ID   LYTH_STAHJ              Reviewed;         291 AA.
AC   Q4L6X7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH; OrderedLocusNames=SH1289;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE04598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP006716; BAE04598.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041615143.1; NC_007168.1.
DR   AlphaFoldDB; Q4L6X7; -.
DR   SMR; Q4L6X7; -.
DR   STRING; 279808.SH1289; -.
DR   EnsemblBacteria; BAE04598; BAE04598; SH1289.
DR   KEGG; sha:SH1289; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_7_1_9; -.
DR   OrthoDB; 1184688at2; -.
DR   Proteomes; UP000000543; Chromosome.
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_0000226288"
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          124..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32541 MW;  459D7E8E8A110713 CRC64;
     MNKVDAWLSK HDLKNLTTLI VVGAFILFLI LLFMLMNHSD QGSNRITVSE NAELRTGPNA
     AYPVIYQVEK GDTFTRLSKS GKWIEVESRD GSEKSWIAGW HTSLNIEAGA NKKVNPLKNK
     VIVLDPGHGG NDQGASSNTS KKSLEKNYTL KTAKELRRAL EKAGATVKLT RSDDTYVSLD
     DRKLNGDAYI SIHNDSLDSP NANGATVYWY KNNQEALAET LNTNIQKKAM LFNRGTRQEN
     FQVLRQTNKP AVLLELGYIS NPTDEVMIRN QIHRQVVEEA VVDGLKQYFA S