ID   LYTG_BACSU              Reviewed;         282 AA.
AC   O32083;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Exo-glucosaminidase LytG;
DE            EC=3.2.1.-;
DE   AltName: Full=Autolysin LytG;
DE   AltName: Full=Exo-beta-N-acetylglucosaminidase LytG;
DE   AltName: Full=Peptidoglycan hydrolase LytG;
DE   Flags: Precursor;
GN   Name=lytG; Synonyms=yubE; OrderedLocusNames=BSU31120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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).
RN   [2]
RP   FUNCTION, CHARACTERIZATION, COFACTOR, SUBCELLULAR LOCATION, AND
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=168;
RX   PubMed=12525152; DOI=10.1021/bi020498c;
RA   Horsburgh G.J., Atrih A., Williamson M.P., Foster S.J.;
RT   "LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major
RT   active glucosaminidase.";
RL   Biochemistry 42:257-264(2003).
CC   -!- FUNCTION: Is the major glucosaminidase responsible for peptidoglycan
CC       structural determination during vegetative growth. Catalyzes the
CC       hydrolysis of 1,4-beta-linkages between N-acetyl-D-glucosamine and N-
CC       acetylmuramic acid residues in peptidoglycan. Acts processively from
CC       the ends of the glycan strands. Also plays a role in motility,
CC       chemotaxis and cell division. {ECO:0000269|PubMed:12525152}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12525152};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimal pH is about 5.7.;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:12525152}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth.
CC   -!- INDUCTION: Expressed under control of sigma-A RNA polymerase.
CC       {ECO:0000269|PubMed:12525152}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15090.1; -; Genomic_DNA.
DR   PIR; H70006; H70006.
DR   RefSeq; NP_390990.1; NC_000964.3.
DR   RefSeq; WP_003228938.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32083; -.
DR   SMR; O32083; -.
DR   STRING; 224308.BSU31120; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; O32083; -.
DR   PRIDE; O32083; -.
DR   EnsemblBacteria; CAB15090; CAB15090; BSU_31120.
DR   GeneID; 937146; -.
DR   KEGG; bsu:BSU31120; -.
DR   PATRIC; fig|224308.179.peg.3372; -.
DR   eggNOG; COG1705; Bacteria.
DR   InParanoid; O32083; -.
DR   OMA; KPSYNFF; -.
DR   PhylomeDB; O32083; -.
DR   BioCyc; BSUB:BSU31120-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.170; -; 1.
DR   InterPro; IPR025987; GW_dom.
DR   InterPro; IPR038200; GW_dom_sf.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF13457; GW; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   PROSITE; PS51780; GW; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Glycosidase; Hydrolase;
KW   Magnesium; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..282
FT                   /note="Exo-glucosaminidase LytG"
FT                   /id="PRO_0000012119"
FT   DOMAIN          203..281
FT                   /note="GW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
SQ   SEQUENCE   282 AA;  31901 MW;  DEA15D5AFA73F327 CRC64;
     MARKKLKKRK LLISLFFLVS IPLALFVLAT TLSKPIEISK ETEEIDEQQV FIDSLSGHAQ
     ILYEKYHVLP SITIAQAILE SDWGNSELAA KANNLFGVKG NYKGHHVTME TDEVEKGKRK
     TIRAKFRKYS TFFESMDDHA QLFVRGTSWN KKKYKPVLEA GNYKEAATAL QTSGYATDPD
     YADKISAIVE KYDLDEYDEV NPSLKSVDLN ASIKDSAVQD VWSKPSTDDR SIRLTSAQSY
     VGKDIKVVSK KQKGQSVWYQ FQINDKLIGW IDDSAVEIKE AT