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Database: UniProt
Entry: A0A0R2A482_9LACO
LinkDB: A0A0R2A482_9LACO
Original site: A0A0R2A482_9LACO 
ID   A0A0R2A482_9LACO        Unreviewed;       374 AA.
AC   A0A0R2A482;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=FC26_GL001266 {ECO:0000313|EMBL:KRM61824.1};
OS   Paucilactobacillus vaccinostercus DSM 20634.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61824.1, ECO:0000313|Proteomes:UP000051733};
RN   [1] {ECO:0000313|EMBL:KRM61824.1, ECO:0000313|Proteomes:UP000051733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61824.1,
RC   ECO:0000313|Proteomes:UP000051733};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001231};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:KRM61824.1}.
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DR   EMBL; AYYY01000020; KRM61824.1; -; Genomic_DNA.
DR   RefSeq; WP_057778204.1; NZ_AYYY01000020.1.
DR   AlphaFoldDB; A0A0R2A482; -.
DR   STRING; 1423813.FC26_GL001266; -.
DR   PATRIC; fig|1423813.3.peg.1290; -.
DR   Proteomes; UP000051733; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051733}.
FT   DOMAIN          42..360
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          111..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  40836 MW;  15E2CC52A1A75B4B CRC64;
     MKKIIGGLLA FLAIFLVSGN IKASKKAPLS NHQLKTAITH MTLQQKIGQM YVSRVQTTPK
     DTVATLTKYQ LGAIILFGPD FENQTKSQFK QRITGYQKAV QIPLLVSTDQ EGGDVSRLSS
     NPKLTHQRSF PSPQTTYQKD GLQATIKEAK QTAKILHGLG INWNFAPVAD VTDDSNSFIY
     ARTLGTTFSK TASYIKKVVP AIQHQQVATS LKHFPGYGSA ADTHTGFAST TRSLADFEAN
     DFLTFKAGIQ SGADSILVSH IVMTAVDPDL PASLSPKVHQ LLRKQLKFNG VIVTDDLAMG
     AITKYAQQHH VSPDLLAVEA GNDMIMSDHY KTGIPAIAQA VQSGQISEHQ INQSVYRILT
     MKNKLHLLAK NQLP
//
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