ID   A0A0C1R7J7_9CLOT        Unreviewed;       487 AA.
AC   A0A0C1R7J7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   Name=pdaB {ECO:0000313|EMBL:KIE46486.1};
GN   ORFNames=U732_1790 {ECO:0000313|EMBL:KIE46486.1};
OS   Clostridium argentinense CDC 2741.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46486.1, ECO:0000313|Proteomes:UP000031366};
RN   [1] {ECO:0000313|EMBL:KIE46486.1, ECO:0000313|Proteomes:UP000031366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46486.1,
RC   ECO:0000313|Proteomes:UP000031366};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC         glucosamine + acetate.; EC=3.5.1.104;
CC         Evidence={ECO:0000256|ARBA:ARBA00043715};
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:KIE46486.1}.
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DR   EMBL; AYSO01000017; KIE46486.1; -; Genomic_DNA.
DR   RefSeq; WP_052268129.1; NZ_AYSO01000017.1.
DR   AlphaFoldDB; A0A0C1R7J7; -.
DR   STRING; 29341.RSJ17_16565; -.
DR   OrthoDB; 9806342at2; -.
DR   Proteomes; UP000031366; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10917; CE4_NodB_like_6s_7s; 2.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 2.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 2.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 2.
DR   PROSITE; PS51677; NODB; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT   DOMAIN          73..252
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   DOMAIN          298..479
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   487 AA;  54614 MW;  E3188A3C526BE058 CRC64;
     MEDIKGKKNK VKLVTLSAII ILFLAYLAGC GIDLWKKDSK EKDAPPKIEA NEDIPKYDGE
     KSKAISYVYT TKRELTLTFS GMGDENMMKQ LLDELDKFQI KAVFFLPGMR VAEEPEIAKD
     ILKRGHEIEN NTLNRVDLTE LSYQNIYKEI QKTNEIIKKE TGVSPKYLRT KSGSYNDDVC
     LAAAQSGLEA IITYSVNPKD WDMKSAKEIG DYIAKYITRG GIIALNADKN PAVIQSIPLI
     AKAVDDVGYK LVPLGKLIEG SYERKPLQSI KGYDAAKINE KIVESQYDIV YKVNTDKKEI
     ALTFDDWGRD ITITKILDIL DKYNIKASFF LRGNGVEKNP NLAKAIAEAG HDVANHTYSH
     PVITNITPEK LQYEVVKCHQ VLTEAIQQQP KMFFRPPTGE INEATAKIIA DCGYKTISLF
     DVSPHDWDVK NSAEDIVNFI LENTGKGSVI LLHLQDEIST VEALPVIIEN LKSMGYSFAT
     ISELMNK
//