ID A0A0M8XKT2_9ACTN Unreviewed; 569 AA.
AC A0A0M8XKT2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:KOX06995.1};
GN ORFNames=ADL04_05305 {ECO:0000313|EMBL:KOX06995.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX06995.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOX06995.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX06995.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:KOX06995.1}.
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DR EMBL; LGDZ01000052; KOX06995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8XKT2; -.
DR PATRIC; fig|1519493.3.peg.1170; -.
DR Proteomes; UP000037702; Unassembled WGS sequence.
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 CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..219
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 225..549
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 59..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 569 AA; 60970 MW; 4C56FA08696CA1DA CRC64;
MGDGWAGDRS YVGRVTQHRL RRRGSARQVI RKRAVVAAAV VGTVALGTGV AVWASADGGG
GAAVSGARQP SPGRAAGPGQ PATASASPRP SPSRSYPLSQ TPRTIPAVRS HTPARGPGWK
PRHGERVVVS DPALADEGRL MAAELGLAYA GEKSDVRAGD VRLALGGGGG NRESYTLTVR
GGRVDISGPG EAGVFYGTRT LKQEVHGGGT APEGVVRDQP AKPVRGFMLD IARKPYSEAW
IEDRIRELGD LKYNELGLHF SDDQAFRIES SSHPEIVSPV HLTKAQVRRI VALADSRHIT
VVPEIDSPGH LGAVLAAHPD LQLRNVNGVA TRGAIDISKD ASARLVDDLL NEYAGLFTGG
QWHLGGDEYQ ALTVRDPQAS YPQLTAAARQ RYGAGGTVAD LATGWLDDRA ATVRAHHRTM
RAWNDGFFRG TSVQPAGDLQ VAYWTGKEIG ARPPAEYLSA GRKVLNYNDE YLYYVLGQPQ
TFVYPTGQRI YEQWNPRVLR GTTAVPARYD GQILGGSFAV WSDRPNAQTE AQVAAGIRMP
LRATAQKLWD ARTPALSWAG FRSLANRLG
//
