ID   A0A0B4R8W5_9BACL        Unreviewed;       698 AA.
AC   A0A0B4R8W5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=Plano_0481 {ECO:0000313|EMBL:AIY04446.1};
OS   Planococcus sp. PAMC 21323.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY04446.1, ECO:0000313|Proteomes:UP000031496};
RN   [1] {ECO:0000313|EMBL:AIY04446.1, ECO:0000313|Proteomes:UP000031496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY04446.1,
RC   ECO:0000313|Proteomes:UP000031496};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT   "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT   Antarctica.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP009129; AIY04446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4R8W5; -.
DR   STRING; 1526927.Plano_0481; -.
DR   KEGG; pln:Plano_0481; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_5_1_9; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000031496; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:AIY04446.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031496};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..698
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038879322"
FT   DOMAIN          31..116
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
SQ   SEQUENCE   698 AA;  75817 MW;  9FFFCC52E0E5D4BD CRC64;
     MKKMLLLPML ITTLIISSFY TGAEKTSAES FVTDLVILQN VPEVEVGTIA GSLQLEAVHL
     ADKGQYQLTR TNLSWHSTNK TVATVDLDGR VSVAGKPGKT FIHVTDGTYT DKVAIHVKPG
     AKTKGEKGKP TLIASVIKES GDRYQLIDRA IEKMTMEEKV GQMLMPDFRK WNGQNVTTLL
     PEIEQLVKEY HLGGVILFRE NVVTTEQTTK LVDDYQQAAE KHNLLMTIDQ EGGIVTRLQS
     GTDMPGNMAL GATRSTEITE NVGRAIGEEL SALGINMNFA PSFDINNNPD NPVIGVRSFG
     EKPELVADLG VAYTKGLQQT GTAATAKHFP GHGDTAVDSH LGLPSVPYDL ERLKAVELYP
     FQKAMEANID AIMTAHVTFP KIDDTKVISQ KDGTEINLPA TLSYKVLTEL MREDMGYEGV
     IFTDALNMQA IADHFGPVDA VIRAVNAGTD IVLMPVGLEQ VAAGLYEAVR SGEISQERID
     ASATRILSLK MKRGILKEES PVSLAEKTAN ALQVVGSEQH KQIEKQAAEK SITLVKNEGV
     LPLAPTPEEL LVVVGNSSSA ELYKEIKARH EQTVWIEATK PLTASQLETL NTAQAVIVGT
     STSSLSQRSP GSDQMKLINQ VIAESQAPVV GVAIRNPYDI MAYPEIDAYL TQYSFRTASY
     KAMAATIMGE LNPTGKLPVT IPNLAGEVFY EYGHSVSY
//