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Database: UniProt
Entry: T0TU94_9STRE
LinkDB: T0TU94_9STRE
Original site: T0TU94_9STRE 
ID   T0TU94_9STRE            Unreviewed;       345 AA.
AC   T0TU94;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EQC74636.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:EQC74636.1};
DE   Flags: Fragment;
GN   ORFNames=HSISS2_1400 {ECO:0000313|EMBL:EQC74636.1};
OS   Streptococcus sp. HSISS2.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316411 {ECO:0000313|EMBL:EQC74636.1};
RN   [1] {ECO:0000313|EMBL:EQC74636.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISS2 {ECO:0000313|EMBL:EQC74636.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC       {ECO:0000256|ARBA:ARBA00010266}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC74636.1}.
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DR   EMBL; ASKC01000061; EQC74636.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0TU94; -.
DR   HOGENOM; CLU_805434_0_0_9; -.
DR   Proteomes; UP000015938; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 2.60.40.3760; -; 1.
DR   InterPro; IPR013688; GBS_Bsp-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; PF08481; GBS_Bsp-like; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   PRINTS; PR01002; FLGFLGJ.
DR   SMART; SM00047; LYZ2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EQC74636.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          113..269
FT                   /note="Mannosyl-glycoprotein endo-beta-N-
FT                   acetylglucosamidase-like"
FT                   /evidence="ECO:0000259|SMART:SM00047"
FT   REGION          18..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         345
FT                   /evidence="ECO:0000313|EMBL:EQC74636.1"
SQ   SEQUENCE   345 AA;  37649 MW;  BAAE74C40DC9054F CRC64;
     MLFLGTCGVT AGADEVMENP SNANATKPIS KEQTTSSTTV SNSETVPKGE KQTSEVTFEN
     SYTTVTAEAS FNTVDQNSTE TVFQDKADYI VASNLTNNSV TRSAYQGPDS VDSTSESQSH
     FLNAIKQGAM DGAKEGVLPS ITAAQAILES GWGNSSLAQA PNHNLFGIKD SDDWGGDTVV
     VPTQEYLNGR YITINAAFRK YSSWNDSVVD HAKFFTSTEW RKNNYRKVIN ATDYRTAAQE
     LKNAGYATDP GYAGKLIRLI EAYKLYEWDE ESNTAINISD NPIEIQNNPK AELAITGLNN
     ATGSYDLVIS NLVAPYGFKE VLVPTWSEKN GQDDIIWYKA AKQAN
//
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