ID   LYTH_STAEQ              Reviewed;         291 AA.
AC   Q5HNS0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH; OrderedLocusNames=SERP1194;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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; CP000029; AAW54573.1; -; Genomic_DNA.
DR   RefSeq; WP_002470411.1; NC_002976.3.
DR   AlphaFoldDB; Q5HNS0; -.
DR   SMR; Q5HNS0; -.
DR   STRING; 176279.SERP1194; -.
DR   EnsemblBacteria; AAW54573; AAW54573; SERP1194.
DR   KEGG; ser:SERP1194; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_1_1_9; -.
DR   OMA; WHTNLNI; -.
DR   OrthoDB; 1184688at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..291
FT                   /note="Probable cell wall amidase LytH"
FT                   /id="PRO_0000226286"
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          123..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32557 MW;  6B70CCFA489344B1 CRC64;
     MKKIDSWLTK HGLKNRLTLV VIVIFIIFLI LLFMFVNLSD EDTGQITITE NAELRTGPNA
     AYPVIYKIEK GESFKKIDRK GKWIEVQNHA GTEKGWVAGW HTNLNIPADQ SLSSNPLKGK
     TIVLDPGHGG SDQGASSSTP SKSLEKNYTL KTAKELKKLL NKEGAHVKMT RSNDKYVSLD
     DRNIKGDAFI SIHNDALDSS NANGVTVYWF KDKQETLAQT LNSAIQKKAL LTNRGSRQQN
     YQVLRQTDIP AVLLELGYIS NPTDESMIND QLHRQVVEQA IVDGLKQYFS S