ID   SLE1_STAEQ              Reviewed;         324 AA.
AC   Q5HRU2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=sle1; Synonyms=aaa; OrderedLocusNames=SERP0100;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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}.
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DR   EMBL; CP000029; AAW53528.1; -; Genomic_DNA.
DR   RefSeq; WP_001829380.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRU2; -.
DR   SMR; Q5HRU2; -.
DR   STRING; 176279.SERP0100; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   EnsemblBacteria; AAW53528; AAW53528; SERP0100.
DR   GeneID; 50019630; -.
DR   KEGG; ser:SERP0100; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3942; Bacteria.
DR   HOGENOM; CLU_016043_1_3_9; -.
DR   OMA; NTPVFNH; -.
DR   OrthoDB; 682655at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Repeat;
KW   Secreted; Septation; Signal; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..324
FT                   /note="N-acetylmuramoyl-L-alanine amidase sle1"
FT                   /id="PRO_0000231627"
FT   DOMAIN          27..70
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          84..127
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          147..190
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          200..324
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
SQ   SEQUENCE   324 AA;  35075 MW;  AE24C366090455F8 CRC64;
     MQKKYITAII GTTALSALAS THAQAATTHT VKSGESVWSI SHKYGISIAK LKSLNGLTSN
     LIFPNQVLKV SGSSSRATST NSGTVYTVKA GDSLSSIAAK YGTTYQKIMQ LNGLNNYLIF
     PGQKLKVSGK ATSSSRAKAS GSSGRTATYT VKYGDSLSAI ASKYGTTYQK IMQLNGLTNF
     FIYPGQKLKV PGGSSSSSSS NNTRSNGGYY SPTFNHQNLY TWGQCTWHVF NRRAEIGKGI
     STYWWNANNW DNASAADGYT IDYRPTVGSI AQTDAGYYGH VAFVERVNSD GSILVSEMNW
     SAAPGNMTYR TIPAYQVRNY KFIH