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 24-JAN-2024, entry version 119. 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; Bacillota; 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=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta- CC D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl- CC [protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]- CC beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L- CC asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603, CC Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248, CC ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_010976495.1; NC_003098.1. DR PDB; 7PJ3; X-ray; 1.43 A; AAA=429-702. DR PDB; 7PJ4; X-ray; 1.25 A; AAA=429-702. DR PDB; 7PJ5; X-ray; 1.55 A; AAA=429-702. DR PDB; 7PJ6; X-ray; 1.30 A; AAA=429-702. DR PDB; 7PL2; X-ray; 2.98 A; A=24-428. DR PDB; 7PL3; X-ray; 1.78 A; AA=429-702. DR PDB; 7PL5; X-ray; 1.99 A; AAA/BBB=24-208. DR PDB; 7POD; X-ray; 1.50 A; A=429-702. DR PDBsum; 7PJ3; -. DR PDBsum; 7PJ4; -. DR PDBsum; 7PJ5; -. DR PDBsum; 7PJ6; -. DR PDBsum; 7PL2; -. DR PDBsum; 7PL3; -. DR PDBsum; 7PL5; -. DR PDBsum; 7POD; -. DR AlphaFoldDB; P59206; -. DR SMR; P59206; -. DR STRING; 171101.spr0867; -. DR CAZy; GH73; Glycoside Hydrolase Family 73. 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 Gene3D; 1.10.530.10; -; 1. DR Gene3D; 2.10.270.10; Cholin Binding; 2. DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 5. DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat. DR InterPro; IPR041074; LytB_SH3. DR InterPro; IPR040742; LytB_WW-like. DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom. DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1. DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1. DR Pfam; PF01473; Choline_bind_1; 9. DR Pfam; PF19085; Choline_bind_2; 2. DR Pfam; PF01832; Glucosaminidase; 1. DR Pfam; PF18342; LytB_SH3; 1. DR Pfam; PF17890; WW_like; 1. DR SMART; SM00047; LYZ2; 1. DR SUPFAM; SSF69360; Cell wall binding repeat; 2. DR PROSITE; PS51170; CW; 15. PE 1: Evidence at protein level; KW 3D-structure; Cell wall biogenesis/degradation; Direct protein sequencing; KW Hydrolase; 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" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 49..52 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 125..130 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 131..134 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 192..195 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 236..242 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 261..265 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 295..300 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 301..304 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 345..348 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 362..366 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 368..374 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 383..388 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 389..392 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 393..398 FT /evidence="ECO:0007829|PDB:7PL2" FT TURN 399..401 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 406..409 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:7PL2" FT STRAND 432..435 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 437..443 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 449..454 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 458..461 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 469..476 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 479..484 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 485..487 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:7POD" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 505..513 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 516..522 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 536..540 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 549..552 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 563..572 FT /evidence="ECO:0007829|PDB:7POD" FT TURN 579..582 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 584..594 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 598..609 FT /evidence="ECO:0007829|PDB:7POD" FT TURN 610..613 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 615..620 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 633..636 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 643..657 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 659..661 FT /evidence="ECO:0007829|PDB:7POD" FT STRAND 669..672 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 674..677 FT /evidence="ECO:0007829|PDB:7POD" FT HELIX 683..697 FT /evidence="ECO:0007829|PDB:7POD" 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 //