ID E6STS1_BACT6 Unreviewed; 1000 AA.
AC E6STS1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=Bache_0244 {ECO:0000313|EMBL:ADV42274.1};
OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS 15421 / P 36-108).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV42274.1, ECO:0000313|Proteomes:UP000008630};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P 36-108;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacteroides helcogenes P 36-108.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADV42274.1, ECO:0000313|Proteomes:UP000008630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108
RC {ECO:0000313|Proteomes:UP000008630};
RX PubMed=21475586; DOI=10.4056/sigs.1513795;
RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT 108).";
RL Stand. Genomic Sci. 4:45-53(2011).
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; CP002352; ADV42274.1; -; Genomic_DNA.
DR RefSeq; WP_013545891.1; NC_014933.1.
DR AlphaFoldDB; E6STS1; -.
DR STRING; 693979.Bache_0244; -.
DR KEGG; bhl:Bache_0244; -.
DR PATRIC; fig|693979.3.peg.263; -.
DR eggNOG; COG1472; Bacteria.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_012120_0_0_10; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000008630; 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; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; 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 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:ADV42274.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008630};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1000
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003209401"
FT DOMAIN 61..373
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 600..973
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 1000 AA; 111170 MW; 4B18FEC2FDE9BD2F CRC64;
MKRIFLFASI LLFCCGHMAL DARHIPVPPA PVPAAEPSLV HALQDDARCR QWVDSVLKRL
TLEERIGQLF IYTIAPHPNK ATRKLLRTVV EDYKVGGLLF SGGLMSNQAV LTNEAQRMAN
VPLMITFDGE WGLSMRLRGT PGFPRNMVLG CIRNDSLIYE YGREMARQCH ELGIQVNFAP
VADVNINPQN PVINTRSFGE NPVNVAKKVI AYSKGLEDGG VLSVCKHFPG HGDTDVDSHK
ALPTLPFTRE RLDSVELYPF KEAIRAGLGG IMVGHLEVPV FEVHGGLPSS LSRSVVYDLL
TRELKFQGLI FTDALAMKGV SDNSTVCLQA LKAGNDLLLV PRRIKEEVEA ILDAVKRREL
KESDIEEKCR KVLMYKYALG LTRKPFIHIS GLGTRINTPR TRELIQRLNL AAITVLGNQD
KVLPLDPAIK EVAVLNVGDS REIRPFMKEL SQFTCPAEFQ LEKNPGEQSC RYLQDTLAQY
KRVLVCITEH RLAPYQTFFA TFAPDVPVTY LCFIPGKQTL QIHRGISAGK AMVLAHSSDD
DVQRQVAKIL YGKAVADGRL SADIGGLFAA GTGVTLGPNS TPHFIPEEYG MNSRILAQID
GIVEEGLRAG AYADCAVAVL KDGREMYNKA FGTHTGDVYD LASLTKTTAT LLAVMKLYDK
GRLSLTDRVS DYLPFLQDTD KKNITVRELL LHESGLPSTL LFYQDAIDKG SYSGSLFKGK
ADKAHPVRVG SQTWGNSKFR FRKGLTSNLR TAECTLQVSD SLWLNRSFKH EYLRKIAETP
LKDKRYRYSC VGFIVLQQLV EARAGMPMDE FLAKEFYIPM GLKRTGFLPL RFLKKEDIIP
SSIDSFLRKT TLQGFVHDEA AAFQGGVSGN AGLFSTAGEV SRIYQMILND GELDGKRYLS
KETCKLFTTT VSRISRRGLG FDKPDARNPQ KSPCAISAPA SVYGHTGFTG TCAWVDPDNG
LVYVFLSNRI YPNVWNNKLM SLDIRKRIQE TIYKAMESGK
//
