ID   LYTH_STAAU              Reviewed;         291 AA.
AC   O32421;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN METHICILLIN RESISTANCE.
RC   STRAIN=SR17238;
RX   PubMed=9335275; DOI=10.1128/jb.179.20.6294-6301.1997;
RA   Fujimura T., Murakami K.;
RT   "Increase of methicillin resistance in Staphylococcus aureus caused by
RT   deletion of a gene whose product is homologous to lytic enzymes.";
RL   J. Bacteriol. 179:6294-6301(1997).
CC   -!- FUNCTION: Probably involved in cell-wall metabolism.
CC       {ECO:0000269|PubMed:9335275}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- MISCELLANEOUS: Inactivation leads to increase of the methicillin
CC       resistance level.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; D76414; BAA23140.1; -; Genomic_DNA.
DR   RefSeq; WP_000717800.1; NZ_WYDB01000002.1.
DR   AlphaFoldDB; O32421; -.
DR   SMR; O32421; -.
DR   OMA; WHTNLNI; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   InterPro; IPR017273; LytH.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF08239; SH3_3; 1.
DR   PIRSF; PIRSF037730; CWA_LytH_prd; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..291
FT                   /note="Probable cell wall amidase LytH"
FT                   /id="PRO_0000226280"
FT   DOMAIN          41..105
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   DOMAIN          122..286
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   REGION          118..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32694 MW;  C296BB1178D37E1B CRC64;
     MKKIEAWLSK KGLKNKRTLI VVIAFVLFII FLFLLLNSNS EDSGNITITE NAELRTGPNA
     AYPVIYKVEK GDHFKKIGKV GKWIEVEDTS SNEKGWIAGW HTNLDIVADN TKEKNPLQGK
     TIVLDPGHGG SDQGASSNTK YKSLEKDYTL KTAKELQRTL EKEGATVKMT RTDDTYVSLE
     NRDIKGDAYL SIHNDALESS NANGMTVYWY HDNQRALADT LDATIQKKGL LSNRGSRQEN
     YQVLRQTKVP AVLLELGYIS NPTDETMIKD QLHRQILEQA IVDGLKIYFS A