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Database: UniProt
Entry: A0A1E7K9P6_9ACTN
LinkDB: A0A1E7K9P6_9ACTN
Original site: A0A1E7K9P6_9ACTN 
ID   A0A1E7K9P6_9ACTN        Unreviewed;       546 AA.
AC   A0A1E7K9P6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:OEV00649.1};
GN   ORFNames=AN217_25835 {ECO:0000313|EMBL:OEV00649.1};
OS   Streptomyces qinglanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV00649.1, ECO:0000313|Proteomes:UP000175829};
RN   [1] {ECO:0000313|EMBL:OEV00649.1, ECO:0000313|Proteomes:UP000175829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV00649.1,
RC   ECO:0000313|Proteomes:UP000175829};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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:OEV00649.1}.
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DR   EMBL; LJGV01000022; OEV00649.1; -; Genomic_DNA.
DR   RefSeq; WP_026004849.1; NZ_LJGV01000022.1.
DR   AlphaFoldDB; A0A1E7K9P6; -.
DR   PATRIC; fig|943816.4.peg.4754; -.
DR   Proteomes; UP000175829; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000175829};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..546
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009196324"
FT   DOMAIN          70..194
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          200..527
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          37..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        343
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   546 AA;  59313 MW;  2BDDCE9090711885 CRC64;
     MGRNWSKKSG RTAMGALRRS GAPLALTLAV SLLGLTACGG DGDGGGDSPS ASGSGSAQPP
     KGPDRLGPAP SAVPSVRQWQ AVRGPGWQRT DRTRVVPAAD SLRDEAKLLA DELKVPVAKA
     PSRTGDIELK RGEDGGKSPG GKVNGGPESY RLVSKDGKVT ITGGGDAGVF YGTRTLLQTW
     RAQGRFAEGT VADAPDRPQR GFSLDIARKN FSADWIKARI RQMGDLKLNQ LQLHLSDDQA
     FRIESETHPE IVSDPHLTKA QVRDIVDLAA SRHITVIPEI DSPGHLGAVL KAHPDLQLRS
     ASGATPRGAI DISKPAAAKL VDELLVEFAD LFPGKWAHAG GDEYQALMTQ NPEQTYPGLA
     KKAREKFGDK ATVQDLATAW LNDRASTLDK QGKIPQVWND GMHRGGVVEP NKPREVAYWT
     GRETGEREPS EYLKEGWKVV NLNDEYLYYV LGQPNNFTYP TGRRIYEEWT PAVVRGTEPV
     PDKWAGRDRI LGGRFAVWGD LADAQTTGQV ARGIRLPLAA TAQKLWDPQR PERSWDDFVK
     LVDKVD
//
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