ID A0A075R6G8_BRELA Unreviewed; 692 AA.
AC A0A075R6G8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=BRLA_c027270 {ECO:0000313|EMBL:AIG27046.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27046.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG27046.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27046.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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; CP007806; AIG27046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075R6G8; -.
DR STRING; 1042163.BRLA_c027270; -.
DR KEGG; blr:BRLA_c027270; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_5_1_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase 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; 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; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:AIG27046.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..489
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 532..684
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 692 AA; 76128 MW; D3280B02F4103FAF CRC64;
MKRKHIFAYT SVSLILLACF FIPFLSKDRA DTMRTTTVST THPTDLLLAQ NLPETPKTYP
ATQIQLQALH TYADGRLSKV QANISWSSSN PLVATVTREG LLTIQDKLGQ TVVLVSDGTY
HDRLVLEKTD KNTVKVITEP QAKYDVISRL LATMSVADKV GQTLMPSFSM YGGKPFQELT
PEIANMIKRL QLGGIILFKD SLNETKQIVQ LTTALQQSQH KFGLLIGTDQ EGGIVSRLKQ
GTNMPGNMAL GATRNPKLAY QAGQVMADEL LSLGINLDFA PTIDVNNNSK NPVIGVRSYG
ESPQLVAEMG TSFIAGMQDA GVVASAKHFP GHGNTSVDSH VGLPVISYGK KQLEQVEFIP
FRQAIKQGVD SVLVAHIAFP QLEPTKVESH QKDKSIYLPA TLSPKLVQGL LRKEFGYDGL
VITDAMDMGG ITQHFETVDA SIRAMNAGAD IILMPPDVEK VSLGMQKAVM SGTIKKERLD
EAVRRILTVK MRRGIFAQEQ MPHVPILQQI AEKSITSPAH KQVERAIAEQ SITVVKNDRI
LPLHPSPEQR IAVIGSRYTS EMTRAFQKYH QNTVAIKLNH VLKAEQQQQI DRADILMVLP
DSFAGGLQPV NQLIKKLIDQ KQKPVIMIST RNPYQLTDFQ KVPTYVAQYG NADASFQATA
AILFGEGKSK GKLPVTIYDT KGNILYPYGH GL
//
