ID   LYTN_STAAS              Reviewed;         383 AA.
AC   Q6G9W6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable cell wall hydrolase LytN;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=lytN; OrderedLocusNames=SAS1181;
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 peptidoglycan hydrolysis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG42958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571857; CAG42958.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6G9W6; -.
DR   SMR; Q6G9W6; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   PRIDE; Q6G9W6; -.
DR   KEGG; sas:SAS1181; -.
DR   HOGENOM; CLU_060961_0_0_9; -.
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_0000227565"
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;  43167 MW;  304728FD04643625 CRC64;
     MFVYYCKECF IMNKQQSKVR YSIRKVSIGI LSISIGMFLA LGMSNKAYAD EIDKSKDFTR
     GYEQNVFAKS ELNANKNTTK DKIKNEGAVK TSDTSLKLDN KSAISNGNEI NQDIKISNTP
     KNSSQGNNLV INNNEPTKEI 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