ID A0A1T5P8U6_9BACT Unreviewed; 764 AA.
AC A0A1T5P8U6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=SAMN05660461_5053 {ECO:0000313|EMBL:SKD09170.1};
OS Chitinophaga ginsengisegetis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD09170.1, ECO:0000313|Proteomes:UP000190166};
RN [1] {ECO:0000313|EMBL:SKD09170.1, ECO:0000313|Proteomes:UP000190166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD09170.1,
RC ECO:0000313|Proteomes:UP000190166};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; FUZZ01000004; SKD09170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5P8U6; -.
DR STRING; 393003.SAMN05660461_5053; -.
DR Proteomes; UP000190166; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR026876; Fn3_assoc_repeat.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF13287; Fn3_assoc; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..764
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012369041"
FT DOMAIN 622..759
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT ACT_SITE 346
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 764 AA; 85288 MW; 22517636476AE42E CRC64;
MKKIFLLAGA LCLLMQATFA QSERYPLIPY PQQLEARTGS FVITPATRLV LPANRTAFTT
ETAQLQSLLT QALGKPLRVT KKAVKGAIVL QQNTALAGAE DYTMDVTAQQ LLITAGTPAG
FFRAIQTLRQ LMPAAVETAP ALKSIAIPAM LLKDHPAYGW RGMHLDVSRH FFSVDYLKKF
IDLLALYKMN KLHLHLTDDQ GWRIEIKKYP LLTSQGAWRE FNNQDSVCMK MAVSNPDMAI
DTQHIIHKDG KTLYGGFYTQ EQMKGIIRYA ADRQVEIIPE IDMPGHMMAA IRAYPFLACS
GEIGWGKTFS TPICPCNEST FAFAEDVFTE IAALFPSKYI HLGADEVEKT SWAASPLCAE
VMKANNLKTV EELQSYFVKR MEKFFHSKGK VLIGWDEILE GGISPTAVLM YWRAWVPDAP
VKAARHGNAV IMTPGNPLYF DAVPDRNSIY NVYHFQPVPK GLTADEAKHI MGAQANIWTE
YIPSEKRADY MFMPRMTALA EVLWTNRNNY DSYLLRLNEQ YKRLDLLGVH YRLPDLDGFT
EDNVFVDQVT LEVKKPLTDM AIRYTTDGTI PGEQAAVLPD NYVIREPQTI KLAAFSPAGN
RGDIYTLRYR KEAYRKATVV KDARQGLKLD YFEGAYKSAT KIKEQADSSI RVNNVIIPEG
MGKGGGPFGA RVYGYINVPA TGIYSFYLTA DDGAILYIDD QEVVNNDGWH APLQKSGQVA
LEKGWHPIKA AFVEGGGGYT LKLEYSVNGS KLQPVPDSWL GAGL
//