ID   LYTN_STAAC              Reviewed;         383 AA.
AC   Q5HGI5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable cell wall hydrolase LytN;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=lytN; OrderedLocusNames=SACOL1264;
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 peptidoglycan hydrolysis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; CP000046; AAW38096.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5HGI5; -.
DR   SMR; Q5HGI5; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   EnsemblBacteria; AAW38096; AAW38096; SACOL1264.
DR   KEGG; sac:SACOL1264; -.
DR   HOGENOM; CLU_060961_0_0_9; -.
DR   OMA; GTNNYFG; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR007921; CHAP_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50911; CHAP; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..49
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..383
FT                   /note="Probable cell wall hydrolase LytN"
FT                   /id="PRO_0000227561"
FT   DOMAIN          175..219
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          241..378
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
SQ   SEQUENCE   383 AA;  43197 MW;  297D44D927AC59C0 CRC64;
     MFLYYCKECF IMNKQQSKVR YSIRKVSIGI LSISIGMFLA LGMSNKAYAD EIDKSKDFTR
     GYEQNVFAKS ELNANKNTTK DKIKNEGAVK TSDTSLKLDN KSAISNGNEI NQDIKISNTP
     KNSSQGNNLV INNNELTKEI KIANLEAQNS NQKKTNKVTN NYFGYYSFRE APKTQIYTVK
     KGDTLSAIAL KYKTTVSNIQ NTNNIANPNL IFIGQKLKVP MTPLVEPKPK TVSSNNKSNS
     NSSTLNYLKT LENRGWDFDG SYGWQCFDLV NVYWNHLYGH GLKGYGAKDI PYANNFNSEA
     KIYHNTPTFK AEPGDLVVFS GRFGGGYGHT AIVLNGDYDG KLMKFQSLDQ NWNNGGWRKA
     EVAHKVVHNY ENDMIFIRPF KKA