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Database: UniProt
Entry: A0A0A7FXZ8_9CLOT
LinkDB: A0A0A7FXZ8_9CLOT
Original site: A0A0A7FXZ8_9CLOT 
ID   A0A0A7FXZ8_9CLOT        Unreviewed;       335 AA.
AC   A0A0A7FXZ8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Polysaccharide deacetylase family protein {ECO:0000313|EMBL:AIY84487.1};
GN   ORFNames=U729_1562 {ECO:0000313|EMBL:AIY84487.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY84487.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY84487.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY84487.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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DR   EMBL; CP006905; AIY84487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7FXZ8; -.
DR   STRING; 1561.NPD11_1450; -.
DR   KEGG; cbv:U729_1562; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_6_2_9; -.
DR   Proteomes; UP000030635; 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   CDD; cd10944; CE4_SmPgdA_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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          130..332
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  37368 MW;  84540C37031C90A4 CRC64;
     MKNKKGKVHN YNMNVRRNFE RQQRGRRKKV VALVGLVIVL IIGGFGIYSA VSSNGENKEA
     TASQSSSSQK PGQAENNNNS VNTEASKLDN SGYIPLKDDK NADDAKVVAE RTSGLLKGKL
     HYPVRDDGKK VVYLTFDDGP STTNTPEVLD ILKKYDVKAT FFVMGKSLAD HPGAKELLKR
     EASEGHAIAN HSYSHNYQHL YPNRVININN FMEEYNKTNA LMKEILGKDF STRTVRFPGG
     YWSWNGRENA RPVLDKNGIE IVDWDALNGD AEGSGKSTPE QLVAKTKKTV EALGPNADSV
     VFLMHDTYGK ENTVKALPEI IEYFKSKGFE FRTMK
//
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