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Database: UniProt
Entry: A0A1F1ZK18_9CORY
LinkDB: A0A1F1ZK18_9CORY
Original site: A0A1F1ZK18_9CORY 
ID   A0A1F1ZK18_9CORY        Unreviewed;       452 AA.
AC   A0A1F1ZK18;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=HMPREF3098_09575 {ECO:0000313|EMBL:OFT87580.1};
OS   Corynebacterium sp. HMSC28B08.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1581066 {ECO:0000313|EMBL:OFT87580.1, ECO:0000313|Proteomes:UP000177449};
RN   [1] {ECO:0000313|EMBL:OFT87580.1, ECO:0000313|Proteomes:UP000177449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC28B08 {ECO:0000313|EMBL:OFT87580.1,
RC   ECO:0000313|Proteomes:UP000177449};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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:OFT87580.1}.
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DR   EMBL; LWOT01000069; OFT87580.1; -; Genomic_DNA.
DR   RefSeq; WP_070434971.1; NZ_KV786180.1.
DR   AlphaFoldDB; A0A1F1ZK18; -.
DR   STRING; 1581066.HMPREF3098_09575; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000177449; 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; 3.20.20.300; 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:SF15; BETA-HEXOSAMINIDASE LPQI; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..452
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038881625"
FT   DOMAIN          133..291
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          344..448
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          22..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  45993 MW;  E9EB061B3810FC1A CRC64;
     MRRILVVVSA SALLLAGCST DSGPTPPAAD SAQNRPSSST LADSSTVSAP ADKNSGDAGD
     ANRAGRPAGM KCESLRDATD RQLAGRLMAV GITDFASAQQ AVDAGVRHLF VGTGSDYSIL
     NGQGDPARSI AALERRAGEK LTISVDEEGG EVQRLSGIIG KLPSPREMAD TMTPQQVRAM
     MAEHGRKLRA LGVTVDFAPV LDLGGAQDIS ANGIGSRAFS ADPRVVATYG RAYAEGLRDA
     GIVPVFKHFP GHGHVKGDSH LGTVVSPPLS VMENQDLLPF RQLATMGTES VGGRPAPEGA
     SAPGRAGQPG PGRAGQPVPS SAGDSSREAA GQSRPAEPVR PAPAMMIGHM QVPGLGDKKP
     ASINPAAYKL LRSYKFNGLI VTDDLTGMKA VSDQLSGPDA VVAAVSAGAD QALAAAGGID
     VPAAVEALAQ AISSGKIPRD RAIASADRGC VL
//
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