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Database: UniProt
Entry: A0A0W0V839_9GAMM
LinkDB: A0A0W0V839_9GAMM
Original site: A0A0W0V839_9GAMM 
ID   A0A0W0V839_9GAMM        Unreviewed;       350 AA.
AC   A0A0W0V839;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=Ljor_0617 {ECO:0000313|EMBL:KTD16311.1};
OS   Legionella jordanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=456 {ECO:0000313|EMBL:KTD16311.1, ECO:0000313|Proteomes:UP000055035};
RN   [1] {ECO:0000313|EMBL:KTD16311.1, ECO:0000313|Proteomes:UP000055035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-540 {ECO:0000313|EMBL:KTD16311.1,
RC   ECO:0000313|Proteomes:UP000055035};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KTD16311.1}.
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DR   EMBL; LNYJ01000011; KTD16311.1; -; Genomic_DNA.
DR   RefSeq; WP_058470174.1; NZ_RDQP01000002.1.
DR   AlphaFoldDB; A0A0W0V839; -.
DR   STRING; 456.Ljor_0617; -.
DR   PATRIC; fig|456.5.peg.652; -.
DR   OrthoDB; 9786661at2; -.
DR   Proteomes; UP000055035; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTD16311.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055035}.
FT   DOMAIN          4..342
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   350 AA;  38619 MW;  1EC90882BE447041 CRC64;
     MAELRQQIAQ MLVMGFAGTS IDEVHPVRKW ISQEQIGAVI LFDYDMQNRC QGKNLINKEQ
     IQQLTEQLQQ ALPDHAKLPL FIAIDYEGGS IDRLKYVPDC PKTLTPSELA ALDETEFQTH
     VGGMASTVKS LGFNLNFAPV VDLDLNKEQG IIGKLGRSFS ANPDEVASLA ASFVSNFAEH
     KLICCYKHFP GHGSAPGDTH EDFVDVTDSF QPSELQPYQQ LAKRHDLPAM IMTAHVINRN
     LDPSGLPATL SKKMLTGLLR EEFGFEGVIV SDDLQMHAIA KHYSLEKSLE LTINAGADML
     IFGNQLGQIT APEVIDKIEQ LVLSGVISSA RIAESYERIL KLKHVLGTSH
//
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