SSAAL_STAA8
ID SSAAL_STAA8 Reviewed; 265 AA.
AC Q2G0D4;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Probable autolysin SsaALP {ECO:0000305};
DE EC=3.5.1.28 {ECO:0000269|PubMed:25690309};
DE Flags: Precursor;
GN OrderedLocusNames=SAOUHSC_00671 {ECO:0000312|EMBL:ABD29804.1};
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 [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 [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35556 / SA113;
RX PubMed=25690309; DOI=10.1007/s00253-015-6443-2;
RA Osipovitch D.C., Therrien S., Griswold K.E.;
RT "Discovery of novel S. aureus autolysins and molecular engineering to
RT enhance bacteriolytic activity.";
RL Appl. Microbiol. Biotechnol. 99:6315-6326(2015).
CC -!- FUNCTION: Has weak lytic activity toward S.aureus cells.
CC {ECO:0000269|PubMed:25690309}.
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 Evidence={ECO:0000269|PubMed:25690309};
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DR EMBL; CP000253; ABD29804.1; -; Genomic_DNA.
DR RefSeq; WP_000731644.1; NZ_LS483365.1.
DR RefSeq; YP_499230.1; NC_007795.1.
DR AlphaFoldDB; Q2G0D4; -.
DR SMR; Q2G0D4; -.
DR STRING; 1280.SAXN108_0732; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR EnsemblBacteria; ABD29804; ABD29804; SAOUHSC_00671.
DR GeneID; 3919434; -.
DR KEGG; sao:SAOUHSC_00671; -.
DR PATRIC; fig|93061.5.peg.602; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3942; Bacteria.
DR HOGENOM; CLU_016043_11_0_9; -.
DR OMA; TQHTVKS; -.
DR Proteomes; UP000008816; Chromosome.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
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; 2.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS50911; CHAP; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW Hydrolase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..265
FT /note="Probable autolysin SsaALP"
FT /evidence="ECO:0000255"
FT /id="PRO_5004207887"
FT DOMAIN 27..70
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 89..132
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 141..265
FT /note="Peptidase C51"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 28187 MW; 16A8159D0F3C0285 CRC64;
MKKLAFAITA TSGAAAFLTH HDAQASTQHT VQSGESLWSI AQKYNTSVES IKQNNQLDNN
LVFPGQVISV GGSDAQNTSN TSPQAGSASS HTVQAGESLN IIASRYGVSV DQLMAANNLR
GYLIMPNQTL QIPNGGSGGT TPTATTGSNG NASSFNHQNL YTAGQCTWYV FDRRAQAGSP
ISTYWSDAKY WAGNAANDGY QVNNTPSVGS IMQSTPGPYG HVAYVERVNG DGSILISEMN
YTYGPYNMNY RTIPASEVSS YAFIH