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Database: UniProt
Entry: C1KG54_STRMT
LinkDB: C1KG54_STRMT
Original site: C1KG54_STRMT 
ID   C1KG54_STRMT            Unreviewed;       568 AA.
AC   C1KG54;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=LytB {ECO:0000313|EMBL:ACO37163.1};
DE            EC=3.2.1.96 {ECO:0000313|EMBL:ACO37163.1};
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KYF33144.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:KYF33144.1};
GN   Name=lytB {ECO:0000313|EMBL:ACO37163.1};
GN   ORFNames=SMI10712_00819 {ECO:0000313|EMBL:KYF33144.1};
OS   Streptococcus mitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037 {ECO:0000313|EMBL:ACO37163.1};
RN   [1] {ECO:0000313|EMBL:ACO37163.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC10712 {ECO:0000313|EMBL:ACO37163.1};
RX   PubMed=19396958; DOI=10.1111/j.1574-6976.2009.00172.x;
RA   Hakenbeck R., Madhour A., Denapaite D., Bruckner R.;
RT   "Versatility of choline metabolism and choline-binding proteins in
RT   Streptococcus pneumoniae and commensal streptococci.";
RL   FEMS Microbiol. Rev. 33:572-586(2009).
RN   [2] {ECO:0000313|EMBL:KYF33144.1, ECO:0000313|Proteomes:UP000075618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10712 {ECO:0000313|EMBL:KYF33144.1,
RC   ECO:0000313|Proteomes:UP000075618};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; FJ824668; ACO37163.1; -; Genomic_DNA.
DR   EMBL; LROT01000028; KYF33144.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1KG54; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PATRIC; fig|28037.237.peg.1556; -.
DR   Proteomes; UP000075618; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; 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; 2.
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; 4.
DR   Pfam; PF19085; Choline_bind_2; 1.
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; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ACO37163.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACO37163.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..568
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002909773"
FT   REPEAT          250..271
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   DOMAIN          438..568
FT                   /note="Mannosyl-glycoprotein endo-beta-N-
FT                   acetylglucosamidase-like"
FT                   /evidence="ECO:0000259|SMART:SM00047"
SQ   SEQUENCE   568 AA;  65440 MW;  0BE68413D323480E CRC64;
     MKKLRFIFLA LLFFLARPES AMASDGTWQG KQYLKADGSQ AANEWVFDTH YQSWFYIKAD
     ANYAENEWLK QGDDYFYLKS GGYMAKSEWV EDKGVLYYLD QDGKMKRNAW LGASYVGATG
     AKVIEDWVYD SQYDAWFYIK ADGQHAEKEW LQIKGKDYYF KSGGYLLTSQ WIEQAYVSTS
     GAKVQQGWLF DKQYQSWFYI KENGNHADKE WIFENGHYYY LKSGGYMAAN EWILDKESWF
     YLKSDGKMAE KEWVYDSKNQ AWYYFKSGGY MAKNETIDGH QLGNDGKWNK ESKTSSDYYQ
     VLPVTANIYN ADGEKLSYIS QGSVVWLDKD RKSDDKRLAI TISGLSGYMK TEDLQALDAG
     KDFIPYYESD GHRFYHYVAQ NASIPVAAHL SDMEVGKKYY SADGLHFDGF NLENPFLFKD
     LTEATNYSAE DLDKVFSLLN INNSLLENKG STFKEAEEHY HINALYLLAH SALESDWGRS
     KIAKDKNNFF GITAYDTTPY LSAKTFDDVD KGILGATKWI KENYIDRGRT FLGNKASGMN
     VEYASDPYWG EKIASVMMKI NEKLGGKD
//
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