SLE1_STAAU
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 25-MAY-2022, entry version 92.
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; Firmicutes; 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; 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..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