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Database: UniProt
Entry: E7GNU3_CLOSY
LinkDB: E7GNU3_CLOSY
Original site: E7GNU3_CLOSY 
ID   E7GNU3_CLOSY            Unreviewed;       439 AA.
AC   E7GNU3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=HMPREF9474_02588 {ECO:0000313|EMBL:EGA93491.1};
OS   [Clostridium] symbiosum WAL-14163.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA93491.1, ECO:0000313|Proteomes:UP000002970};
RN   [1] {ECO:0000313|EMBL:EGA93491.1, ECO:0000313|Proteomes:UP000002970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA93491.1,
RC   ECO:0000313|Proteomes:UP000002970};
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL   Submitted (DEC-2010) 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:EGA93491.1}.
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DR   EMBL; ADLQ01000056; EGA93491.1; -; Genomic_DNA.
DR   RefSeq; WP_003501173.1; NZ_GL834311.1.
DR   AlphaFoldDB; E7GNU3; -.
DR   STRING; 1512.GCA_900049235_02787; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_2_9; -.
DR   Proteomes; UP000002970; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:EGA93491.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002970};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..436
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          68..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  47630 MW;  F4B8EE636B000F53 CRC64;
     MEERQRGQSR RNPKSRRRQR GPAAGWLVLL LVAAAAAAVS VFFLRHLKVQ EEERAKTRDS
     SEAVVAEYFP GDDRNEAAKD SAASEEELEG KTPMTVEEAL QEMTLREKVL QLFMVTPEAL
     TGVDEVYAAG AKTEESIREY PVGGIVYFKQ NLRSPDQVKD MLTRTQKYFR DNTGIEAFLA
     VDEEGGQVSR ISGREEFGIA SFPDMSEIGA SGEPQKAYEV GDKIGTYLAD LGFNMDFAPV
     ADVLTNPENT VVARRSFGTD GAVTAAFSNE VVKGLQAHGI SAVLKHFPGH GGTTADSHDG
     YAATERTLEE LMAEDFVPFL EGGRAGARFI MSGHIAAPAV TGDNTPASMS PKMITEILRG
     TLGYDGIIIT DALNMGAVTS SYSSADAAVR ALQAGNDMLL MPENFQEAYQ GVLTAVENGT
     LSEERINQSV ERILKVKFH
//
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