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Database: UniProt
Entry: A0A2T0B6L1_9CLOT
LinkDB: A0A2T0B6L1_9CLOT
Original site: A0A2T0B6L1_9CLOT 
ID   A0A2T0B6L1_9CLOT        Unreviewed;       238 AA.
AC   A0A2T0B6L1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   Name=pdaA_2 {ECO:0000313|EMBL:PRR79505.1};
GN   ORFNames=CLVI_33500 {ECO:0000313|EMBL:PRR79505.1};
OS   Clostridium vincentii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR79505.1, ECO:0000313|Proteomes:UP000239471};
RN   [1] {ECO:0000313|EMBL:PRR79505.1, ECO:0000313|Proteomes:UP000239471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR79505.1,
RC   ECO:0000313|Proteomes:UP000239471};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium vincentii DSM 10228.";
RL   Submitted (MAR-2018) 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};
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:PRR79505.1}.
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DR   EMBL; PVXQ01000064; PRR79505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0B6L1; -.
DR   OrthoDB; 9806342at2; -.
DR   Proteomes; UP000239471; 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   Hydrolase {ECO:0000313|EMBL:PRR79505.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239471};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..238
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   238 AA;  26988 MW;  6C9F448D7382E5AB CRC64;
     MKKFIVFIVT SIMLSGIICV FINIKEREVM SNKENEVNID GTVKDLNEES VEIKKFNVGE
     ILFNISVIDK ESIEKITKLK VIKQKDTVYL NDQPESNSVY LTFDDGPDGE VTPRILDILE
     SYNVKGNFFF LGENAKMYPE VVKRTFDSGN FIGNHTYYHE DLTTLSPEGI KDELEKTEEV
     ISSITGKRTT AMRPPYGASN ETVIKVIKDS NSVSILWSID TLDWSHKEVS SILKVSVK
//
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