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Database: UniProt
Entry: I3VVI0_THESW
LinkDB: I3VVI0_THESW
Original site: I3VVI0_THESW 
ID   I3VVI0_THESW            Unreviewed;       256 AA.
AC   I3VVI0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:AFK86525.1};
GN   OrderedLocusNames=Tsac_1518 {ECO:0000313|EMBL:AFK86525.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86525.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK86525.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
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DR   EMBL; CP003184; AFK86525.1; -; Genomic_DNA.
DR   RefSeq; WP_014758396.1; NC_017992.1.
DR   AlphaFoldDB; I3VVI0; -.
DR   STRING; 1094508.Tsac_1518; -.
DR   KEGG; tsh:Tsac_1518; -.
DR   PATRIC; fig|1094508.3.peg.1539; -.
DR   eggNOG; COG0726; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-1541-MONOMER; -.
DR   Proteomes; UP000006178; 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; 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; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF80; POLYSACCHARIDE DEACETYLASE-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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..233
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   256 AA;  29816 MW;  5339F0AC77035950 CRC64;
     MKIYYIKKSV IINLLAVFVL AFISILYTNY GVPPVINTLF NINRQLPIYS VDIPDKRVAI
     SFDASWGSDK TERLLQILRD KNVKATFFLT GLWIDKYPDL VKKIYEEGHD VENHSNTHPH
     MTQLSDSEMV DEIKACEEKL VKITGRKPYL FRPPYGDYND KVIEIAKSLG YYTIQWDVDS
     LDWRGLDTEA IINRVLPNVK KGSIILFHNN GQFTPEAIPY IIDKLKENGY QIVPISQLIY
     KENYYIDHEG RQHKKQ
//
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