ID Q180A0_CLOD6 Unreviewed; 275 AA.
AC Q180A0;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:CAJ70154.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:CAJ70154.1};
GN OrderedLocusNames=CD630_32570 {ECO:0000313|EMBL:CAJ70154.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ70154.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ70154.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ70154.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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DR EMBL; AM180355; CAJ70154.1; -; Genomic_DNA.
DR RefSeq; WP_003432345.1; NZ_JAUPES010000002.1.
DR RefSeq; YP_001089773.1; NC_009089.1.
DR AlphaFoldDB; Q180A0; -.
DR STRING; 272563.CD630_32570; -.
DR EnsemblBacteria; CAJ70154; CAJ70154; CD630_32570.
DR GeneID; 66355676; -.
DR KEGG; cdf:CD630_32570; -.
DR KEGG; pdc:CDIF630_03555; -.
DR PATRIC; fig|272563.120.peg.3441; -.
DR eggNOG; COG0726; Bacteria.
DR OrthoDB; 258610at2; -.
DR PhylomeDB; Q180A0; -.
DR BioCyc; PDIF272563:G12WB-3425-MONOMER; -.
DR PHI-base; PHI:10937; -.
DR Proteomes; UP000001978; Chromosome.
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 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; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10587:SF125; POLYSACCHARIDE DEACETYLASE YHEN-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:CAJ70154.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001978};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..259
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 275 AA; 31542 MW; EC322E3576FE0DE4 CRC64;
MKIKDNKAVF HVFIRIFLIA VLILTGTLLE EKINNVPVEN ISSKGENTLE LLSQSNTLGE
IIYKASQEET KGPGATSEKV AYITIDDGPS KYTNALLDIL KENDVKATFF MLNQNMKNHK
EEVRRVLEEE NSIGFHSVSH DIHKLYKSPE VTVGEFNTCN NTLQEITGQS SKLIRLPYGS
KPYMPEGSYN KLMANDYLIW DWNLDTQDWK SSTSQIVSNI LYYGRKRDEL VVLIHEKEQS
LNALNNIIRI LKERGYTILP ITENITPKNF WQENL
//
