ID   SLE1_STAHJ              Reviewed;         329 AA.
AC   Q4L3C1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=sle1; Synonyms=aaa; OrderedLocusNames=SH2547;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Peptidoglycan hydrolase involved in the splitting of the
CC       septum during cell division. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell surface
CC       {ECO:0000250}.
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; AP006716; BAE05856.1; -; Genomic_DNA.
DR   RefSeq; WP_011276796.1; NC_007168.1.
DR   AlphaFoldDB; Q4L3C1; -.
DR   SMR; Q4L3C1; -.
DR   STRING; 279808.SH2547; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   EnsemblBacteria; BAE05856; BAE05856; SH2547.
DR   GeneID; 58061412; -.
DR   KEGG; sha:SH2547; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3942; Bacteria.
DR   HOGENOM; CLU_016043_1_3_9; -.
DR   OMA; NTPVFNH; -.
DR   OrthoDB; 682655at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 3.
DR   Gene3D; 3.10.350.10; -; 3.
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; 3.
DR   SMART; SM00257; LysM; 3.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54106; SSF54106; 3.
DR   PROSITE; PS50911; CHAP; 1.
DR   PROSITE; PS51782; LYSM; 3.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cell cycle; Cell division;
KW   Cell wall biogenesis/degradation; Hydrolase; Repeat; Secreted; Septation;
KW   Signal; Virulence.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..329
FT                   /note="N-acetylmuramoyl-L-alanine amidase sle1"
FT                   /id="PRO_0000231629"
FT   DOMAIN          28..71
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          88..131
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          152..195
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          205..329
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
SQ   SEQUENCE   329 AA;  36019 MW;  8C1645D548459455 CRC64;
     MNKKILATAV LGTGALSTLF AHQAEASTTH TVRSGESLWS ISHHYGITVS KLKSLNGLSS
     NLIFPNQVLK VSGSSNYSSR SNYGNSSSTY TVRAGDSLSS IASRYGTTYR HIMNLNGLNS
     FLIFPGQQLK VSGSVSSNSH SSYNSNSGGS SSTYTVRYGD SLSSIASRYG TTYQHIMRLN
     GLNNFFIYPG QKLRVSGSAS SNTYSTRSAQ STYYSSPVFN HRNLYDWGQC TWHVFNRRAA
     IGKGISTYWW NANNWDNAAA RDGYRIDGNP TVGSIAQSDA GYYGHVAFVE RVNSNGSILV
     SEMNFSASPG ILTYRTIPAY QVRNYKFIH