ID   LYTN_STAAR              Reviewed;         383 AA.
AC   Q6GHI8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Probable cell wall hydrolase LytN;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=lytN; OrderedLocusNames=SAR1223;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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=CAG40225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571856; CAG40225.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6GHI8; -.
DR   SMR; Q6GHI8; -.
DR   KEGG; sar:SAR1223; -.
DR   HOGENOM; CLU_060961_0_0_9; -.
DR   Proteomes; UP000000596; 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_0000227564"
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;  43233 MW;  B9B5A69EDDE6DC65 CRC64;
     MFIYYCKECF VMNKQQSKVR YSIRKVSIGI LSISIGMFLA LGMSNKAYAD EIDKSKDFTR
     GYEQNVFAKS ELNANKNTTK DKIKNEAVVK TSDTSLKLDN KSAISNGNEI NQDMKISNTP
     KNSNQGNNLV VNNNEPTKEI KIANLEAQNS NQKKVNKGTN NYFGYYSFRE APKTQIYTVK
     KGDTLSAIAL KYKTTVSNIQ NTNNIANPNL IFIGQKLKVP MTPLVEPKPK TVPSNNKSNS
     NNSTLNYLKT LENRGWDFDG SYGWQCFDLV NVYWNHLYGH GLKGYGAKDI PYANNFNSEA
     KIYHNTPTFK AEPGDLVVFS GRFGGGYGHT AIVLNGDYDG KLMKFQSLDQ NWNNGGWRKA
     EVAHKVVHNY ENDMIFIRPF KKA