SLE1_STAA8
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 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=SAOUHSC_00427;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; 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}.
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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; 1280.SAXN108_0515; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR EnsemblBacteria; ABD29587; ABD29587; SAOUHSC_00427.
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 OMA; NTPVFNH; -.
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: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 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
