ID   LYTH_STAAS              Reviewed;         291 AA.
AC   Q6G8T7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH; OrderedLocusNames=SAS1568;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Probably involved in cell-wall metabolism. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; BX571857; CAG43369.1; -; Genomic_DNA.
DR   RefSeq; WP_000717800.1; NC_002953.3.
DR   AlphaFoldDB; Q6G8T7; -.
DR   SMR; Q6G8T7; -.
DR   KEGG; sas:SAS1568; -.
DR   HOGENOM; CLU_014322_1_1_9; -.
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_0000226284"
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