ID   LYTD_BACSU              Reviewed;         880 AA.
AC   P39848;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Beta-N-acetylglucosaminidase;
DE            EC=3.2.1.96;
DE   AltName: Full=Cell wall-associated polypeptide 90;
DE            Short=CWBP90;
DE   Flags: Precursor;
GN   Name=lytD; Synonyms=cwlG; OrderedLocusNames=BSU35780;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=7934877; DOI=10.1111/j.1365-2958.1994.tb01040.x;
RA   Margot P., Maueel C., Karamata D.;
RT   "The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall
RT   hydrolase not involved in vegetative cell autolysis.";
RL   Mol. Microbiol. 12:535-545(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP   REGULATION BY SIGD.
RC   STRAIN=168 / AC327;
RX   PubMed=7581999; DOI=10.1099/13500872-141-10-2391;
RA   Rashid M.H., Mori M., Sekiguchi J.;
RT   "Glucosaminidase of Bacillus subtilis: cloning, regulation, primary
RT   structure and biochemical characterization.";
RL   Microbiology 141:2391-2404(1995).
RN   [3]
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   [4]
RP   PROTEIN SEQUENCE OF N-TERMINUS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / AC327;
RX   PubMed=8405954; DOI=10.1111/j.1574-6968.1993.tb06438.x;
RA   Rashid M.H., Kuroda A., Sekiguchi J.;
RT   "Bacillus subtilis mutant deficient in the major autolytic amidase and
RT   glucosaminidase is impaired in motility.";
RL   FEMS Microbiol. Lett. 112:135-140(1993).
RN   [5]
RP   SUBCELLULAR LOCATION, INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=11987133;
RX   DOI=10.1002/1615-9861(200205)2:5<591::aid-prot591>3.0.co;2-8;
RA   Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
RT   "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
RT   approach.";
RL   Proteomics 2:591-602(2002).
CC   -!- FUNCTION: Cell wall hydrolase not involved in cell autolysis,
CC       competence, sporulation or germination. It hydrolyzes the beta-1,4
CC       glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl
CC       residues in the glycan chain. {ECO:0000269|PubMed:7581999,
CC       ECO:0000269|PubMed:7934877}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC         mannose glycopeptides and glycoproteins containing the
CC         -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC         remains attached to the protein, the rest of the oligosaccharide is
CC         released intact.; EC=3.2.1.96;
CC   -!- ACTIVITY REGULATION: Inhibited by diethyl pyrocarbonate, slightly by
CC       EDTA. Not inhibited by PMSF, diisopropyl fluorophosphate, 2-
CC       mercaptoethanol or N-ethylmaleimide. {ECO:0000269|PubMed:7581999}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11987133}. Secreted,
CC       cell wall {ECO:0000269|PubMed:11987133}.
CC   -!- INDUCTION: In stationary phase (PubMed:11987133); under control of SigD
CC       (PubMed:7581999). {ECO:0000269|PubMed:11987133,
CC       ECO:0000269|PubMed:7581999}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no motility changes
CC       on swarm plates; however in combination with an amidase deletion (lytC,
CC       AC Q02114) greatly reduced motility is seen.
CC       {ECO:0000269|PubMed:8405954}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
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DR   EMBL; U02562; AAA67857.1; -; Genomic_DNA.
DR   EMBL; D45048; BAA08089.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15595.1; -; Genomic_DNA.
DR   PIR; S60137; S60137.
DR   RefSeq; NP_391459.1; NC_000964.3.
DR   RefSeq; WP_003243594.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39848; -.
DR   SMR; P39848; -.
DR   STRING; 224308.BSU35780; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; P39848; -.
DR   PRIDE; P39848; -.
DR   EnsemblBacteria; CAB15595; CAB15595; BSU_35780.
DR   GeneID; 936822; -.
DR   KEGG; bsu:BSU35780; -.
DR   PATRIC; fig|224308.179.peg.3873; -.
DR   eggNOG; COG4193; Bacteria.
DR   OMA; WAYKQVN; -.
DR   BioCyc; BSUB:BSU35780-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF08239; SH3_3; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   SMART; SM00287; SH3b; 1.
DR   PROSITE; PS51781; SH3B; 1.
DR   PROSITE; PS51724; SPOR; 3.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:8405954"
FT   CHAIN           28..880
FT                   /note="Beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000012118"
FT   DOMAIN          70..149
FT                   /note="SPOR 1"
FT   DOMAIN          150..229
FT                   /note="SPOR 2"
FT   DOMAIN          230..311
FT                   /note="SPOR 3"
FT   REPEAT          439..473
FT                   /note="1"
FT   REPEAT          479..513
FT                   /note="2"
FT   DOMAIN          630..700
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
SQ   SEQUENCE   880 AA;  95554 MW;  2A912A478FCFC1D1 CRC64;
     MKKRLIAPML LSAASLAFFA MSGSAQAAAY TDYSLYKVEP SNTFSTESQA SQAVAKLEKD
     TGWDASYQAS GTTTTYQISA SGIHSESEAK AILSGLAKQT SITGTSSPVG SKQPYVTISS
     GAISGEKQAN TILAKLKQET GVAGAVKAYG AAQPYMNVMT SDIADETKVK ALIQSLAKQT
     GIKSSYQPIT HTVSVTTIQS GTIVGDSRAA QIKNAFQKES GLQASLKETV KGQAYYTFTT
     AAISGEANAK TLLQQLKQST GITGSYKSIN QKTTVESYNV QSAYFKGLST VKDAISQIKK
     NTGVSGSYQQ VGKSTSYTVN MKGITKQQLQ KIDTFFKKKK WHYTSSSVKK TTTSAAYQIT
     TAKILGEQQA NKAAAFFAQK KVKAAKTAAG STAENQYQLI SEETSDQAKV TKGLNILKKN
     QLSASAKSVK KQIADTFKIT TESLLDQTKV NQALTFFKSN HISVASQKTG QTAASSYQIT
     TEAIISQEEI DRVLTFFKQN HIAVTTSKTG QTAYTQYKIV TTQLSSKTAL NNGLTYLKSK
     SVTPSYTTKS NTLYKISVNE QFTGNDTAAA ASTKLKQLYG WTSSIVKIKN GPQIMKTNYN
     LSLRDMVQKQ MTVSPQTDGA AYVSLTYINT ATSTVTADVL NIRSTPEVSP TNVIGQFKKG
     DKVKVIGQIN GWAKINLGWR NASSDEVVQY VDPNNFSRDS KYYFQFLKLS QTAGLSVTEV
     NQKVLAGKGI LTGRAKAFID AANQYSINEL YLISHALLET GNGTSALANG LTYNGKTVYN
     MYGIGAYDSN PNYYGAKYAY EQGWFTPEAA IIGGAKFIGS SYIHNTAYNQ DTLYKMRWSA
     TATHQYATDI GWAYKQVNRM YSLYSLLDGY TLYFDVPEYR