ID A0A0L0JKC0_9ACTN Unreviewed; 642 AA.
AC A0A0L0JKC0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:KND25820.1};
GN ORFNames=IQ63_39585 {ECO:0000313|EMBL:KND25820.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND25820.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KND25820.1}.
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DR EMBL; JPPY01000217; KND25820.1; -; Genomic_DNA.
DR RefSeq; WP_050374926.1; NZ_KQ257834.1.
DR AlphaFoldDB; A0A0L0JKC0; -.
DR PATRIC; fig|42234.21.peg.8145; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000037151; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..642
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005541525"
FT DOMAIN 30..173
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 180..491
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT REGION 23..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 68796 MW; 47FF6676358E4F17 CRC64;
MGLRLTVAAL VVSCMFATPP PASATDATLP QVTPQPQQLT ANGTPLTVPP RVHIRTAGQQ
DRPTHDLVVS TLRAAGATDI DEAPLPTTGV DPADLTVVIG GIQDTRVTDA LRAVGGQVPA
TLPAEGYALA SRAAPGGGSI ILAGADASGT YYAAQTLRQL ASGTSLAAVS VVDHPLMPLR
GAIEGFYGSP WTHAERLDQL AFYGALKMNT YLYAPKDDPY HRERWRDPYP PQLLAQLGEL
VRQATDHHVR FTFALSPGVS ICYSSAADRT ALEAKLQAVY DLGVRSFSVP LDDISYTRWN
CTADQTAYGA PSQQSAARAQ VGLLNALQRQ FLAARPGTQP LQMVPTEYGD VTDTPYKKTI
REQLDTRVEV MWTGTDTVPP RITVQDASRA AAVWGRKVFL WDNYPVNDYG QAEGRLLLAP
YSAREPGLHA QLSGLVLNPM NQAAASKVAL FGGADFAWND TSYDAQRAWR AAAAYLSNGN
PSTVEALLAF FDVEHLAPTF GASPWQPQAP QLAAKLGEFR TAWASGAKDS ALRALRPYAQ
LLTATPDRIS TGVTDPGFVA DCAPWLNALR LWGPAFEKTL DALTARLSTN EPEAQRLFTE
ASSLATRAGA IQTIPGETRP QGPVRVADGV LDTFLTEARS LR
//
