC_007795.1.
DR   AlphaFoldDB; Q2G278; -.
DR   SMR; Q2G278; -.
DR   STRING; 1280.SAXN108_0822; -.
DR   EnsemblBacteria; ABD29903; ABD29903; SAOUHSC_00773.
DR   GeneID; 3919064; -.
DR   KEGG; sao:SAOUHSC_00773; -.
DR   PATRIC; fig|93061.5.peg.695; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3942; Bacteria.
DR   HOGENOM; CLU_016043_11_1_9; -.
DR   OMA; NANTWAI; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR007921; CHAP_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS50911; CHAP; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..279
FT                   /note="Probable autolysin LDP"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004207712"
FT   DOMAIN          51..94
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          158..279
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
SQ   SEQUENCE   279 AA;  30284 MW;  2A6F4DC80412F59A CRC64;
     MKKSLTVTVS SVLAFLALNN AAHAQQHGTQ VKTPVQHNYV SNVQAQTQSP TTYTVVAGDS
     LYKIALEHHL TLNQLYSYNP GVTPLIFPGD VISLVPQNKV KQTKAVKSPV RKASQAKKVV
     KQPVQQASKK VVVKQAPKQA VTKTVNVAYK PAQVQKSVPT VPVAHNYNKS VANRGNLYAY
     GNCTYYAFDR RAQLGRSIGS LWGNANNWNY AAKVAGFKVD KTPEVGAIFQ TAAGPYGHVG
     VVESVNPNGT ITVSEMNYAG FNVKSSRTIL NPGKYNYIH