ID   LYTA_STAAU              Reviewed;         481 AA.
AC   P24556;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Autolysin;
DE            EC=3.5.1.28;
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase;
GN   Name=lytA;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1677905; DOI=10.1016/0378-1119(91)90547-o;
RA   Wang X., Wilkinson B.J., Jayaswal R.K.;
RT   "Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan
RT   hydrolase activity.";
RL   Gene 102:105-109(1991).
CC   -!- FUNCTION: Autolysins are involved in some important biological
CC       processes such as cell separation, cell-wall turnover, competence for
CC       genetic transformation, formation of the flagella and sporulation.
CC       Autolysin strictly depends on the presence of choline-containing cell
CC       walls for activity.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; M76714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JQ1147; JQ1147.
DR   AlphaFoldDB; P24556; -.
DR   SMR; P24556; -.
DR   MEROPS; C51.001; -.
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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Competence; Hydrolase; Secreted;
KW   Sporulation.
FT   CHAIN           1..481
FT                   /note="Autolysin"
FT                   /id="PRO_0000070441"
FT   DOMAIN          7..142
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:0000255"
FT   DOMAIN          398..466
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
SQ   SEQUENCE   481 AA;  53819 MW;  6D5A1620D97359EA CRC64;
     MQAKLTKNEF IERLKTSEGK QFNVDLWYGF QCFDYANAGW KVLFGLLLKG LGAKDIPFAN
     NFDGLATVYQ NTPDFLAQPG DMVVFGSNYG AGYGHVAWVI EATLDYIIVY EQNWLGGGWT
     DGIEQPAGVG KKLQDDNMLM ISLCGLSVRI LKVRQRHDQF NLLHKHPKKE 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