SLE1_STAAB
ID SLE1_STAAB Reviewed; 335 AA.
AC Q2YVT4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase sle1;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=sle1; Synonyms=aaa; OrderedLocusNames=SAB0414;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80102.1; -; Genomic_DNA.
DR RefSeq; WP_001170266.1; NC_007622.1.
DR AlphaFoldDB; Q2YVT4; -.
DR SMR; Q2YVT4; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR MoonProt; Q2YVT4; -.
DR KEGG; sab:SAB0414; -.
DR HOGENOM; CLU_016043_1_3_9; -.
DR OMA; NTPVFNH; -.
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; Repeat; Secreted; Septation;
KW Signal; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..335
FT /note="N-acetylmuramoyl-L-alanine amidase sle1"
FT /id="PRO_0000231621"
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 211..335
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 335 AA; 35937 MW; 4C132CC34205FFB3 CRC64;
MQKKVIAAII GTSAISAVAA TQANAATTHT VKPGESVWAI SNKYGISIAK LKSLNNLTSN
LIFPNQVLKV SGSSNSTSNS SRPSTNSGGG SYYTVQAGDS LSLIASKYGT TYQNIMRLNG
LNNFFIYPGQ KLKVSGTASS SNAASNSSRP STNSGGGSYY TVQAGDSLSL IASKYGTTYQ
KIMSLNGLNN FFIYPGQKLK VTGNATSSNS ASATTTNRGY NTPVFSHQNL YTWGQCTYHV
FNRRAEIGKG ISTYWWNANN WDNAAAADGY TIDNRPTVGS IAQTDVGYYG HVMFVERVNN
DGSILVSEMN YSAAPGILTY RTVPAYQVNN YRYIH