ID   LYTB_STRR6              Reviewed;         702 AA.
AC   P59206; Q9Z4P7;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative endo-beta-N-acetylglucosaminidase;
DE            EC=3.2.1.96;
DE   AltName: Full=Murein hydrolase;
DE   Flags: Precursor;
GN   Name=lytB; OrderedLocusNames=spr0867;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-30.
RX   PubMed=10096093; DOI=10.1046/j.1365-2958.1999.01238.x;
RA   Garcia P., Gonzalez M.P., Garcia E., Lopez R., Garcia J.L.;
RT   "LytB, a novel pneumococcal murein hydrolase essential for cell
RT   separation.";
RL   Mol. Microbiol. 31:1275-1281(1999).
RN   [2]
RP   SEQUENCE REVISION.
RA   Garcia J.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
CC   -!- FUNCTION: Plays an important role in cell wall degradation and cell
CC       separation.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK99671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ010312; CAA09078.2; -; Genomic_DNA.
DR   EMBL; AE007317; AAK99671.1; ALT_INIT; Genomic_DNA.
DR   PIR; C97980; C97980.
DR   RefSeq; NP_358461.1; NC_003098.1.
DR   RefSeq; WP_000757725.1; NC_003098.1.
DR   AlphaFoldDB; P59206; -.
DR   SMR; P59206; -.
DR   STRING; 171101.spr0867; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PRIDE; P59206; -.
DR   EnsemblBacteria; AAK99671; AAK99671; spr0867.
DR   KEGG; spr:spr0867; -.
DR   PATRIC; fig|171101.6.peg.955; -.
DR   eggNOG; COG4193; Bacteria.
DR   eggNOG; COG5263; Bacteria.
DR   HOGENOM; CLU_427450_0_0_9; -.
DR   PHI-base; PHI:3153; -.
DR   Proteomes; UP000000586; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR   InterPro; IPR041074; LytB_WW.
DR   InterPro; IPR040742; LytB_WW-like.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   Pfam; PF01473; Choline_bind_1; 9.
DR   Pfam; PF19085; Choline_bind_2; 2.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF18342; LytB_WW; 1.
DR   Pfam; PF17890; WW_like; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   PROSITE; PS51170; CW; 15.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10096093"
FT   CHAIN           24..702
FT                   /note="Putative endo-beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000012117"
FT   REPEAT          42..63
FT                   /note="Cell wall-binding 1"
FT   REPEAT          65..84
FT                   /note="Cell wall-binding 2"
FT   REPEAT          86..105
FT                   /note="Cell wall-binding 3"
FT   REPEAT          124..145
FT                   /note="Cell wall-binding 4"
FT   REPEAT          147..166
FT                   /note="Cell wall-binding 5"
FT   REPEAT          185..206
FT                   /note="Cell wall-binding 6"
FT   REPEAT          208..227
FT                   /note="Cell wall-binding 7"
FT   REPEAT          229..248
FT                   /note="Cell wall-binding 8"
FT   REPEAT          250..271
FT                   /note="Cell wall-binding 9"
FT   REPEAT          273..292
FT                   /note="Cell wall-binding 10"
FT   REPEAT          294..315
FT                   /note="Cell wall-binding 11"
FT   REPEAT          317..336
FT                   /note="Cell wall-binding 12"
FT   REPEAT          338..359
FT                   /note="Cell wall-binding 13"
FT   REPEAT          361..380
FT                   /note="Cell wall-binding 14"
FT   REPEAT          382..403
FT                   /note="Cell wall-binding 15"
SQ   SEQUENCE   702 AA;  81900 MW;  84B6536E75301FE5 CRC64;
     MKKVRFIFLA LLFFLASPEG AMASDGTWQG KQYLKEDGSQ AANEWVFDTH YQSWFYIKAD
     ANYAENEWLK QGDDYFYLKS GGYMAKSEWV EDKGAFYYLD QDGKMKRNAW VGTSYVGATG
     AKVIEDWVYD SQYDAWFYIK ADGQHAEKEW LQIKGKDYYF KSGGYLLTSQ WINQAYVNAS
     GAKVQQGWLF DKQYQSWFYI KENGNYADKE WIFENGHYYY LKSGGYMAAN EWIWDKESWF
     YLKFDGKIAE KEWVYDSHSQ AWYYFKSGGY MAANEWIWDK ESWFYLKFDG KMAEKEWVYD
     SHSQAWYYFK SGGYMTANEW IWDKESWFYL KSDGKIAEKE WVYDSHSQAW YYFKSGGYMT
     ANEWIWDKES WFYLKSDGKM AEKEWVYDSH SQAWYYFKSG GYMAKNETVD GYQLGSDGKW
     LGGKATNKNA AYYQVVPVTA NVYDSDGEKL SYISQGSVVW LDKDRKSDDK RLAITISGLS
     GYMKTEDLQA LDASKDFIPY YESDGHRFYH YVAQNASIPV ASHLSDMEVG KKYYSADGLH
     FDGFKLENPF LFKDLTEATN YSAEELDKVF SLLNINNSLL ENKGATFKEA EEHYHINALY
     LLAHSALESN WGRSKIAKDK NNFFGITAYD TTPYLSAKTF DDVDKGILGA TKWIKENYID
     RGRTFLGNKA SGMNVEYASD PYWGEKIASV MMKINEKLGG KD