ID A0A098F3I2_9BACI Unreviewed; 732 AA.
AC A0A098F3I2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=O-GlcNAcase NagJ {ECO:0000313|EMBL:CEG28716.1};
GN Name=nagJ_2 {ECO:0000313|EMBL:CEG28716.1};
GN ORFNames=BN1002_03639 {ECO:0000313|EMBL:CEG28716.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG28716.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG28716.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG28716.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCXR01000001; CEG28716.1; -; Genomic_DNA.
DR RefSeq; WP_048826785.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098F3I2; -.
DR STRING; 1476857.BN1002_03639; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000042335; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR049019; NagJ-like_helical.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR Pfam; PF21774; NagJ_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039009584"
FT DOMAIN 40..185
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 191..496
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT DOMAIN 511..624
FT /note="NagJ-like helical"
FT /evidence="ECO:0000259|Pfam:PF21774"
SQ SEQUENCE 732 AA; 82503 MW; AFBC61AAD956A8F5 CRC64;
MKKRYPLWKK ALVLSASLLL SVPSLQGINK ASAASPAIQS INPKPQEVKV TGNGFPLTPK
VGIVIGENTD EEAIKEVVQA LEKAEVKQVI RYNDKEKATT PVTVWIGGPS ENEAVLDVLK
QMEVDSPEAL EREGYVLASS SKGKKQIVLA GKDQTGTYYA AKSFSQLIQE QEGNDWFPQA
EIRDWPEMPI RGSIEGFYGP PWTHEDRLNQ LEFYGDNKLN TYIYAPKDDP YHRENWREPY
PEEELARIKE LIDKAKENHV KFTFSLSPGQ SICYSGDEDF ELLMNKMDAV WDLGVRSYAI
FLDDINKDLY CEQDKERFSG DEDPIAAAHA YLLNRFTKEF IDTHEGAERL ITVPTDYAGN
QSNTYRERFA DLLNEDAIVM WTGPDVVSKE ITAEGTQKVH EIFKHDLLLW DNYPVNDFER
NRLFLGPLEH RDASLTEHGL VGLTANPMNE AEASKIPLFT IADYSWNPSA YNPVDSWERS
IQSFGGKAAD ALKTFAENSY SSTLSDRDSL TLTPLIEEFW KAYGTEAMDQ AANKLIAEFE
KLQTAPERLR QNLDNQKFLD ETEPYLDKVE LYGEAGQLAV KALVAEKSNN LEEAQQYREK
LKSMLITIDS IPQKIGEKAL RPFLVQGIWG QHVKSRALDG INKGRGADQL ILYTPERGET
TRTNPYGYEV TVENGVVVKR GGNNSAIPTN GYVLSIHNSN WMERNWLDLN AEIGAKVLIE
NGQVLITPPA AQ
//
