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Database: UniProt
Entry: A0A0V8HNZ6_9BACI
LinkDB: A0A0V8HNZ6_9BACI
Original site: A0A0V8HNZ6_9BACI 
ID   A0A0V8HNZ6_9BACI        Unreviewed;       233 AA.
AC   A0A0V8HNZ6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=GA0061094_0049 {ECO:0000313|EMBL:SCB72253.1};
OS   [Bacillus] enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCB72253.1, ECO:0000313|Proteomes:UP000181997};
RN   [1] {ECO:0000313|EMBL:SCB72253.1, ECO:0000313|Proteomes:UP000181997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-1123 {ECO:0000313|EMBL:SCB72253.1,
RC   ECO:0000313|Proteomes:UP000181997};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; FMAU01000001; SCB72253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V8HNZ6; -.
DR   Proteomes; UP000181997; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd10959; CE4_NodB_like_3; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
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; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..226
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   233 AA;  27048 MW;  D89742ACA7007040 CRC64;
     MSGLFILIFI IVTFFIYSII STIVIRKMDI KIIRRVPQER TIALTFDDGP HPLHTSALLE
     ILKRHGVKAT FFVVGENAEQ NPGLIKRMVD EGHSLGLHHY RHISSWFLTP WGLKKQLERT
     NEVLKRITGE GTYLYRPPWG HLNFSSLMFA NRYRIIIWSH IFKDWKVKEC KEHLSRRLNH
     SDSEGAVFVL HDNGATLGAD EDAPKYMVEC VDAFIKDALE RDIRFISLDE AFQ
//
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