ID   LYTH_STAAC              Reviewed;         291 AA.
AC   Q5HFD1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH; OrderedLocusNames=SACOL1687;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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}.
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DR   EMBL; CP000046; AAW36793.1; -; Genomic_DNA.
DR   RefSeq; WP_000717800.1; NC_002951.2.
DR   AlphaFoldDB; Q5HFD1; -.
DR   SMR; Q5HFD1; -.
DR   EnsemblBacteria; AAW36793; AAW36793; SACOL1687.
DR   KEGG; sac:SACOL1687; -.
DR   HOGENOM; CLU_014322_1_1_9; -.
DR   OMA; WHTNLNI; -.
DR   Proteomes; UP000000530; 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_0000226281"
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