ID   A0A285CIJ1_9BACI        Unreviewed;       429 AA.
AC   A0A285CIJ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=SAMN05877753_101114 {ECO:0000313|EMBL:SNX66803.1};
OS   Bacillus oleivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1448271 {ECO:0000313|EMBL:SNX66803.1, ECO:0000313|Proteomes:UP000219546};
RN   [1] {ECO:0000313|EMBL:SNX66803.1, ECO:0000313|Proteomes:UP000219546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC228 {ECO:0000313|EMBL:SNX66803.1,
RC   ECO:0000313|Proteomes:UP000219546};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) 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; OAOP01000001; SNX66803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285CIJ1; -.
DR   OrthoDB; 9812065at2; -.
DR   Proteomes; UP000219546; 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; cd10917; CE4_NodB_like_6s_7s; 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   Reference proteome {ECO:0000313|Proteomes:UP000219546};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          251..426
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          207..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  49362 MW;  CA4C697486F44640 CRC64;
     MSVYSVKLLE LLSVEENGEK SFLQVRLLFQ SSNQFLWEID RDTAANIQKI VDFQGSFKYR
     MSFQTSWDNH RNQYLSFLTR TFRDQSDRIY FPCSEEFAKG LDTLRKMEQI SEIDTFPFLL
     REQTAHAEEE GVETELFSRP KSHRVSWMAA AMVAFLSISA FLLVYLKDSF RNDTPFSHPA
     IVEAKTIGEQ DYNGSLNEQT DIASLIKPEN KPSDTPISDV NESSSESLTA EEPSIPLIEV
     EERLTYSIPE GSVALTFDDG PSKYSKEIID ILKKYEVGGT FFFIGLHAKK YPEYVQYVHD
     NGYSIGSHTM NHTNMTNLSY EEQEKEMIQS IHLIEDIIQE EVVLFRPPYG AKNETTLELA
     ERTNHKLVLW NKDTEDWKHH NSEEIFQYVA NSDTSGAIIL LHESQAVIDA LPRIIEYLQQ
     QGLEVVGLR
//