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Database: UniProt
Entry: A0A2T0MCW4_9FLAO
LinkDB: A0A2T0MCW4_9FLAO
Original site: A0A2T0MCW4_9FLAO 
ID   A0A2T0MCW4_9FLAO        Unreviewed;       969 AA.
AC   A0A2T0MCW4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=CLV81_3722 {ECO:0000313|EMBL:PRX55313.1};
OS   Allomuricauda pacifica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1080225 {ECO:0000313|EMBL:PRX55313.1, ECO:0000313|Proteomes:UP000237640};
RN   [1] {ECO:0000313|EMBL:PRX55313.1, ECO:0000313|Proteomes:UP000237640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25027 {ECO:0000313|EMBL:PRX55313.1,
RC   ECO:0000313|Proteomes:UP000237640};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PRX55313.1}.
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DR   EMBL; PVYX01000002; PRX55313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0MCW4; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000237640; 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; 3.40.710.10; 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, ECO:0000313|EMBL:PRX55313.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237640};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..969
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015641639"
FT   DOMAIN          43..358
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          590..946
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   969 AA;  108860 MW;  44E312A20C171BE3 CRC64;
     MRINVYFPLL LLFFLGAKAQ NPLVAKDTLA QMEWVDNTYN NLTLEEKIGQ LFMVSIGSNK
     SVESTNRIQS LIENQHVGGV IFLKGGPVQQ VRLTNEFQSK SKIPLMIGMD AEWGLAMRLD
     STYAFPWNMT LGAIQDDKIV EKVGFQIGKH AKRMGVHINF APDIDVNNNP RNPIIGNRSF
     GESPENVANK GLAIMKGMQK AGILACGKHF PGHGDTDVDS HKALPIIDAD RQRLDSIELY
     PFKYLIKNGL SSVMVAHLDV PCLESRDGHP SSLSKSIISD LLIKELGFEG LVFTDALNMK
     AVSQFANEGE VELESFLAGT DVLLMPQNPM ESIKRFIDAY NTGRISEYRL SLSVKKILMA
     KYKAGLHTYV PVAEENLLNE LNGVENDIIY EESIEKALTV AKNNFSLLPI KNLENKRIAY
     VQFGDADGSP FYDILSKYTK VTWVKEKNIA DYRKELAEYN LVIIGFHKNN DSPWKSYKFS
     DTELFWLQEI SKLRTSNTIL SIFAKPYALL DVVNSTTIDA LLIGYQNSEL AQKKAAQAIF
     GAIGANGKLP VSVGSTFQEG TGLEVKPIQR LGYSIPEKVG MSSKNLKAVD SLVQIGLDSL
     MFPGAQILIA KKGKVIYNKN FGKPTYGSDG KVNKDHIYDL ASLTKILSTL PMIMKMEEEG
     NIALNDTFKE LVPEYEDSEL KDVTVLKALS HYGRLPAWIA FYIDTLSEDR KPSPDFYRNH
     PAEGFPFKVA DNLYLTSAYK DSIYNRIGRQ DLKSNRYRYS DVGYYVFKKY IEEFYGSSID
     ELVDRFFYRP MGLQYTGFNP LGKFKKNQII PTEEDTYFRY QTIQGYVHDM GAAMQGGVGG
     HAGLFSNAND VAKIMQMYLQ GGVYGGRRFL NDRTIQKFNT CYFCHKMVRR GVGFDKPQLE
     EKGPTCGCVS RKSFGHSGFT GTYTWADPDE ELIYVFLSNR TFPTASNTLL IKSGLRTRIQ
     QAIYDSIIN
//
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