ID SLE1_STAA8 Reviewed; 334 AA. AC Q2G0U9; Q33E91; Q99WD8; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1; DE EC=3.5.1.28; DE Flags: Precursor; GN Name=sle1; Synonyms=aaa; OrderedLocusNames=SAOUHSC_00427; OS Staphylococcus aureus (strain NCTC 8325 / PS 47). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-39, AND FUNCTION. RX PubMed=16262792; DOI=10.1111/j.1365-2958.2005.04881.x; RA Kajimura J., Fujiwara T., Yamada S., Suzawa Y., Nishida T., Oyamada Y., RA Hayashi I., Yamagishi J., Komatsuzawa H., Sugai M.; RT "Identification and molecular characterization of an N-acetylmuramyl-L- RT alanine amidase Sle1 involved in cell separation of Staphylococcus RT aureus."; RL Mol. Microbiol. 58:1087-1101(2005). RN [2] 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION. RC STRAIN=RN4220; RX PubMed=20472795; DOI=10.1128/jb.01452-09; RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E., RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S., RA van Dijl J.M.; RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in RT Staphylococcus aureus."; RL J. Bacteriol. 192:3788-3800(2010). 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:16262792}. 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:0000269|PubMed:20472795}. CC -!- INDUCTION: Repressed by mgrA. More protein is secreted in a secG mutant CC (at protein level). {ECO:0000269|PubMed:20472795}. 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; AB113206; BAE47503.1; -; Genomic_DNA. DR EMBL; CP000253; ABD29587.1; -; Genomic_DNA. DR RefSeq; WP_001170264.1; NZ_LS483365.1. DR RefSeq; YP_499011.1; NC_007795.1. DR AlphaFoldDB; Q2G0U9; -. DR SMR; Q2G0U9; -. DR STRING; 93061.SAOUHSC_00427; -. DR CAZy; CBM50; Carbohydrate-Binding Module Family 50. DR PaxDb; 1280-SAXN108_0515; -. DR GeneID; 3919100; -. DR KEGG; sao:SAOUHSC_00427; -. DR PATRIC; fig|93061.5.peg.391; -. DR eggNOG; COG1388; Bacteria. DR eggNOG; COG3942; Bacteria. DR HOGENOM; CLU_016043_1_3_9; -. DR OrthoDB; 9813368at2; -. DR PRO; PR:Q2G0U9; -. DR Proteomes; UP000008816; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008932; F:lytic endotransglycosylase activity; IBA:GO_Central. 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 1: Evidence at protein level; KW Antimicrobial; Bacteriolytic enzyme; Cell cycle; Cell division; KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase; KW Reference proteome; Repeat; Secreted; Septation; 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_0000249326" 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 //