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Database: UniProt
Entry: Q891W2_CLOTE
LinkDB: Q891W2_CLOTE
Original site: Q891W2_CLOTE 
ID   Q891W2_CLOTE            Unreviewed;       310 AA.
AC   Q891W2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Chitooligosaccharide deacetylase {ECO:0000313|EMBL:AAO36733.1};
DE            EC=3.5.1.- {ECO:0000313|EMBL:AAO36733.1};
GN   OrderedLocusNames=CTC_02251 {ECO:0000313|EMBL:AAO36733.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36733.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO36733.1, ECO:0000313|Proteomes:UP000001412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA   Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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DR   EMBL; AE015927; AAO36733.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q891W2; -.
DR   STRING; 212717.CTC_02251; -.
DR   KEGG; ctc:CTC_02251; -.
DR   HOGENOM; CLU_021264_12_0_9; -.
DR   OrthoDB; 9812065at2; -.
DR   Proteomes; UP000001412; Chromosome.
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; cd10948; CE4_BsPdaA_like; 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   InterPro; IPR014235; Spore_PdaA.
DR   NCBIfam; TIGR02884; spore_pdaA; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF78; PEPTIDOGLYCAN-N-ACETYLMURAMIC ACID DEACETYLASE PDAA; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AAO36733.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT   DOMAIN          120..304
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          42..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  35490 MW;  43612E7B6721B6BB CRC64;
     MKKAISLLII FSFISLSTTS CSPKYSNNDK IKVETPINKK YNEDIKKKDE TKSLNDNEKI
     DDESKKDNSK NTSSKSSLET KERDWFFEPK KDGSPSTVPN DVENVIKNHS TYFLGDTSEK
     VIYLTFDEGY ENGYTSKILD VLKANDVKAA FFVVTPYIKT NKDLIKRMVD EGHLVCNHSV
     HHPSMAQVAL KGKEKFKEEF TGVEEIFKEV TGKEMPKFFR PPMGKYSELS LAYTKELGYK
     TIFWSFAYND WNVDKQPNPE AAKKRIVDKA HNGAIYLLHA VSKTNTEVLD SVIKELKDKG
     FRFASLEELK
//
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