ID F2QDZ3_STROU Unreviewed; 750 AA.
AC F2QDZ3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=LytB endo-beta-N-acetylglucosaminidase {ECO:0000313|EMBL:CBZ00862.1};
GN Name=lytB {ECO:0000313|EMBL:CBZ00862.1};
GN OrderedLocusNames=SOR_1204 {ECO:0000313|EMBL:CBZ00862.1};
OS Streptococcus oralis (strain Uo5).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=927666 {ECO:0000313|EMBL:CBZ00862.1, ECO:0000313|Proteomes:UP000008131};
RN [1] {ECO:0000313|EMBL:CBZ00862.1, ECO:0000313|Proteomes:UP000008131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uo5 {ECO:0000313|EMBL:CBZ00862.1,
RC ECO:0000313|Proteomes:UP000008131};
RX PubMed=21460080; DOI=10.1128/JB.00321-11;
RA Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., Maurer P.,
RA Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT "Genome of Streptococcus oralis strain Uo5.";
RL J. Bacteriol. 193:2888-2889(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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DR EMBL; FR720602; CBZ00862.1; -; Genomic_DNA.
DR AlphaFoldDB; F2QDZ3; -.
DR KEGG; sor:SOR_1204; -.
DR eggNOG; COG4193; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_427450_0_0_9; -.
DR Proteomes; UP000008131; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 4.
DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 3.
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; 5.
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; 3.
DR PROSITE; PS51170; CW; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..750
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003288662"
FT REPEAT 414..433
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 620..750
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 750 AA; 86384 MW; B08EF80895564904 CRC64;
MKRWKVALVS AGLLGCFFTV VETARAEEGT WQGKTYLKAD GKPATNQWIF DQTQQAWFYL
TADGNRAENG WLTVAGKDYY FNEAGKLATK TWIDQYYVTE SGAKAKEQWV FNQEQESWYY
LKSNGQKAQN EWIQQGQEKY YLKADGKMAK DEWITQGENQ YYINSQGKML KNAWLGKNYI
SENGNKVKQA WIYDDNYSSW FYLQQDGTYA ENGWLTIDGK DYHFKSGGYL STERWIDRFY
VAKSGAKLKS EWLFDKNYDS WFYLKADGSY AEKGWETIKE KDYHFKPGGY LSTERWIDRF
YVAKSGAKLK SEWLFDKNYN SWFYLKADGT YAEKGWQTIK GKDYHFKSGG YLSTETWIDR
SYVTSSGAKA GKGWLFDKNF NSWFYINSDG NYANKEWLWD NGYYYLKSGG YMATNEWVWY
KNNWFYLKSN GKMAEKELIY DSSDQSWYYL KSGGYMARNE TVDGHTLDAS GRWHVADKTK
YYKVKPITAY VYSASGEILS YINQGSIVSL DSSTRKGGRL AVSISGLSGY MNQSDLTAVD
EGSEFIPHYT SDGKFLYHEL SPYTSIKVAP HTSAMVIGKK YYSTDGEHFD GFTIKNPFLY
KNLREPSNYS AAELDKLYSM MNLQDSPLAG KGATFKEAEE RYGVNALYLM AHSALESAWG
RSQIARDKNN FFGIAAYDTS PYLSAKSFDN VDKGILGAAK WIRENYIDYG RDHLGNKATG
MNVRYASDPY WGEKIASIMM TINSRLGGKD
//
