LYTO_STAA8
ID LYTO_STAA8 Reviewed; 481 AA.
AC Q2FX77;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Probable autolysin LytO {ECO:0000305};
DE EC=3.5.1.28 {ECO:0000269|PubMed:25690309};
GN Name=lytO {ECO:0000303|PubMed:25690309};
GN OrderedLocusNames=SAOUHSC_02019 {ECO:0000312|EMBL:ABD31075.1};
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};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31075.1; -; Genomic_DNA.
DR RefSeq; WP_001148145.1; NZ_LS483365.1.
DR RefSeq; YP_500516.1; NC_007795.1.
DR AlphaFoldDB; Q2FX77; -.
DR SMR; Q2FX77; -.
DR STRING; 1280.SAXN108_1909; -.
DR MEROPS; C51.001; -.
DR EnsemblBacteria; ABD31075; ABD31075; SAOUHSC_02019.
DR GeneID; 3920473; -.
DR KEGG; sao:SAOUHSC_02019; -.
DR PATRIC; fig|93061.5.peg.1832; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_050469_0_0_9; -.
DR OMA; WHTANQV; -.
DR Proteomes; UP000008816; Chromosome.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF08460; SH3_5; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
DR PROSITE; PS50911; CHAP; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW Hydrolase; Reference proteome.
FT CHAIN 1..481
FT /note="Probable autolysin LytO"
FT /id="PRO_0000445038"
FT DOMAIN 7..148
FT /note="Peptidase C51"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT DOMAIN 198..323
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000305|PubMed:25690309"
FT DOMAIN 398..466
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT REGION 155..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 54030 MW; B3F6E041E617ED85 CRC64;
MQAKLTKNEF IEWLKTSEGK QFNVDLWYGF QCFDYANAGW KVLFGLLLKG LGAKDIPFAN
NFDGLATVYQ NTPDFLAQPG DMVVFGSNYG AGYGHVAWVI EATLDYIIVY EQNWLGGGWT
DGIEQPGWGW EKVTRRQHAY DFPMWFIRPN FKSETAPRSV QSPTQAPKKE TAKPQPKAVE
LKIIKDVVKG YDLPKRGSNP KGIVIHNDAG SKGATAEAYR NGLVNAPLSR LEAGIAHSYV
SGNTVWQALD ESQVGWHTAN QIGNKYYYGI EVCQSMGADN ATFLKNEQAT FQECARLLKK
WGLPANRNTI RLHNEFTSTS CPHRSSVLHT GFDPVTRGLL PEDKRLQLKD YFIKQIRAYM
DGKIPVATVS NESSASSNTV KPVASAWKRN KYGTYYMEES ARFTNGNQPI TVRKVGPFLS
CPVGYQFQPG GYCDYTEVML QDGHVWVGYT WEGQRYYLPI RTWNGSAPPN QILGDLWGEI
S