ID   SLE1_STAAU              Reviewed;         334 AA.
AC   P0C1U7; Q33E91; Q99WD8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=sle1; Synonyms=aaa;
OS   Staphylococcus aureus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=4074;
RX   PubMed=16040992; DOI=10.1128/iai.73.8.4793-4802.2005;
RA   Heilmann C., Hartleib J., Hussain M.S., Peters G.;
RT   "The multifunctional Staphylococcus aureus autolysin aaa mediates adherence
RT   to immobilized fibrinogen and fibronectin.";
RL   Infect. Immun. 73:4793-4802(2005).
CC   -!- FUNCTION: Peptidoglycan hydrolase involved in the splitting of the
CC       septum during cell division. Binds to both alpha and beta-chains of
CC       human fibrinogen as well as fibronectin, which suggests a role in the
CC       colonization of host factor-coated material or host tissue. Also
CC       exhibits lytic activity against S.carnosus and S.aureus cells but not
CC       against M.luteus cells. {ECO:0000269|PubMed:16040992}.
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:0000269|PubMed:16040992}. Cell
CC       surface {ECO:0000269|PubMed:16040992}.
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DR   EMBL; AJ250906; CAC80837.1; -; Genomic_DNA.
DR   RefSeq; WP_001170264.1; NZ_WWFR01000010.1.
DR   AlphaFoldDB; P0C1U7; -.
DR   SMR; P0C1U7; -.
DR   OMA; NHSNLYD; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 3.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 3.10.350.10; LysM domain; 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   PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01476; LysM; 3.
DR   SMART; SM00257; LysM; 3.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54106; LysM domain; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..334
FT                   /note="N-acetylmuramoyl-L-alanine amidase sle1"
FT                   /id="PRO_0000231620"
FT   DOMAIN          27..70
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          91..134
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          158..201
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          210..334
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  35836 MW;  4C1E30AD9DE61D36 CRC64;
     MQKKVIAAII GTSAISAVAA TQANAATTHT VKPGESVWAI SNKYGISIAK LKSLNNLTSN
     LIFPNQVLKV SGSSNSTSNS SRPSTNSGGG SYYTVQAGDS LSLIASKYGT TYQNIMRLNG
     LNNFFIYPGQ KLKVSGTASS SNAASNSSRP STNSGGGSYY TVQAGDSLSL IASKYGTTYQ
     KIMSLNGLNN FFIYPGQKLK VTGNASTNSG SATTTNRGYN TPVFSHQNLY TWGQCTYHVF
     NRRAEIGKGI STYWWNANNW DNAAAADGYT IDNRPTVGSI AQTDVGYYGH VMFVERVNND
     GSILVSEMNY SAAPGILTYR TVPAYQVNNY RYIH
//