ID   A0A1W6E0P9_9BACT        Unreviewed;      1008 AA.
AC   A0A1W6E0P9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=A6C57_00840 {ECO:0000313|EMBL:ARK08971.1};
OS   Fibrella sp. ES10-3-2-2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK08971.1, ECO:0000313|Proteomes:UP000193660};
RN   [1] {ECO:0000313|Proteomes:UP000193660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA   Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL   Submitted (APR-2016) 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, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP015317; ARK08971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6E0P9; -.
DR   STRING; 1834519.A6C57_00840; -.
DR   KEGG; fib:A6C57_00840; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000193660; Chromosome.
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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
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; PF00144; Beta-lactamase; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193660};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1008
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012032001"
FT   DOMAIN          63..379
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          422..581
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          616..980
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   1008 AA;  111891 MW;  C3027CDE49BF6F04 CRC64;
     MTSSRQTLLS LLFLLTVSVQ LLAQTATAPV RKPLSMPVTV PTFLRNTERS TRWADSVMAD
     MPLEQQVAQL IMVAGYSNRT RTYEDSLTDL VRTWKLGGVV FFQGGPMRQA KLSNRLQAAS
     QVPLLVAMDA EWGIAMRLDS TIRYPYQMTL GGMPKASEGL IYQMGADLAR QARRLGMHVN
     FAPVADVNNN PNNPVINFRS FGEDKYAVTR KALAYLRGMQ DNRLLTSIKH FPGHGDTGTD
     SHYDLPLIVK SREQLDSLEL YPFKELIKAG AAGVMVAHLS IPSLDTTRNR PSTLSPNIVT
     GLLKNELGFG GLIFSDAMNM KGMTKFFPSG LADRRGLEAG MDILEFTENI PRAVSEICKA
     VDERTLSTQT IAERCRKMLI AKYWAGLNNY RPIVLDGLLA DLNRPESEVL NRRLTEASLT
     VVTNKRAVLP LQHLDTLRIA SVSVEAVAPT VFQSRLGDYT SVTPYVISSK STDAQIATLL
     DSLNQFNLIL VGVHLNNIRP GANYGMQART AELVQKLTNT GKAVVSVFGN PYVLDRFPDI
     DKAQAIVMPY QLTNHTEDLS AQLIFGAIGA AGRLPVTVNQ TYRLGDGVTI QPIGRLKYTI
     PEEVGISSAY LAQQVDSVVN VGLQAKAFPG CVVQLAKDGK VIFRKAYGKH TYDTSLGGDA
     QPTKLDDLFD FASVTKISTS TPALMRLVDA GKFNIDGTMG EYLPGYKKSN KDTLRWRDVL
     THQSKLKAWI PFWQSTKNPD GTFKKNTFST ERSNKFPVEV TDSLFLHRKY AKTVFAQIKD
     SPLNAKKEYV YSDLSFYLYP QIVQRITGVP FETYLKDSLY RPLGATTLTY NPRRFYPLSR
     IVPTEYDSLF RKTLIWGRVH DEGAAMLGGL SGHAGLFGTA NDLMKLTQLY LQHGSFGGQQ
     FISSETITEF TRYQFPELGN RRGLGFEKAA YKYNGNAPRL ASPSSYGHSG YTGTFTWIDP
     AVGLNYVFLC NRVYPTRNNN KVTELGIRTG VADAFYRAIQ KGNPSRNL
//