ID   LYTN_STAA8              Reviewed;         383 AA.
AC   Q9ZNI1; Q2FZ35; Q9S684;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Probable cell wall hydrolase LytN;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=lytN; OrderedLocusNames=SAOUHSC_01219;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RX   PubMed=9931440; DOI=10.1016/s0378-1119(98)00508-3;
RA   Sugai M., Fujiwara T., Komatsuzawa H., Suginaka H.;
RT   "Identification and molecular characterization of a gene homologous to epr
RT   (endopeptidase resistance gene) in Staphylococcus aureus.";
RL   Gene 224:67-75(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10077832; DOI=10.1111/j.1574-6968.1999.tb13417.x;
RA   Tschierske M., Mori C., Rohrer S., Ehlert K., Shaw K.J., Berger-Baechi B.;
RT   "Identification of three additional femAB-like open reading frames in
RT   Staphylococcus aureus.";
RL   FEMS Microbiol. Lett. 171:97-102(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [4]
RP   REGULATION BY MGRA.
RX   PubMed=12791130; DOI=10.1046/j.1365-2958.2003.03503.x;
RA   Ingavale S.S., Van Wamel W., Cheung A.L.;
RT   "Characterization of RAT, an autolysis regulator in Staphylococcus
RT   aureus.";
RL   Mol. Microbiol. 48:1451-1466(2003).
CC   -!- FUNCTION: Probably involved in peptidoglycan hydrolysis.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Repressed by MgrA.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD30323.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB015195; BAA33856.1; -; Genomic_DNA.
DR   EMBL; AF106851; AAD23962.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30323.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_499755.1; NC_007795.1.
DR   AlphaFoldDB; Q9ZNI1; -.
DR   SMR; Q9ZNI1; -.
DR   STRING; 93061.SAOUHSC_01219; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   PaxDb; 1280-SAXN108_1249; -.
DR   GeneID; 3919484; -.
DR   KEGG; sao:SAOUHSC_01219; -.
DR   PATRIC; fig|93061.5.peg.1117; -.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_060961_0_0_9; -.
DR   OrthoDB; 2195319at2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 3.10.350.10; LysM domain; 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   NCBIfam; TIGR01168; YSIRK_signal; 1.
DR   PANTHER; PTHR33734:SF39; CELL WALL HYDROLASE LYTN-RELATED; 1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   PROSITE; PS50911; CHAP; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..49
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..383
FT                   /note="Probable cell wall hydrolase LytN"
FT                   /id="PRO_0000227560"
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"
FT   CONFLICT        3
FT                   /note="V -> I (in Ref. 2; AAD23962)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="F -> S (in Ref. 2; AAD23962)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="L -> P (in Ref. 2; AAD23962)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="Q -> P (in Ref. 1; BAA33856)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  43183 MW;  2C4728F144643620 CRC64;
     MFVYYCKECF 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
//