ID   SLE1_STAS1              Reviewed;         327 AA.
AC   Q49UX4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=sle1; Synonyms=aaa; OrderedLocusNames=SSP2291;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE19436.1; -; Genomic_DNA.
DR   RefSeq; WP_011303892.1; NZ_MTGA01000035.1.
DR   AlphaFoldDB; Q49UX4; -.
DR   SMR; Q49UX4; -.
DR   STRING; 342451.SSP2291; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   EnsemblBacteria; BAE19436; BAE19436; SSP2291.
DR   KEGG; ssp:SSP2291; -.
DR   PATRIC; fig|342451.11.peg.2282; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3942; Bacteria.
DR   HOGENOM; CLU_016043_1_3_9; -.
DR   OMA; NTPVFNH; -.
DR   OrthoDB; 682655at2; -.
DR   Proteomes; UP000006371; 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..327
FT                   /note="N-acetylmuramoyl-L-alanine amidase sle1"
FT                   /id="PRO_0000231630"
FT   DOMAIN          27..70
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          86..129
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          150..193
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          203..327
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT   REGION          68..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  34491 MW;  32B7759C57878F5A CRC64;
     MRKKIIATVI GTSALAAVTW TNADAATTYK VKSGDSLWSI ANKYNMSVAK LKSLNNLTSN
     VIFPNQSLKV SGSTSSSTSS NTSTGSTYTV KSGDTLSGIA AKYGTTYQKI MSLNGLSNFN
     IYPGQKLKVS GAASSSSSNT SGNTSSGSTT TYTVKSGDSL SAIAAKYGTT YQKIMSLNGL
     TNFNIYPGQK LKVSGKASTG GSGSSSTGSA GYKTPVFNHS NLYDWGQCTW HVFNKRAQIG
     KGISTYWWNA NNWDTAAAAD GYTIDRKATV GSILQSDMGY YGHVAFVESV NANGSITISE
     MNYSASPGIV TYRTIPASQV SSYVYIH