ID   XLYB_BACSU              Reviewed;         317 AA.
AC   O34391;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase XlyB;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   Flags: Precursor;
GN   Name=xlyB; Synonyms=yjpB; OrderedLocusNames=BSU12460;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   da Silva E., Karamata D.;
RT   "Sequencing and characterisation of the region comprising xlyB, the second
RT   lytic enzyme of the defective prophage PBSX of Bacillus subtilis.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Autolysins are involved in some important biological
CC       processes such as cell separation, cell-wall turnover, competence for
CC       genetic transformation, formation of the flagella and sporulation.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF034138; AAB87514.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13103.1; -; Genomic_DNA.
DR   PIR; B69734; B69734.
DR   RefSeq; NP_389128.1; NC_000964.3.
DR   RefSeq; WP_003244876.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34391; -.
DR   SMR; O34391; -.
DR   STRING; 224308.BSU12460; -.
DR   PaxDb; O34391; -.
DR   EnsemblBacteria; CAB13103; CAB13103; BSU_12460.
DR   GeneID; 936464; -.
DR   KEGG; bsu:BSU12460; -.
DR   PATRIC; fig|224308.179.peg.1347; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   eggNOG; COG5632; Bacteria.
DR   InParanoid; O34391; -.
DR   OMA; IEICYSK; -.
DR   PhylomeDB; O34391; -.
DR   BioCyc; BSUB:BSU12460-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR   GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   Gene3D; 3.40.80.10; -; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   SUPFAM; SSF55846; SSF55846; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Competence; Hydrolase;
KW   Reference proteome; Secreted; Signal; Sporulation.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000250"
FT   CHAIN           40..317
FT                   /note="N-acetylmuramoyl-L-alanine amidase XlyB"
FT                   /id="PRO_0000006458"
FT   DOMAIN          40..142
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          177..221
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
SQ   SEQUENCE   317 AA;  33863 MW;  955DF80EE6DD0757 CRC64;
     MSIPVKKNLV SEAKYALKCP NAMSAEYITI HNTANDASAA NEISYMIGNT SSTSFHFAVD
     DQEVIQGLPL NRNAWHTGDG TNGPGNRKSI GVEICYSKSG GPKYEAAEAL AISFVAQLLK
     ERGWGIDRVR KHQDWSGKYC PHRILSEGRW DQVKAAIEKE LNGGVSAKKA AVSSSASEYH
     VKKGDTLSGI AASHGASVKT LQSINHITDP NHIKIGQVIK LPQTASASKS HAASSYPLPS
     GVIKVTSPLT QGTKVKQVQT ALAALYFYPD KGAKNHGVDG VYGPKTANAV KRFQSVSGLT
     ADGIYGPKTK AKMEEKL