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Database: UniProt
Entry: W0F0L2_9BACT
LinkDB: W0F0L2_9BACT
Original site: W0F0L2_9BACT 
ID   W0F0L2_9BACT            Unreviewed;       975 AA.
AC   W0F0L2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=NIASO_17980 {ECO:0000313|EMBL:AHF16547.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16547.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF16547.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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}.
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DR   EMBL; CP007035; AHF16547.1; -; Genomic_DNA.
DR   RefSeq; WP_008587834.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0F0L2; -.
DR   STRING; 929713.NIASO_17980; -.
DR   KEGG; nso:NIASO_17980; -.
DR   eggNOG; COG1472; Bacteria.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_012120_0_0_10; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000003586; 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; 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   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003586};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..975
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004788492"
FT   DOMAIN          44..357
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          590..952
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   975 AA;  108480 MW;  BD2AD7E44B97CBB2 CRC64;
     MKHCRLYIPL LALFLIPYLA TAQYKSNLSA KKWVDSVYKS LSKDQRIAQL IIVRAHSNLG
     PDHIAKVTDD VKKYNVGALC FFQGGPIRQA NLTNYYQSLA KTPLMITIDG EYGLGMRLDS
     VIKFPYQMTL GAMGDTSLVF EMGRAVGLQH KRLGVQVNYA PDVDINNNPN NPVIGFRSFG
     EDKYKVAAMG IAYMKGMQDA GIMACAKHFP GHGDVAVDSH LDLPVINKTL DQLQELELYP
     FKQLIKAGVQ SVMVGHLFVP SIDNTPHHAT SISKNAVTGL LKNTLGFNGL VFTDALEMKG
     VAKYFPGNTI AVESLIAGND MLCLPESVAG TISAVNDAIK KRRLRRKDIE AKVKKVLLAK
     YNLGLNQWQP VSIENLTNEL NSSTNSIRQK VAEKALTVVN LINPDGFRND FFSLPLKGKK
     IAYVAFTNNE KTVLANRLQS DLNADIYYIH YNDSPGKGGS VVKNIIEGKY DAVILGFHDV
     NLRKGANNYG ISQNALQNWQ VLNKENAVTM VFGNPLSLSN FCTAKSLVGA YEDDAIFQNT
     AADWLESKFV ATGTLPVSVC NWKYGTGMVL KNTATGGMRP IDDARFAPID SIAEAGIQQK
     AYPGCVVLAA KDGKIVFHKA FGNYEYDSTH PMQLNSIFDL ASVTKVSATT VSVMKLYEEG
     KIDLKKRLED YLPWTKKTNK AKLTLEDIIL HQAGMVPFIA FYKKTLNADG SVRSDLYRSV
     RSEGFTTQVA RNLYLRDDYK DTIWREILES PVIPPGQKYI YSDNDFWFLG KIVEAVTKMP
     LETYVQKTFY QPMHMTTTGF HPLERFPLEA IVPTEKETHF RNQLIQGTVH DEGSALGGGV
     AGHAGLFSDA YDLGKLYQML LNGGELNGHR FLKRETIQYF SAYHSSISRR GYGFDKPEKD
     NATSSDPYPS KYASPQAYGH TGFTGTCVWV DPKYNIVYIF LSNRVYPTRE NPRLSSLSIR
     RSILDAIYKA VVPNL
//
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