ID   LYTB_STRPN              Reviewed;         658 AA.
AC   P59205; Q9Z4P7;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=SP_0965;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: Plays an important role in cell wall degradation and cell
CC       separation. {ECO:0000250}.
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}.
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DR   EMBL; AE005672; AAK75086.1; -; Genomic_DNA.
DR   PIR; E95111; E95111.
DR   RefSeq; WP_000757741.1; NC_003028.3.
DR   PDB; 4Q2W; X-ray; 1.65 A; A=375-658.
DR   PDBsum; 4Q2W; -.
DR   AlphaFoldDB; P59205; -.
DR   SMR; P59205; -.
DR   STRING; 170187.SP_0965; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   EnsemblBacteria; AAK75086; AAK75086; SP_0965.
DR   KEGG; spn:SP_0965; -.
DR   eggNOG; COG4193; Bacteria.
DR   eggNOG; COG5263; Bacteria.
DR   OMA; KESWFYL; -.
DR   PhylomeDB; P59205; -.
DR   Proteomes; UP000000585; 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; 7.
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; 13.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Hydrolase; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..658
FT                   /note="Putative endo-beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000012116"
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   STRAND          387..391
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          393..399
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          405..410
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          414..417
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          425..432
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          435..440
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           441..443
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          444..446
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   TURN            449..451
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          456..459
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          461..469
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          472..478
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          492..496
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   TURN            505..508
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           519..528
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   TURN            535..538
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           540..550
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           554..565
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   TURN            566..569
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           571..576
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           598..613
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           615..617
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   STRAND          625..628
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           630..633
FT                   /evidence="ECO:0007829|PDB:4Q2W"
FT   HELIX           639..653
FT                   /evidence="ECO:0007829|PDB:4Q2W"
SQ   SEQUENCE   658 AA;  76469 MW;  B625515006C9CB36 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
     YLKFDGKMAE KEWVYDSHSQ AWYYFKSGGY MTANEWIWDK ESWFYLKSDG KIAEKEWVYD
     SHSQAWYYFK SGGYMTANEW IWDKESWFYL KSDGKIAEKE WVYDSHSQAW YYFKSGGYMA
     KNETVDGYQL GSDGKWLGGK TTNENAAYYQ VVPVTANVYD SDGEKLSYIS QGSVVWLDKD
     RKSDDKRLAI TISGLSGYMK TEDLQALDAS KDFIPYYESD GHRFYHYVAQ NASIPVASHL
     SDMEVGKKYY SADGLHFDGF KLENPFLFKD LTEATNYSAE ELDKVFSLLN INNSLLENKG
     ATFKEAEEHY HINALYLLAH SALESNWGRS KIAKDKNNFF GITAYDTTPY LSAKTFDDVD
     KGILGATKWI KENYIDRGRT FLGNKASGMN VEYASDPYWG EKIASVMMKI NEKLGGKD