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Database: UniProt
Entry: B1ID42_CLOBK
LinkDB: B1ID42_CLOBK
Original site: B1ID42_CLOBK 
ID   B1ID42_CLOBK            Unreviewed;       289 AA.
AC   B1ID42;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Polysaccharide deacetylase family protein {ECO:0000313|EMBL:ACA45967.1};
GN   OrderedLocusNames=CLD_0718 {ECO:0000313|EMBL:ACA45967.1};
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA45967.1, ECO:0000313|Proteomes:UP000008541};
RN   [1] {ECO:0000313|EMBL:ACA45967.1, ECO:0000313|Proteomes:UP000008541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; CP000939; ACA45967.1; -; Genomic_DNA.
DR   RefSeq; WP_003404883.1; NC_010516.1.
DR   AlphaFoldDB; B1ID42; -.
DR   KEGG; cbb:CLD_0718; -.
DR   HOGENOM; CLU_030024_2_0_9; -.
DR   Proteomes; UP000008541; 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; cd10918; CE4_NodB_like_5s_6s; 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; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 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   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..289
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039111686"
FT   DOMAIN          124..289
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   289 AA;  33512 MW;  65CB3F2E78EC832C CRC64;
     MKNKKSLIFF AFIMMIAVLF SGCKKNNNVD DNNINEKKAQ SKKQESNVKN TDVRSFTKEP
     LIYNNKSVPV LMYHSIDYEK GNELRVPKEQ FKEQMKYLKD NGYTTLTLNE LYNFLEKNKP
     IPEKSIVITL DDGYVDNYTN AYPILKELGF NATVFVITSN IDKDKRTLTS KQIKEMDEAG
     IQIASHTYNH DKLDDLSYEK QLQTMKKSKD DLEKILNHKV DFIAYPYGKW NEESIKAAKD
     SGYKMAFTTQ GGWSNKQNGI YTLNRVYISS LKGIDNFKDR ITNPNYNKS
//
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