ID A0A1Q5JF98_9ACTN Unreviewed; 540 AA.
AC A0A1Q5JF98;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:OKJ67977.1};
GN ORFNames=AMK29_07990 {ECO:0000313|EMBL:OKJ67977.1};
OS Streptomyces sp. CB02261.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ67977.1, ECO:0000313|Proteomes:UP000186742};
RN [1] {ECO:0000313|EMBL:OKJ67977.1, ECO:0000313|Proteomes:UP000186742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02261 {ECO:0000313|EMBL:OKJ67977.1,
RC ECO:0000313|Proteomes:UP000186742};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(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:OKJ67977.1}.
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DR EMBL; LIVX01000002; OKJ67977.1; -; Genomic_DNA.
DR RefSeq; WP_073809805.1; NZ_LIVX01000002.1.
DR AlphaFoldDB; A0A1Q5JF98; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000186742; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039075661"
FT DOMAIN 73..189
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 196..521
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 32..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 540 AA; 58345 MW; 036438DE133FA4BA CRC64;
MMRYSIRGPH KGPALLATAV ALATVAACSN GTPTGAPPPP TPSGGTSASA APTSAPPSPT
PTPTRTYPLS TAPRTIPAVR DHEAARGPGW KPTPTAGIVI AAGSEGLADE ARMLAGELKI
AYRGAVAARA GDVELALGGK GSPESYTLIT RDDRVRITGP DQAGVFYGTR TLKQSVNGSG
AMPEGTVVDT PAKPQRGLNL DIARKFFTAE WIEARLREMA DLKLNQFGLH FSDDQGFRIA
SDTHPEIVSD QHLTKAEVRR ILALAQSLHI TVVPEIDSPG HLGAVLRAYP ELRLLNVQGT
PRQGAIDISK PASARLVDEL LREYAALFPG GWFHVGADEY QALTVRSPEA SYPQLASAAR
QKYGPDARVQ DLAEGWLNDR AAVVRGTDKV AKAWNDGFFR GGVVNADKGI EVEYWTGKEI
GVRPPVEYLA EGRKVVNLND EYLYYVLGEP NQFTYPTGRR IYEQWTPRVL RGTTPVPARY
DPQILGARFA VWCDLSRAQT QAQVADGIRL PLTALAQKVW DPARPTLTWD QFRALAAEVR
//